anno_start	anno_end	anno_text	entity_type	sentence	section
0	17	Crystal Structure	evidence	Crystal Structure of the SPOC Domain of the Arabidopsis Flowering Regulator FPA	TITLE
25	29	SPOC	structure_element	Crystal Structure of the SPOC Domain of the Arabidopsis Flowering Regulator FPA	TITLE
44	55	Arabidopsis	taxonomy_domain	Crystal Structure of the SPOC Domain of the Arabidopsis Flowering Regulator FPA	TITLE
56	75	Flowering Regulator	protein_type	Crystal Structure of the SPOC Domain of the Arabidopsis Flowering Regulator FPA	TITLE
76	79	FPA	protein	Crystal Structure of the SPOC Domain of the Arabidopsis Flowering Regulator FPA	TITLE
4	15	Arabidopsis	taxonomy_domain	The Arabidopsis protein FPA controls flowering time by regulating the alternative 3′-end processing of the FLOWERING LOCUS (FLC) antisense RNA.	ABSTRACT
24	27	FPA	protein	The Arabidopsis protein FPA controls flowering time by regulating the alternative 3′-end processing of the FLOWERING LOCUS (FLC) antisense RNA.	ABSTRACT
107	122	FLOWERING LOCUS	gene	The Arabidopsis protein FPA controls flowering time by regulating the alternative 3′-end processing of the FLOWERING LOCUS (FLC) antisense RNA.	ABSTRACT
124	127	FLC	gene	The Arabidopsis protein FPA controls flowering time by regulating the alternative 3′-end processing of the FLOWERING LOCUS (FLC) antisense RNA.	ABSTRACT
129	142	antisense RNA	chemical	The Arabidopsis protein FPA controls flowering time by regulating the alternative 3′-end processing of the FLOWERING LOCUS (FLC) antisense RNA.	ABSTRACT
0	3	FPA	protein	FPA belongs to the split ends (SPEN) family of proteins, which contain N-terminal RNA recognition motifs (RRMs) and a SPEN paralog and ortholog C-terminal (SPOC) domain.	ABSTRACT
19	29	split ends	protein_type	FPA belongs to the split ends (SPEN) family of proteins, which contain N-terminal RNA recognition motifs (RRMs) and a SPEN paralog and ortholog C-terminal (SPOC) domain.	ABSTRACT
31	35	SPEN	protein_type	FPA belongs to the split ends (SPEN) family of proteins, which contain N-terminal RNA recognition motifs (RRMs) and a SPEN paralog and ortholog C-terminal (SPOC) domain.	ABSTRACT
82	104	RNA recognition motifs	structure_element	FPA belongs to the split ends (SPEN) family of proteins, which contain N-terminal RNA recognition motifs (RRMs) and a SPEN paralog and ortholog C-terminal (SPOC) domain.	ABSTRACT
106	110	RRMs	structure_element	FPA belongs to the split ends (SPEN) family of proteins, which contain N-terminal RNA recognition motifs (RRMs) and a SPEN paralog and ortholog C-terminal (SPOC) domain.	ABSTRACT
118	154	SPEN paralog and ortholog C-terminal	structure_element	FPA belongs to the split ends (SPEN) family of proteins, which contain N-terminal RNA recognition motifs (RRMs) and a SPEN paralog and ortholog C-terminal (SPOC) domain.	ABSTRACT
156	160	SPOC	structure_element	FPA belongs to the split ends (SPEN) family of proteins, which contain N-terminal RNA recognition motifs (RRMs) and a SPEN paralog and ortholog C-terminal (SPOC) domain.	ABSTRACT
4	8	SPOC	structure_element	The SPOC domain is highly conserved among FPA homologs in plants, but the conservation with the domain in other SPEN proteins is much lower.	ABSTRACT
19	35	highly conserved	protein_state	The SPOC domain is highly conserved among FPA homologs in plants, but the conservation with the domain in other SPEN proteins is much lower.	ABSTRACT
42	45	FPA	protein	The SPOC domain is highly conserved among FPA homologs in plants, but the conservation with the domain in other SPEN proteins is much lower.	ABSTRACT
58	64	plants	taxonomy_domain	The SPOC domain is highly conserved among FPA homologs in plants, but the conservation with the domain in other SPEN proteins is much lower.	ABSTRACT
112	116	SPEN	protein_type	The SPOC domain is highly conserved among FPA homologs in plants, but the conservation with the domain in other SPEN proteins is much lower.	ABSTRACT
23	40	crystal structure	evidence	We have determined the crystal structure of Arabidopsis thaliana FPA SPOC domain at 2.7 Å resolution.	ABSTRACT
44	64	Arabidopsis thaliana	species	We have determined the crystal structure of Arabidopsis thaliana FPA SPOC domain at 2.7 Å resolution.	ABSTRACT
65	68	FPA	protein	We have determined the crystal structure of Arabidopsis thaliana FPA SPOC domain at 2.7 Å resolution.	ABSTRACT
69	73	SPOC	structure_element	We have determined the crystal structure of Arabidopsis thaliana FPA SPOC domain at 2.7 Å resolution.	ABSTRACT
12	21	structure	evidence	The overall structure is similar to that of the SPOC domain in human SMRT/HDAC1 Associated Repressor Protein (SHARP), although there are also substantial conformational differences between them.	ABSTRACT
48	52	SPOC	structure_element	The overall structure is similar to that of the SPOC domain in human SMRT/HDAC1 Associated Repressor Protein (SHARP), although there are also substantial conformational differences between them.	ABSTRACT
63	68	human	species	The overall structure is similar to that of the SPOC domain in human SMRT/HDAC1 Associated Repressor Protein (SHARP), although there are also substantial conformational differences between them.	ABSTRACT
69	108	SMRT/HDAC1 Associated Repressor Protein	protein	The overall structure is similar to that of the SPOC domain in human SMRT/HDAC1 Associated Repressor Protein (SHARP), although there are also substantial conformational differences between them.	ABSTRACT
110	115	SHARP	protein	The overall structure is similar to that of the SPOC domain in human SMRT/HDAC1 Associated Repressor Protein (SHARP), although there are also substantial conformational differences between them.	ABSTRACT
0	32	Structural and sequence analyses	experimental_method	Structural and sequence analyses identify a surface patch that is conserved among plant FPA homologs.	ABSTRACT
44	57	surface patch	site	Structural and sequence analyses identify a surface patch that is conserved among plant FPA homologs.	ABSTRACT
66	75	conserved	protein_state	Structural and sequence analyses identify a surface patch that is conserved among plant FPA homologs.	ABSTRACT
82	87	plant	taxonomy_domain	Structural and sequence analyses identify a surface patch that is conserved among plant FPA homologs.	ABSTRACT
88	91	FPA	protein	Structural and sequence analyses identify a surface patch that is conserved among plant FPA homologs.	ABSTRACT
0	9	Mutations	experimental_method	Mutations of two residues in this surface patch did not disrupt FPA functions, suggesting that either the SPOC domain is not required for the role of FPA in regulating RNA 3′-end formation or the functions of the FPA SPOC domain cannot be disrupted by the combination of mutations, in contrast to observations with the SHARP SPOC domain.	ABSTRACT
34	47	surface patch	site	Mutations of two residues in this surface patch did not disrupt FPA functions, suggesting that either the SPOC domain is not required for the role of FPA in regulating RNA 3′-end formation or the functions of the FPA SPOC domain cannot be disrupted by the combination of mutations, in contrast to observations with the SHARP SPOC domain.	ABSTRACT
64	67	FPA	protein	Mutations of two residues in this surface patch did not disrupt FPA functions, suggesting that either the SPOC domain is not required for the role of FPA in regulating RNA 3′-end formation or the functions of the FPA SPOC domain cannot be disrupted by the combination of mutations, in contrast to observations with the SHARP SPOC domain.	ABSTRACT
106	110	SPOC	structure_element	Mutations of two residues in this surface patch did not disrupt FPA functions, suggesting that either the SPOC domain is not required for the role of FPA in regulating RNA 3′-end formation or the functions of the FPA SPOC domain cannot be disrupted by the combination of mutations, in contrast to observations with the SHARP SPOC domain.	ABSTRACT
150	153	FPA	protein	Mutations of two residues in this surface patch did not disrupt FPA functions, suggesting that either the SPOC domain is not required for the role of FPA in regulating RNA 3′-end formation or the functions of the FPA SPOC domain cannot be disrupted by the combination of mutations, in contrast to observations with the SHARP SPOC domain.	ABSTRACT
168	171	RNA	chemical	Mutations of two residues in this surface patch did not disrupt FPA functions, suggesting that either the SPOC domain is not required for the role of FPA in regulating RNA 3′-end formation or the functions of the FPA SPOC domain cannot be disrupted by the combination of mutations, in contrast to observations with the SHARP SPOC domain.	ABSTRACT
213	216	FPA	protein	Mutations of two residues in this surface patch did not disrupt FPA functions, suggesting that either the SPOC domain is not required for the role of FPA in regulating RNA 3′-end formation or the functions of the FPA SPOC domain cannot be disrupted by the combination of mutations, in contrast to observations with the SHARP SPOC domain.	ABSTRACT
217	221	SPOC	structure_element	Mutations of two residues in this surface patch did not disrupt FPA functions, suggesting that either the SPOC domain is not required for the role of FPA in regulating RNA 3′-end formation or the functions of the FPA SPOC domain cannot be disrupted by the combination of mutations, in contrast to observations with the SHARP SPOC domain.	ABSTRACT
319	324	SHARP	protein	Mutations of two residues in this surface patch did not disrupt FPA functions, suggesting that either the SPOC domain is not required for the role of FPA in regulating RNA 3′-end formation or the functions of the FPA SPOC domain cannot be disrupted by the combination of mutations, in contrast to observations with the SHARP SPOC domain.	ABSTRACT
325	329	SPOC	structure_element	Mutations of two residues in this surface patch did not disrupt FPA functions, suggesting that either the SPOC domain is not required for the role of FPA in regulating RNA 3′-end formation or the functions of the FPA SPOC domain cannot be disrupted by the combination of mutations, in contrast to observations with the SHARP SPOC domain.	ABSTRACT
0	10	Eukaryotic	taxonomy_domain	Eukaryotic messenger RNAs (mRNAs) are made as precursors through transcription by RNA polymerase II (Pol II), and these primary transcripts undergo extensive processing, including 3′-end cleavage and polyadenylation.	INTRO
11	25	messenger RNAs	chemical	Eukaryotic messenger RNAs (mRNAs) are made as precursors through transcription by RNA polymerase II (Pol II), and these primary transcripts undergo extensive processing, including 3′-end cleavage and polyadenylation.	INTRO
27	32	mRNAs	chemical	Eukaryotic messenger RNAs (mRNAs) are made as precursors through transcription by RNA polymerase II (Pol II), and these primary transcripts undergo extensive processing, including 3′-end cleavage and polyadenylation.	INTRO
82	99	RNA polymerase II	complex_assembly	Eukaryotic messenger RNAs (mRNAs) are made as precursors through transcription by RNA polymerase II (Pol II), and these primary transcripts undergo extensive processing, including 3′-end cleavage and polyadenylation.	INTRO
101	107	Pol II	complex_assembly	Eukaryotic messenger RNAs (mRNAs) are made as precursors through transcription by RNA polymerase II (Pol II), and these primary transcripts undergo extensive processing, including 3′-end cleavage and polyadenylation.	INTRO
103	113	eukaryotes	taxonomy_domain	In addition, alternative 3′-end cleavage and polyadenylation is an essential and ubiquitous process in eukaryotes.	INTRO
14	24	split ends	protein_type	Recently, the split ends (SPEN) family of proteins was identified as RNA binding proteins that regulate alternative 3′-end cleavage and polyadenylation.	INTRO
26	30	SPEN	protein_type	Recently, the split ends (SPEN) family of proteins was identified as RNA binding proteins that regulate alternative 3′-end cleavage and polyadenylation.	INTRO
69	89	RNA binding proteins	protein_type	Recently, the split ends (SPEN) family of proteins was identified as RNA binding proteins that regulate alternative 3′-end cleavage and polyadenylation.	INTRO
48	70	RNA recognition motifs	structure_element	They are characterized by possessing N-terminal RNA recognition motifs (RRMs) and a conserved SPEN paralog and ortholog C-terminal (SPOC) domain (Fig 1A).	INTRO
72	76	RRMs	structure_element	They are characterized by possessing N-terminal RNA recognition motifs (RRMs) and a conserved SPEN paralog and ortholog C-terminal (SPOC) domain (Fig 1A).	INTRO
84	93	conserved	protein_state	They are characterized by possessing N-terminal RNA recognition motifs (RRMs) and a conserved SPEN paralog and ortholog C-terminal (SPOC) domain (Fig 1A).	INTRO
94	130	SPEN paralog and ortholog C-terminal	structure_element	They are characterized by possessing N-terminal RNA recognition motifs (RRMs) and a conserved SPEN paralog and ortholog C-terminal (SPOC) domain (Fig 1A).	INTRO
132	136	SPOC	structure_element	They are characterized by possessing N-terminal RNA recognition motifs (RRMs) and a conserved SPEN paralog and ortholog C-terminal (SPOC) domain (Fig 1A).	INTRO
4	8	SPOC	structure_element	The SPOC domain is believed to mediate protein-protein interactions and has diverse functions among SPEN family proteins, but the molecular mechanism of these functions is not well understood.	INTRO
100	104	SPEN	protein_type	The SPOC domain is believed to mediate protein-protein interactions and has diverse functions among SPEN family proteins, but the molecular mechanism of these functions is not well understood.	INTRO
0	21	Sequence conservation	evidence	Sequence conservation of SPOC domains.	FIG
25	29	SPOC	structure_element	Sequence conservation of SPOC domains.	FIG
23	34	A. thaliana	species	Domain organization of A. thaliana FPA. (B).	FIG
35	38	FPA	protein	Domain organization of A. thaliana FPA. (B).	FIG
0	18	Sequence alignment	experimental_method	Sequence alignment of the SPOC domains of Arabidopsis thaliana FPA, human RBM15, Drosophila SPEN, mouse MINT, and human SHARP.	FIG
26	30	SPOC	structure_element	Sequence alignment of the SPOC domains of Arabidopsis thaliana FPA, human RBM15, Drosophila SPEN, mouse MINT, and human SHARP.	FIG
42	62	Arabidopsis thaliana	species	Sequence alignment of the SPOC domains of Arabidopsis thaliana FPA, human RBM15, Drosophila SPEN, mouse MINT, and human SHARP.	FIG
63	66	FPA	protein	Sequence alignment of the SPOC domains of Arabidopsis thaliana FPA, human RBM15, Drosophila SPEN, mouse MINT, and human SHARP.	FIG
68	73	human	species	Sequence alignment of the SPOC domains of Arabidopsis thaliana FPA, human RBM15, Drosophila SPEN, mouse MINT, and human SHARP.	FIG
74	79	RBM15	protein	Sequence alignment of the SPOC domains of Arabidopsis thaliana FPA, human RBM15, Drosophila SPEN, mouse MINT, and human SHARP.	FIG
81	91	Drosophila	taxonomy_domain	Sequence alignment of the SPOC domains of Arabidopsis thaliana FPA, human RBM15, Drosophila SPEN, mouse MINT, and human SHARP.	FIG
92	96	SPEN	protein_type	Sequence alignment of the SPOC domains of Arabidopsis thaliana FPA, human RBM15, Drosophila SPEN, mouse MINT, and human SHARP.	FIG
98	103	mouse	taxonomy_domain	Sequence alignment of the SPOC domains of Arabidopsis thaliana FPA, human RBM15, Drosophila SPEN, mouse MINT, and human SHARP.	FIG
104	108	MINT	protein	Sequence alignment of the SPOC domains of Arabidopsis thaliana FPA, human RBM15, Drosophila SPEN, mouse MINT, and human SHARP.	FIG
114	119	human	species	Sequence alignment of the SPOC domains of Arabidopsis thaliana FPA, human RBM15, Drosophila SPEN, mouse MINT, and human SHARP.	FIG
120	125	SHARP	protein	Sequence alignment of the SPOC domains of Arabidopsis thaliana FPA, human RBM15, Drosophila SPEN, mouse MINT, and human SHARP.	FIG
12	27	surface patch 1	site	Residues in surface patch 1 are indicated with the orange dots, and those in surface patch 2 with the green dots.	FIG
77	92	surface patch 2	site	Residues in surface patch 1 are indicated with the orange dots, and those in surface patch 2 with the green dots.	FIG
40	49	structure	evidence	The secondary structure elements in the structure of FPA SPOC are labeled.	FIG
53	56	FPA	protein	The secondary structure elements in the structure of FPA SPOC are labeled.	FIG
57	61	SPOC	structure_element	The secondary structure elements in the structure of FPA SPOC are labeled.	FIG
18	36	strictly conserved	protein_state	Residues that are strictly conserved among the five proteins are shown in white with a red background, and those that are mostly conserved in red.	FIG
122	138	mostly conserved	protein_state	Residues that are strictly conserved among the five proteins are shown in white with a red background, and those that are mostly conserved in red.	FIG
0	3	FPA	protein	FPA, a SPEN family protein in Arabidopsis thaliana and other plants, was found to regulate the 3′-end alternative cleavage and polyadenylation of the antisense RNAs of FLOWERING LOCUS (FLC), a flowering repressor gene.	INTRO
7	11	SPEN	protein_type	FPA, a SPEN family protein in Arabidopsis thaliana and other plants, was found to regulate the 3′-end alternative cleavage and polyadenylation of the antisense RNAs of FLOWERING LOCUS (FLC), a flowering repressor gene.	INTRO
30	50	Arabidopsis thaliana	species	FPA, a SPEN family protein in Arabidopsis thaliana and other plants, was found to regulate the 3′-end alternative cleavage and polyadenylation of the antisense RNAs of FLOWERING LOCUS (FLC), a flowering repressor gene.	INTRO
61	67	plants	taxonomy_domain	FPA, a SPEN family protein in Arabidopsis thaliana and other plants, was found to regulate the 3′-end alternative cleavage and polyadenylation of the antisense RNAs of FLOWERING LOCUS (FLC), a flowering repressor gene.	INTRO
150	164	antisense RNAs	chemical	FPA, a SPEN family protein in Arabidopsis thaliana and other plants, was found to regulate the 3′-end alternative cleavage and polyadenylation of the antisense RNAs of FLOWERING LOCUS (FLC), a flowering repressor gene.	INTRO
168	183	FLOWERING LOCUS	gene	FPA, a SPEN family protein in Arabidopsis thaliana and other plants, was found to regulate the 3′-end alternative cleavage and polyadenylation of the antisense RNAs of FLOWERING LOCUS (FLC), a flowering repressor gene.	INTRO
185	188	FLC	gene	FPA, a SPEN family protein in Arabidopsis thaliana and other plants, was found to regulate the 3′-end alternative cleavage and polyadenylation of the antisense RNAs of FLOWERING LOCUS (FLC), a flowering repressor gene.	INTRO
0	3	FPA	protein	FPA promotes the 3′-end processing of class I FLC antisense RNAs, which includes the proximal polyadenylation site.	INTRO
46	49	FLC	gene	FPA promotes the 3′-end processing of class I FLC antisense RNAs, which includes the proximal polyadenylation site.	INTRO
50	64	antisense RNAs	chemical	FPA promotes the 3′-end processing of class I FLC antisense RNAs, which includes the proximal polyadenylation site.	INTRO
94	114	polyadenylation site	site	FPA promotes the 3′-end processing of class I FLC antisense RNAs, which includes the proximal polyadenylation site.	INTRO
24	43	histone demethylase	protein_type	This is associated with histone demethylase activity and down-regulation of FLC transcription.	INTRO
76	79	FLC	gene	This is associated with histone demethylase activity and down-regulation of FLC transcription.	INTRO
11	15	SPOC	structure_element	Although a SPOC domain is found in all the SPEN family proteins, its sequence conservation is rather low.	INTRO
43	47	SPEN	protein_type	Although a SPOC domain is found in all the SPEN family proteins, its sequence conservation is rather low.	INTRO
47	51	SPOC	structure_element	For example, the sequence identity between the SPOC domains of A. thaliana FPA and human SMRT/HDAC1 Associated Repressor Protein (SHARP) is only 19% (Fig 1B).	INTRO
63	74	A. thaliana	species	For example, the sequence identity between the SPOC domains of A. thaliana FPA and human SMRT/HDAC1 Associated Repressor Protein (SHARP) is only 19% (Fig 1B).	INTRO
75	78	FPA	protein	For example, the sequence identity between the SPOC domains of A. thaliana FPA and human SMRT/HDAC1 Associated Repressor Protein (SHARP) is only 19% (Fig 1B).	INTRO
83	88	human	species	For example, the sequence identity between the SPOC domains of A. thaliana FPA and human SMRT/HDAC1 Associated Repressor Protein (SHARP) is only 19% (Fig 1B).	INTRO
89	128	SMRT/HDAC1 Associated Repressor Protein	protein	For example, the sequence identity between the SPOC domains of A. thaliana FPA and human SMRT/HDAC1 Associated Repressor Protein (SHARP) is only 19% (Fig 1B).	INTRO
130	135	SHARP	protein	For example, the sequence identity between the SPOC domains of A. thaliana FPA and human SMRT/HDAC1 Associated Repressor Protein (SHARP) is only 19% (Fig 1B).	INTRO
15	20	SHARP	protein	Currently, the SHARP SPOC domain is the only one with structural information.	INTRO
21	25	SPOC	structure_element	Currently, the SHARP SPOC domain is the only one with structural information.	INTRO
126	129	FPA	protein	As a first step toward understanding the molecular basis for the regulation of alternative 3′-end processing and flowering by FPA, we have determined the crystal structure of the SPOC domain of A. thaliana FPA at 2.7 Å resolution.	INTRO
154	171	crystal structure	evidence	As a first step toward understanding the molecular basis for the regulation of alternative 3′-end processing and flowering by FPA, we have determined the crystal structure of the SPOC domain of A. thaliana FPA at 2.7 Å resolution.	INTRO
179	183	SPOC	structure_element	As a first step toward understanding the molecular basis for the regulation of alternative 3′-end processing and flowering by FPA, we have determined the crystal structure of the SPOC domain of A. thaliana FPA at 2.7 Å resolution.	INTRO
194	205	A. thaliana	species	As a first step toward understanding the molecular basis for the regulation of alternative 3′-end processing and flowering by FPA, we have determined the crystal structure of the SPOC domain of A. thaliana FPA at 2.7 Å resolution.	INTRO
206	209	FPA	protein	As a first step toward understanding the molecular basis for the regulation of alternative 3′-end processing and flowering by FPA, we have determined the crystal structure of the SPOC domain of A. thaliana FPA at 2.7 Å resolution.	INTRO
12	21	structure	evidence	The overall structure is similar to that of the SHARP SPOC domain, although there are also substantial conformational differences between them.	INTRO
48	53	SHARP	protein	The overall structure is similar to that of the SHARP SPOC domain, although there are also substantial conformational differences between them.	INTRO
54	58	SPOC	structure_element	The overall structure is similar to that of the SHARP SPOC domain, although there are also substantial conformational differences between them.	INTRO
4	13	structure	evidence	The structure reveals a surface patch that is conserved among FPA homologs.	INTRO
24	37	surface patch	site	The structure reveals a surface patch that is conserved among FPA homologs.	INTRO
46	55	conserved	protein_state	The structure reveals a surface patch that is conserved among FPA homologs.	INTRO
62	65	FPA	protein	The structure reveals a surface patch that is conserved among FPA homologs.	INTRO
0	9	Structure	evidence	Structure of FPA SPOC domain	RESULTS
13	16	FPA	protein	Structure of FPA SPOC domain	RESULTS
17	21	SPOC	structure_element	Structure of FPA SPOC domain	RESULTS
4	21	crystal structure	evidence	The crystal structure of the SPOC domain of A. thaliana FPA has been determined at 2.7 Å resolution using the selenomethionyl single-wavelength anomalous dispersion method.	RESULTS
29	33	SPOC	structure_element	The crystal structure of the SPOC domain of A. thaliana FPA has been determined at 2.7 Å resolution using the selenomethionyl single-wavelength anomalous dispersion method.	RESULTS
44	55	A. thaliana	species	The crystal structure of the SPOC domain of A. thaliana FPA has been determined at 2.7 Å resolution using the selenomethionyl single-wavelength anomalous dispersion method.	RESULTS
56	59	FPA	protein	The crystal structure of the SPOC domain of A. thaliana FPA has been determined at 2.7 Å resolution using the selenomethionyl single-wavelength anomalous dispersion method.	RESULTS
110	171	selenomethionyl single-wavelength anomalous dispersion method	experimental_method	The crystal structure of the SPOC domain of A. thaliana FPA has been determined at 2.7 Å resolution using the selenomethionyl single-wavelength anomalous dispersion method.	RESULTS
44	51	433–565	residue_range	The expression construct contained residues 433–565 of FPA, but only residues 439–460 and 465–565 are ordered in the crystal.	RESULTS
55	58	FPA	protein	The expression construct contained residues 433–565 of FPA, but only residues 439–460 and 465–565 are ordered in the crystal.	RESULTS
78	85	439–460	residue_range	The expression construct contained residues 433–565 of FPA, but only residues 439–460 and 465–565 are ordered in the crystal.	RESULTS
90	97	465–565	residue_range	The expression construct contained residues 433–565 of FPA, but only residues 439–460 and 465–565 are ordered in the crystal.	RESULTS
117	124	crystal	evidence	The expression construct contained residues 433–565 of FPA, but only residues 439–460 and 465–565 are ordered in the crystal.	RESULTS
4	16	atomic model	evidence	The atomic model has good agreement with the X-ray diffraction data and the expected bond lengths, bond angles and other geometric parameters (Table 1).	RESULTS
45	67	X-ray diffraction data	evidence	The atomic model has good agreement with the X-ray diffraction data and the expected bond lengths, bond angles and other geometric parameters (Table 1).	RESULTS
59	76	Ramachandran plot	evidence	All the residues are located in the favored regions of the Ramachandran plot (data not shown).	RESULTS
4	13	structure	evidence	The structure has been deposited in the Protein Data Bank, with accession code 5KXF.	RESULTS
159	167	R factor	evidence	"Resolution range (Å)1	50–2.7 (2.8–2.7)	 	Number of observations	78,008	 	Rmerge (%)	10.5 (45.3)	 	I/σI	24.1 (6.3)	 	Redundancy		 	Completeness (%)	100 (100)	 	R factor (%)	19.2 (25.0)	 	Free R factor (%)	25.4 (35.4)	 	Rms deviation in bond lengths (Å)	0.017	 	Rms deviation in bond angles (°)	1.9	 	"	TABLE
186	199	Free R factor	evidence	"Resolution range (Å)1	50–2.7 (2.8–2.7)	 	Number of observations	78,008	 	Rmerge (%)	10.5 (45.3)	 	I/σI	24.1 (6.3)	 	Redundancy		 	Completeness (%)	100 (100)	 	R factor (%)	19.2 (25.0)	 	Free R factor (%)	25.4 (35.4)	 	Rms deviation in bond lengths (Å)	0.017	 	Rms deviation in bond angles (°)	1.9	 	"	TABLE
4	21	crystal structure	evidence	The crystal structure of the FPA SPOC domain contains a seven-stranded, mostly anti-parallel β-barrel (β1-β7) and three helices (αA-αC) (Fig 2A).	RESULTS
29	32	FPA	protein	The crystal structure of the FPA SPOC domain contains a seven-stranded, mostly anti-parallel β-barrel (β1-β7) and three helices (αA-αC) (Fig 2A).	RESULTS
33	37	SPOC	structure_element	The crystal structure of the FPA SPOC domain contains a seven-stranded, mostly anti-parallel β-barrel (β1-β7) and three helices (αA-αC) (Fig 2A).	RESULTS
56	101	seven-stranded, mostly anti-parallel β-barrel	structure_element	The crystal structure of the FPA SPOC domain contains a seven-stranded, mostly anti-parallel β-barrel (β1-β7) and three helices (αA-αC) (Fig 2A).	RESULTS
103	108	β1-β7	structure_element	The crystal structure of the FPA SPOC domain contains a seven-stranded, mostly anti-parallel β-barrel (β1-β7) and three helices (αA-αC) (Fig 2A).	RESULTS
120	127	helices	structure_element	The crystal structure of the FPA SPOC domain contains a seven-stranded, mostly anti-parallel β-barrel (β1-β7) and three helices (αA-αC) (Fig 2A).	RESULTS
129	134	αA-αC	structure_element	The crystal structure of the FPA SPOC domain contains a seven-stranded, mostly anti-parallel β-barrel (β1-β7) and three helices (αA-αC) (Fig 2A).	RESULTS
28	35	strands	structure_element	Only two of the neighboring strands, β1 and β3, are parallel to each other.	RESULTS
37	39	β1	structure_element	Only two of the neighboring strands, β1 and β3, are parallel to each other.	RESULTS
44	46	β3	structure_element	Only two of the neighboring strands, β1 and β3, are parallel to each other.	RESULTS
0	5	Helix	structure_element	Helix αB covers one end of the barrel, while helices αA and αC are located next to each other at one side of the barrel (Fig 2B).	RESULTS
6	8	αB	structure_element	Helix αB covers one end of the barrel, while helices αA and αC are located next to each other at one side of the barrel (Fig 2B).	RESULTS
31	37	barrel	structure_element	Helix αB covers one end of the barrel, while helices αA and αC are located next to each other at one side of the barrel (Fig 2B).	RESULTS
45	52	helices	structure_element	Helix αB covers one end of the barrel, while helices αA and αC are located next to each other at one side of the barrel (Fig 2B).	RESULTS
53	55	αA	structure_element	Helix αB covers one end of the barrel, while helices αA and αC are located next to each other at one side of the barrel (Fig 2B).	RESULTS
60	62	αC	structure_element	Helix αB covers one end of the barrel, while helices αA and αC are located next to each other at one side of the barrel (Fig 2B).	RESULTS
113	119	barrel	structure_element	Helix αB covers one end of the barrel, while helices αA and αC are located next to each other at one side of the barrel (Fig 2B).	RESULTS
21	29	β-barrel	structure_element	The other end of the β-barrel is covered by the loop connecting strands β2 and β3, which contains the disordered 461–464 segment.	RESULTS
48	52	loop	structure_element	The other end of the β-barrel is covered by the loop connecting strands β2 and β3, which contains the disordered 461–464 segment.	RESULTS
64	71	strands	structure_element	The other end of the β-barrel is covered by the loop connecting strands β2 and β3, which contains the disordered 461–464 segment.	RESULTS
72	74	β2	structure_element	The other end of the β-barrel is covered by the loop connecting strands β2 and β3, which contains the disordered 461–464 segment.	RESULTS
79	81	β3	structure_element	The other end of the β-barrel is covered by the loop connecting strands β2 and β3, which contains the disordered 461–464 segment.	RESULTS
102	112	disordered	protein_state	The other end of the β-barrel is covered by the loop connecting strands β2 and β3, which contains the disordered 461–464 segment.	RESULTS
113	120	461–464	residue_range	The other end of the β-barrel is covered by the loop connecting strands β2 and β3, which contains the disordered 461–464 segment.	RESULTS
18	24	barrel	structure_element	The center of the barrel is filled with hydrophobic side chains and is not accessible to the solvent.	RESULTS
0	17	Crystal structure	evidence	Crystal structure of the SPOC domain of A. thaliana FPA.	FIG
25	29	SPOC	structure_element	Crystal structure of the SPOC domain of A. thaliana FPA.	FIG
40	51	A. thaliana	species	Crystal structure of the SPOC domain of A. thaliana FPA.	FIG
52	55	FPA	protein	Crystal structure of the SPOC domain of A. thaliana FPA.	FIG
25	34	structure	evidence	Schematic drawing of the structure of FPA SPOC domain, colored from blue at the N terminus to red at the C terminus.	FIG
38	41	FPA	protein	Schematic drawing of the structure of FPA SPOC domain, colored from blue at the N terminus to red at the C terminus.	FIG
42	46	SPOC	structure_element	Schematic drawing of the structure of FPA SPOC domain, colored from blue at the N terminus to red at the C terminus.	FIG
33	41	β-barrel	structure_element	The view is from the side of the β-barrel.	FIG
4	14	disordered	protein_state	The disordered segment (residues 460–465) is indicated with the dotted line.	FIG
33	40	460–465	residue_range	The disordered segment (residues 460–465) is indicated with the dotted line.	FIG
0	9	Structure	evidence	Structure of the FPA SPOC domain, viewed from the end of the β-barrel, after 90° rotation around the horizontal axis from panel A. All structure figures were produced with PyMOL (www.pymol.org).	FIG
17	20	FPA	protein	Structure of the FPA SPOC domain, viewed from the end of the β-barrel, after 90° rotation around the horizontal axis from panel A. All structure figures were produced with PyMOL (www.pymol.org).	FIG
21	25	SPOC	structure_element	Structure of the FPA SPOC domain, viewed from the end of the β-barrel, after 90° rotation around the horizontal axis from panel A. All structure figures were produced with PyMOL (www.pymol.org).	FIG
61	69	β-barrel	structure_element	Structure of the FPA SPOC domain, viewed from the end of the β-barrel, after 90° rotation around the horizontal axis from panel A. All structure figures were produced with PyMOL (www.pymol.org).	FIG
0	34	Comparisons to structural homologs	experimental_method	Comparisons to structural homologs of the SPOC domain	RESULTS
42	46	SPOC	structure_element	Comparisons to structural homologs of the SPOC domain	RESULTS
37	40	FPA	protein	Only five structural homologs of the FPA SPOC domain were found in the Protein Data Bank with the DaliLite server, suggesting that the SPOC domain structure is relatively unique.	RESULTS
41	45	SPOC	structure_element	Only five structural homologs of the FPA SPOC domain were found in the Protein Data Bank with the DaliLite server, suggesting that the SPOC domain structure is relatively unique.	RESULTS
98	113	DaliLite server	experimental_method	Only five structural homologs of the FPA SPOC domain were found in the Protein Data Bank with the DaliLite server, suggesting that the SPOC domain structure is relatively unique.	RESULTS
135	139	SPOC	structure_element	Only five structural homologs of the FPA SPOC domain were found in the Protein Data Bank with the DaliLite server, suggesting that the SPOC domain structure is relatively unique.	RESULTS
147	156	structure	evidence	Only five structural homologs of the FPA SPOC domain were found in the Protein Data Bank with the DaliLite server, suggesting that the SPOC domain structure is relatively unique.	RESULTS
19	23	SPOC	structure_element	The top hit is the SPOC domain of human SHARP (Fig 3A), with a Z score of 12.3.	RESULTS
34	39	human	species	The top hit is the SPOC domain of human SHARP (Fig 3A), with a Z score of 12.3.	RESULTS
40	45	SHARP	protein	The top hit is the SPOC domain of human SHARP (Fig 3A), with a Z score of 12.3.	RESULTS
63	70	Z score	evidence	The top hit is the SPOC domain of human SHARP (Fig 3A), with a Z score of 12.3.	RESULTS
47	55	β-barrel	structure_element	The other four structural homologs include the β-barrel domain of the proteins Ku70 and Ku80 (Z score 11.4) (Fig 3B), a domain in the chromodomain protein Chp1 (Z score 10.8) (Fig 3C), and the activator interacting domain (ACID) of the Med25 subunit of the Mediator complex (Z score 8.5) (Fig 3D).	RESULTS
79	83	Ku70	protein	The other four structural homologs include the β-barrel domain of the proteins Ku70 and Ku80 (Z score 11.4) (Fig 3B), a domain in the chromodomain protein Chp1 (Z score 10.8) (Fig 3C), and the activator interacting domain (ACID) of the Med25 subunit of the Mediator complex (Z score 8.5) (Fig 3D).	RESULTS
88	92	Ku80	protein	The other four structural homologs include the β-barrel domain of the proteins Ku70 and Ku80 (Z score 11.4) (Fig 3B), a domain in the chromodomain protein Chp1 (Z score 10.8) (Fig 3C), and the activator interacting domain (ACID) of the Med25 subunit of the Mediator complex (Z score 8.5) (Fig 3D).	RESULTS
94	101	Z score	evidence	The other four structural homologs include the β-barrel domain of the proteins Ku70 and Ku80 (Z score 11.4) (Fig 3B), a domain in the chromodomain protein Chp1 (Z score 10.8) (Fig 3C), and the activator interacting domain (ACID) of the Med25 subunit of the Mediator complex (Z score 8.5) (Fig 3D).	RESULTS
134	154	chromodomain protein	protein_type	The other four structural homologs include the β-barrel domain of the proteins Ku70 and Ku80 (Z score 11.4) (Fig 3B), a domain in the chromodomain protein Chp1 (Z score 10.8) (Fig 3C), and the activator interacting domain (ACID) of the Med25 subunit of the Mediator complex (Z score 8.5) (Fig 3D).	RESULTS
155	159	Chp1	protein	The other four structural homologs include the β-barrel domain of the proteins Ku70 and Ku80 (Z score 11.4) (Fig 3B), a domain in the chromodomain protein Chp1 (Z score 10.8) (Fig 3C), and the activator interacting domain (ACID) of the Med25 subunit of the Mediator complex (Z score 8.5) (Fig 3D).	RESULTS
161	168	Z score	evidence	The other four structural homologs include the β-barrel domain of the proteins Ku70 and Ku80 (Z score 11.4) (Fig 3B), a domain in the chromodomain protein Chp1 (Z score 10.8) (Fig 3C), and the activator interacting domain (ACID) of the Med25 subunit of the Mediator complex (Z score 8.5) (Fig 3D).	RESULTS
193	221	activator interacting domain	structure_element	The other four structural homologs include the β-barrel domain of the proteins Ku70 and Ku80 (Z score 11.4) (Fig 3B), a domain in the chromodomain protein Chp1 (Z score 10.8) (Fig 3C), and the activator interacting domain (ACID) of the Med25 subunit of the Mediator complex (Z score 8.5) (Fig 3D).	RESULTS
223	227	ACID	structure_element	The other four structural homologs include the β-barrel domain of the proteins Ku70 and Ku80 (Z score 11.4) (Fig 3B), a domain in the chromodomain protein Chp1 (Z score 10.8) (Fig 3C), and the activator interacting domain (ACID) of the Med25 subunit of the Mediator complex (Z score 8.5) (Fig 3D).	RESULTS
236	241	Med25	protein	The other four structural homologs include the β-barrel domain of the proteins Ku70 and Ku80 (Z score 11.4) (Fig 3B), a domain in the chromodomain protein Chp1 (Z score 10.8) (Fig 3C), and the activator interacting domain (ACID) of the Med25 subunit of the Mediator complex (Z score 8.5) (Fig 3D).	RESULTS
275	282	Z score	evidence	The other four structural homologs include the β-barrel domain of the proteins Ku70 and Ku80 (Z score 11.4) (Fig 3B), a domain in the chromodomain protein Chp1 (Z score 10.8) (Fig 3C), and the activator interacting domain (ACID) of the Med25 subunit of the Mediator complex (Z score 8.5) (Fig 3D).	RESULTS
34	41	Z score	evidence	The next structural homolog has a Z score of 3.0.	RESULTS
27	30	FPA	protein	Structural homologs of the FPA SPOC domain.	FIG
31	35	SPOC	structure_element	Structural homologs of the FPA SPOC domain.	FIG
0	7	Overlay	experimental_method	Overlay of the structures of the FPA SPOC domain (cyan) and the SHARP SPOC domain (gray).	FIG
15	25	structures	evidence	Overlay of the structures of the FPA SPOC domain (cyan) and the SHARP SPOC domain (gray).	FIG
33	36	FPA	protein	Overlay of the structures of the FPA SPOC domain (cyan) and the SHARP SPOC domain (gray).	FIG
37	41	SPOC	structure_element	Overlay of the structures of the FPA SPOC domain (cyan) and the SHARP SPOC domain (gray).	FIG
64	69	SHARP	protein	Overlay of the structures of the FPA SPOC domain (cyan) and the SHARP SPOC domain (gray).	FIG
70	74	SPOC	structure_element	Overlay of the structures of the FPA SPOC domain (cyan) and the SHARP SPOC domain (gray).	FIG
24	45	doubly-phosphorylated	protein_state	The bound position of a doubly-phosphorylated peptide from SMRT is shown in magenta.	FIG
46	53	peptide	chemical	The bound position of a doubly-phosphorylated peptide from SMRT is shown in magenta.	FIG
59	63	SMRT	protein	The bound position of a doubly-phosphorylated peptide from SMRT is shown in magenta.	FIG
0	7	Overlay	experimental_method	Overlay of the structures of the FPA SPOC domain (cyan) and the Ku70 β-barrel domain (gray).	FIG
15	25	structures	evidence	Overlay of the structures of the FPA SPOC domain (cyan) and the Ku70 β-barrel domain (gray).	FIG
33	36	FPA	protein	Overlay of the structures of the FPA SPOC domain (cyan) and the Ku70 β-barrel domain (gray).	FIG
37	41	SPOC	structure_element	Overlay of the structures of the FPA SPOC domain (cyan) and the Ku70 β-barrel domain (gray).	FIG
64	68	Ku70	protein	Overlay of the structures of the FPA SPOC domain (cyan) and the Ku70 β-barrel domain (gray).	FIG
69	77	β-barrel	structure_element	Overlay of the structures of the FPA SPOC domain (cyan) and the Ku70 β-barrel domain (gray).	FIG
0	4	Ku80	protein	Ku80 contains a homologous domain (green), which forms a hetero-dimer with that in Ku70.	FIG
57	69	hetero-dimer	oligomeric_state	Ku80 contains a homologous domain (green), which forms a hetero-dimer with that in Ku70.	FIG
83	87	Ku70	protein	Ku80 contains a homologous domain (green), which forms a hetero-dimer with that in Ku70.	FIG
71	76	dsDNA	chemical	The two domains, and inserted segments on them, mediate the binding of dsDNA (orange).	FIG
67	75	β-barrel	structure_element	The red rectangle highlights the region of contact between the two β-barrel domains.	FIG
0	7	Overlay	experimental_method	Overlay of the structures of the FPA SPOC domain (cyan) and the homologous domain in Chp1 (gray).	FIG
15	25	structures	evidence	Overlay of the structures of the FPA SPOC domain (cyan) and the homologous domain in Chp1 (gray).	FIG
33	36	FPA	protein	Overlay of the structures of the FPA SPOC domain (cyan) and the homologous domain in Chp1 (gray).	FIG
37	41	SPOC	structure_element	Overlay of the structures of the FPA SPOC domain (cyan) and the homologous domain in Chp1 (gray).	FIG
85	89	Chp1	protein	Overlay of the structures of the FPA SPOC domain (cyan) and the homologous domain in Chp1 (gray).	FIG
23	27	Chp1	protein	The binding partner of Chp1, Tas3, is shown in green.	FIG
29	33	Tas3	protein	The binding partner of Chp1, Tas3, is shown in green.	FIG
57	69	binding site	site	The red rectangle indicates the region equivalent to the binding site of the SMART phosphopeptide in SHARP SPOC domain, where a loop of Tas3 is also located. (D).	FIG
77	82	SMART	protein	The red rectangle indicates the region equivalent to the binding site of the SMART phosphopeptide in SHARP SPOC domain, where a loop of Tas3 is also located. (D).	FIG
83	97	phosphopeptide	ptm	The red rectangle indicates the region equivalent to the binding site of the SMART phosphopeptide in SHARP SPOC domain, where a loop of Tas3 is also located. (D).	FIG
101	106	SHARP	protein	The red rectangle indicates the region equivalent to the binding site of the SMART phosphopeptide in SHARP SPOC domain, where a loop of Tas3 is also located. (D).	FIG
107	111	SPOC	structure_element	The red rectangle indicates the region equivalent to the binding site of the SMART phosphopeptide in SHARP SPOC domain, where a loop of Tas3 is also located. (D).	FIG
128	132	loop	structure_element	The red rectangle indicates the region equivalent to the binding site of the SMART phosphopeptide in SHARP SPOC domain, where a loop of Tas3 is also located. (D).	FIG
136	140	Tas3	protein	The red rectangle indicates the region equivalent to the binding site of the SMART phosphopeptide in SHARP SPOC domain, where a loop of Tas3 is also located. (D).	FIG
0	7	Overlay	experimental_method	Overlay of the structures of the FPA SPOC domain (cyan) and the Med25 ACID (gray).	FIG
15	25	structures	evidence	Overlay of the structures of the FPA SPOC domain (cyan) and the Med25 ACID (gray).	FIG
33	36	FPA	protein	Overlay of the structures of the FPA SPOC domain (cyan) and the Med25 ACID (gray).	FIG
37	41	SPOC	structure_element	Overlay of the structures of the FPA SPOC domain (cyan) and the Med25 ACID (gray).	FIG
64	69	Med25	protein	Overlay of the structures of the FPA SPOC domain (cyan) and the Med25 ACID (gray).	FIG
70	74	ACID	structure_element	Overlay of the structures of the FPA SPOC domain (cyan) and the Med25 ACID (gray).	FIG
0	5	SHARP	protein	SHARP is a transcriptional co-repressor in the nuclear receptor and Notch/RBP-Jκ signaling pathways.	RESULTS
11	39	transcriptional co-repressor	protein_type	SHARP is a transcriptional co-repressor in the nuclear receptor and Notch/RBP-Jκ signaling pathways.	RESULTS
47	63	nuclear receptor	protein_type	SHARP is a transcriptional co-repressor in the nuclear receptor and Notch/RBP-Jκ signaling pathways.	RESULTS
68	73	Notch	protein	SHARP is a transcriptional co-repressor in the nuclear receptor and Notch/RBP-Jκ signaling pathways.	RESULTS
74	80	RBP-Jκ	protein	SHARP is a transcriptional co-repressor in the nuclear receptor and Notch/RBP-Jκ signaling pathways.	RESULTS
4	8	SPOC	structure_element	The SPOC domain of SHARP interacts directly with silencing mediator for retinoid and thyroid receptor (SMRT), nuclear receptor co-repressor (N-CoR), HDAC, and other components to represses transcription.	RESULTS
19	24	SHARP	protein	The SPOC domain of SHARP interacts directly with silencing mediator for retinoid and thyroid receptor (SMRT), nuclear receptor co-repressor (N-CoR), HDAC, and other components to represses transcription.	RESULTS
49	101	silencing mediator for retinoid and thyroid receptor	protein	The SPOC domain of SHARP interacts directly with silencing mediator for retinoid and thyroid receptor (SMRT), nuclear receptor co-repressor (N-CoR), HDAC, and other components to represses transcription.	RESULTS
103	107	SMRT	protein	The SPOC domain of SHARP interacts directly with silencing mediator for retinoid and thyroid receptor (SMRT), nuclear receptor co-repressor (N-CoR), HDAC, and other components to represses transcription.	RESULTS
110	139	nuclear receptor co-repressor	protein_type	The SPOC domain of SHARP interacts directly with silencing mediator for retinoid and thyroid receptor (SMRT), nuclear receptor co-repressor (N-CoR), HDAC, and other components to represses transcription.	RESULTS
141	146	N-CoR	protein_type	The SPOC domain of SHARP interacts directly with silencing mediator for retinoid and thyroid receptor (SMRT), nuclear receptor co-repressor (N-CoR), HDAC, and other components to represses transcription.	RESULTS
149	153	HDAC	protein	The SPOC domain of SHARP interacts directly with silencing mediator for retinoid and thyroid receptor (SMRT), nuclear receptor co-repressor (N-CoR), HDAC, and other components to represses transcription.	RESULTS
18	27	structure	evidence	While the overall structure of the FPA SPOC domain is similar to that of the SHARP SPOC domain, there are noticeable differences in the positioning of the β-strands and the helices, and most of the loops have substantially different conformations as well (Fig 3A).	RESULTS
35	38	FPA	protein	While the overall structure of the FPA SPOC domain is similar to that of the SHARP SPOC domain, there are noticeable differences in the positioning of the β-strands and the helices, and most of the loops have substantially different conformations as well (Fig 3A).	RESULTS
39	43	SPOC	structure_element	While the overall structure of the FPA SPOC domain is similar to that of the SHARP SPOC domain, there are noticeable differences in the positioning of the β-strands and the helices, and most of the loops have substantially different conformations as well (Fig 3A).	RESULTS
77	82	SHARP	protein	While the overall structure of the FPA SPOC domain is similar to that of the SHARP SPOC domain, there are noticeable differences in the positioning of the β-strands and the helices, and most of the loops have substantially different conformations as well (Fig 3A).	RESULTS
83	87	SPOC	structure_element	While the overall structure of the FPA SPOC domain is similar to that of the SHARP SPOC domain, there are noticeable differences in the positioning of the β-strands and the helices, and most of the loops have substantially different conformations as well (Fig 3A).	RESULTS
155	164	β-strands	structure_element	While the overall structure of the FPA SPOC domain is similar to that of the SHARP SPOC domain, there are noticeable differences in the positioning of the β-strands and the helices, and most of the loops have substantially different conformations as well (Fig 3A).	RESULTS
173	180	helices	structure_element	While the overall structure of the FPA SPOC domain is similar to that of the SHARP SPOC domain, there are noticeable differences in the positioning of the β-strands and the helices, and most of the loops have substantially different conformations as well (Fig 3A).	RESULTS
198	203	loops	structure_element	While the overall structure of the FPA SPOC domain is similar to that of the SHARP SPOC domain, there are noticeable differences in the positioning of the β-strands and the helices, and most of the loops have substantially different conformations as well (Fig 3A).	RESULTS
17	22	SHARP	protein	In addition, the SHARP SPOC domain has three extra helices.	RESULTS
23	27	SPOC	structure_element	In addition, the SHARP SPOC domain has three extra helices.	RESULTS
51	58	helices	structure_element	In addition, the SHARP SPOC domain has three extra helices.	RESULTS
40	48	β-barrel	structure_element	One of them covers the other end of the β-barrel, and the other two shield an additional surface of the side of the β-barrel from solvent.	RESULTS
116	124	β-barrel	structure_element	One of them covers the other end of the β-barrel, and the other two shield an additional surface of the side of the β-barrel from solvent.	RESULTS
2	23	doubly-phosphorylated	protein_state	A doubly-phosphorylated peptide from SMRT is bound to the side of the barrel, near strands β1 and β3 (Fig 3A).	RESULTS
24	31	peptide	chemical	A doubly-phosphorylated peptide from SMRT is bound to the side of the barrel, near strands β1 and β3 (Fig 3A).	RESULTS
37	41	SMRT	protein	A doubly-phosphorylated peptide from SMRT is bound to the side of the barrel, near strands β1 and β3 (Fig 3A).	RESULTS
45	53	bound to	protein_state	A doubly-phosphorylated peptide from SMRT is bound to the side of the barrel, near strands β1 and β3 (Fig 3A).	RESULTS
70	76	barrel	structure_element	A doubly-phosphorylated peptide from SMRT is bound to the side of the barrel, near strands β1 and β3 (Fig 3A).	RESULTS
83	90	strands	structure_element	A doubly-phosphorylated peptide from SMRT is bound to the side of the barrel, near strands β1 and β3 (Fig 3A).	RESULTS
91	93	β1	structure_element	A doubly-phosphorylated peptide from SMRT is bound to the side of the barrel, near strands β1 and β3 (Fig 3A).	RESULTS
98	100	β3	structure_element	A doubly-phosphorylated peptide from SMRT is bound to the side of the barrel, near strands β1 and β3 (Fig 3A).	RESULTS
54	57	FPA	protein	Such a binding mode probably would not be possible in FPA, as the peptide would clash with the β1-β2 loop.	RESULTS
66	73	peptide	chemical	Such a binding mode probably would not be possible in FPA, as the peptide would clash with the β1-β2 loop.	RESULTS
95	105	β1-β2 loop	structure_element	Such a binding mode probably would not be possible in FPA, as the peptide would clash with the β1-β2 loop.	RESULTS
4	13	Ku70-Ku80	complex_assembly	The Ku70-Ku80 hetero-dimer is involved in DNA double-strand break repair and the β-barrel domain contributes to DNA binding.	RESULTS
14	26	hetero-dimer	oligomeric_state	The Ku70-Ku80 hetero-dimer is involved in DNA double-strand break repair and the β-barrel domain contributes to DNA binding.	RESULTS
81	89	β-barrel	structure_element	The Ku70-Ku80 hetero-dimer is involved in DNA double-strand break repair and the β-barrel domain contributes to DNA binding.	RESULTS
112	115	DNA	chemical	The Ku70-Ku80 hetero-dimer is involved in DNA double-strand break repair and the β-barrel domain contributes to DNA binding.	RESULTS
13	21	β-barrel	structure_element	In fact, the β-barrel domains of Ku70 and Ku80 form a hetero-dimer, primarily through interactions between the loops connecting the third and fourth strands of the barrel (Fig 3B).	RESULTS
33	37	Ku70	protein	In fact, the β-barrel domains of Ku70 and Ku80 form a hetero-dimer, primarily through interactions between the loops connecting the third and fourth strands of the barrel (Fig 3B).	RESULTS
42	46	Ku80	protein	In fact, the β-barrel domains of Ku70 and Ku80 form a hetero-dimer, primarily through interactions between the loops connecting the third and fourth strands of the barrel (Fig 3B).	RESULTS
54	66	hetero-dimer	oligomeric_state	In fact, the β-barrel domains of Ku70 and Ku80 form a hetero-dimer, primarily through interactions between the loops connecting the third and fourth strands of the barrel (Fig 3B).	RESULTS
111	116	loops	structure_element	In fact, the β-barrel domains of Ku70 and Ku80 form a hetero-dimer, primarily through interactions between the loops connecting the third and fourth strands of the barrel (Fig 3B).	RESULTS
132	156	third and fourth strands	structure_element	In fact, the β-barrel domains of Ku70 and Ku80 form a hetero-dimer, primarily through interactions between the loops connecting the third and fourth strands of the barrel (Fig 3B).	RESULTS
164	170	barrel	structure_element	In fact, the β-barrel domains of Ku70 and Ku80 form a hetero-dimer, primarily through interactions between the loops connecting the third and fourth strands of the barrel (Fig 3B).	RESULTS
25	34	β-barrels	structure_element	The open ends of the two β-barrels face the DNA binding sites, and contact the phosphodiester backbone of the dsDNA.	RESULTS
44	61	DNA binding sites	site	The open ends of the two β-barrels face the DNA binding sites, and contact the phosphodiester backbone of the dsDNA.	RESULTS
110	115	dsDNA	chemical	The open ends of the two β-barrels face the DNA binding sites, and contact the phosphodiester backbone of the dsDNA.	RESULTS
15	26	long insert	structure_element	In addition, a long insert connecting strands β2 and β3 in the two domains form an arch-like structure, encircling the dsDNA.	RESULTS
38	45	strands	structure_element	In addition, a long insert connecting strands β2 and β3 in the two domains form an arch-like structure, encircling the dsDNA.	RESULTS
46	48	β2	structure_element	In addition, a long insert connecting strands β2 and β3 in the two domains form an arch-like structure, encircling the dsDNA.	RESULTS
53	55	β3	structure_element	In addition, a long insert connecting strands β2 and β3 in the two domains form an arch-like structure, encircling the dsDNA.	RESULTS
83	102	arch-like structure	structure_element	In addition, a long insert connecting strands β2 and β3 in the two domains form an arch-like structure, encircling the dsDNA.	RESULTS
119	124	dsDNA	chemical	In addition, a long insert connecting strands β2 and β3 in the two domains form an arch-like structure, encircling the dsDNA.	RESULTS
0	4	Chp1	protein	Chp1 is a subunit of the RNA-induced initiation of transcriptional gene silencing (RITS) complex.	RESULTS
25	81	RNA-induced initiation of transcriptional gene silencing	complex_assembly	Chp1 is a subunit of the RNA-induced initiation of transcriptional gene silencing (RITS) complex.	RESULTS
83	87	RITS	complex_assembly	Chp1 is a subunit of the RNA-induced initiation of transcriptional gene silencing (RITS) complex.	RESULTS
15	19	Chp1	protein	The partner of Chp1, Tas3, is bound between the barrel domain and the second domain of Chp1, and the linker between the two domains is also crucial for this interaction (Fig 3C).	RESULTS
21	25	Tas3	protein	The partner of Chp1, Tas3, is bound between the barrel domain and the second domain of Chp1, and the linker between the two domains is also crucial for this interaction (Fig 3C).	RESULTS
48	61	barrel domain	structure_element	The partner of Chp1, Tas3, is bound between the barrel domain and the second domain of Chp1, and the linker between the two domains is also crucial for this interaction (Fig 3C).	RESULTS
70	83	second domain	structure_element	The partner of Chp1, Tas3, is bound between the barrel domain and the second domain of Chp1, and the linker between the two domains is also crucial for this interaction (Fig 3C).	RESULTS
87	91	Chp1	protein	The partner of Chp1, Tas3, is bound between the barrel domain and the second domain of Chp1, and the linker between the two domains is also crucial for this interaction (Fig 3C).	RESULTS
101	107	linker	structure_element	The partner of Chp1, Tas3, is bound between the barrel domain and the second domain of Chp1, and the linker between the two domains is also crucial for this interaction (Fig 3C).	RESULTS
33	41	β-barrel	structure_element	It is probably unlikely that the β-barrel itself is sufficient to bind Tas3.	RESULTS
71	75	Tas3	protein	It is probably unlikely that the β-barrel itself is sufficient to bind Tas3.	RESULTS
17	21	loop	structure_element	Interestingly, a loop in Tas3 contacts strand β3 of the barrel domain, at a location somewhat similar to that of the N-terminal segment of the SMRT peptide in complex with SHARP SPOC domain (Fig 3A).	RESULTS
25	29	Tas3	protein	Interestingly, a loop in Tas3 contacts strand β3 of the barrel domain, at a location somewhat similar to that of the N-terminal segment of the SMRT peptide in complex with SHARP SPOC domain (Fig 3A).	RESULTS
39	45	strand	structure_element	Interestingly, a loop in Tas3 contacts strand β3 of the barrel domain, at a location somewhat similar to that of the N-terminal segment of the SMRT peptide in complex with SHARP SPOC domain (Fig 3A).	RESULTS
46	48	β3	structure_element	Interestingly, a loop in Tas3 contacts strand β3 of the barrel domain, at a location somewhat similar to that of the N-terminal segment of the SMRT peptide in complex with SHARP SPOC domain (Fig 3A).	RESULTS
56	69	barrel domain	structure_element	Interestingly, a loop in Tas3 contacts strand β3 of the barrel domain, at a location somewhat similar to that of the N-terminal segment of the SMRT peptide in complex with SHARP SPOC domain (Fig 3A).	RESULTS
143	147	SMRT	protein	Interestingly, a loop in Tas3 contacts strand β3 of the barrel domain, at a location somewhat similar to that of the N-terminal segment of the SMRT peptide in complex with SHARP SPOC domain (Fig 3A).	RESULTS
148	155	peptide	chemical	Interestingly, a loop in Tas3 contacts strand β3 of the barrel domain, at a location somewhat similar to that of the N-terminal segment of the SMRT peptide in complex with SHARP SPOC domain (Fig 3A).	RESULTS
156	171	in complex with	protein_state	Interestingly, a loop in Tas3 contacts strand β3 of the barrel domain, at a location somewhat similar to that of the N-terminal segment of the SMRT peptide in complex with SHARP SPOC domain (Fig 3A).	RESULTS
172	177	SHARP	protein	Interestingly, a loop in Tas3 contacts strand β3 of the barrel domain, at a location somewhat similar to that of the N-terminal segment of the SMRT peptide in complex with SHARP SPOC domain (Fig 3A).	RESULTS
178	182	SPOC	structure_element	Interestingly, a loop in Tas3 contacts strand β3 of the barrel domain, at a location somewhat similar to that of the N-terminal segment of the SMRT peptide in complex with SHARP SPOC domain (Fig 3A).	RESULTS
0	8	Mediator	protein_type	Mediator is a coactivator complex that promotes transcription by Pol II.	RESULTS
65	71	Pol II	complex_assembly	Mediator is a coactivator complex that promotes transcription by Pol II.	RESULTS
4	9	Med25	protein	The Med25 subunit ACID is the target of the potent activator VP16 of the herpes simplex virus.	RESULTS
18	22	ACID	structure_element	The Med25 subunit ACID is the target of the potent activator VP16 of the herpes simplex virus.	RESULTS
61	65	VP16	protein	The Med25 subunit ACID is the target of the potent activator VP16 of the herpes simplex virus.	RESULTS
73	93	herpes simplex virus	species	The Med25 subunit ACID is the target of the potent activator VP16 of the herpes simplex virus.	RESULTS
4	13	structure	evidence	The structure of ACID contains a helix at the C-terminus as well as an extended β1-β2 loop.	RESULTS
17	21	ACID	structure_element	The structure of ACID contains a helix at the C-terminus as well as an extended β1-β2 loop.	RESULTS
33	38	helix	structure_element	The structure of ACID contains a helix at the C-terminus as well as an extended β1-β2 loop.	RESULTS
80	90	β1-β2 loop	structure_element	The structure of ACID contains a helix at the C-terminus as well as an extended β1-β2 loop.	RESULTS
17	29	binding site	site	Nonetheless, the binding site for VP16 has been mapped to roughly the same surface patch, near strands β1 and β3, that is used by the SHARP and Tas3 SPOC domains for binding their partners.	RESULTS
34	38	VP16	protein	Nonetheless, the binding site for VP16 has been mapped to roughly the same surface patch, near strands β1 and β3, that is used by the SHARP and Tas3 SPOC domains for binding their partners.	RESULTS
75	88	surface patch	site	Nonetheless, the binding site for VP16 has been mapped to roughly the same surface patch, near strands β1 and β3, that is used by the SHARP and Tas3 SPOC domains for binding their partners.	RESULTS
95	102	strands	structure_element	Nonetheless, the binding site for VP16 has been mapped to roughly the same surface patch, near strands β1 and β3, that is used by the SHARP and Tas3 SPOC domains for binding their partners.	RESULTS
103	105	β1	structure_element	Nonetheless, the binding site for VP16 has been mapped to roughly the same surface patch, near strands β1 and β3, that is used by the SHARP and Tas3 SPOC domains for binding their partners.	RESULTS
110	112	β3	structure_element	Nonetheless, the binding site for VP16 has been mapped to roughly the same surface patch, near strands β1 and β3, that is used by the SHARP and Tas3 SPOC domains for binding their partners.	RESULTS
134	139	SHARP	protein	Nonetheless, the binding site for VP16 has been mapped to roughly the same surface patch, near strands β1 and β3, that is used by the SHARP and Tas3 SPOC domains for binding their partners.	RESULTS
144	148	Tas3	protein	Nonetheless, the binding site for VP16 has been mapped to roughly the same surface patch, near strands β1 and β3, that is used by the SHARP and Tas3 SPOC domains for binding their partners.	RESULTS
149	153	SPOC	structure_element	Nonetheless, the binding site for VP16 has been mapped to roughly the same surface patch, near strands β1 and β3, that is used by the SHARP and Tas3 SPOC domains for binding their partners.	RESULTS
2	11	conserved	protein_state	A conserved surface patch in the FPA SPOC domain	RESULTS
12	25	surface patch	site	A conserved surface patch in the FPA SPOC domain	RESULTS
33	36	FPA	protein	A conserved surface patch in the FPA SPOC domain	RESULTS
37	41	SPOC	structure_element	A conserved surface patch in the FPA SPOC domain	RESULTS
19	23	SPOC	structure_element	An analysis of the SPOC domain indicates a large surface patch near strands β1, β3, β5 and β6 that is conserved among plant FPA homologs (Fig 4A).	RESULTS
49	62	surface patch	site	An analysis of the SPOC domain indicates a large surface patch near strands β1, β3, β5 and β6 that is conserved among plant FPA homologs (Fig 4A).	RESULTS
68	75	strands	structure_element	An analysis of the SPOC domain indicates a large surface patch near strands β1, β3, β5 and β6 that is conserved among plant FPA homologs (Fig 4A).	RESULTS
76	78	β1	structure_element	An analysis of the SPOC domain indicates a large surface patch near strands β1, β3, β5 and β6 that is conserved among plant FPA homologs (Fig 4A).	RESULTS
80	82	β3	structure_element	An analysis of the SPOC domain indicates a large surface patch near strands β1, β3, β5 and β6 that is conserved among plant FPA homologs (Fig 4A).	RESULTS
84	86	β5	structure_element	An analysis of the SPOC domain indicates a large surface patch near strands β1, β3, β5 and β6 that is conserved among plant FPA homologs (Fig 4A).	RESULTS
91	93	β6	structure_element	An analysis of the SPOC domain indicates a large surface patch near strands β1, β3, β5 and β6 that is conserved among plant FPA homologs (Fig 4A).	RESULTS
102	111	conserved	protein_state	An analysis of the SPOC domain indicates a large surface patch near strands β1, β3, β5 and β6 that is conserved among plant FPA homologs (Fig 4A).	RESULTS
118	123	plant	taxonomy_domain	An analysis of the SPOC domain indicates a large surface patch near strands β1, β3, β5 and β6 that is conserved among plant FPA homologs (Fig 4A).	RESULTS
124	127	FPA	protein	An analysis of the SPOC domain indicates a large surface patch near strands β1, β3, β5 and β6 that is conserved among plant FPA homologs (Fig 4A).	RESULTS
5	18	surface patch	site	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
42	53	sub-patches	site	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
69	75	Lys447	residue_name_number	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
80	86	strand	structure_element	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
87	89	β1	structure_element	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
92	98	Arg477	residue_name_number	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
100	102	β3	structure_element	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
105	111	Tyr515	residue_name_number	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
113	115	αB	structure_element	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
121	127	Arg521	residue_name_number	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
129	131	β5	structure_element	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
140	149	sub-patch	site	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
164	170	His486	residue_name_number	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
172	174	αA	structure_element	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
177	183	Thr478	residue_name_number	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
185	187	β3	structure_element	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
190	196	Val524	residue_name_number	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
198	200	β5	structure_element	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
206	212	Phe534	residue_name_number	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
214	216	β6	structure_element	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
231	240	sub-patch	site	This surface patch can be broken into two sub-patches, with residues Lys447 (in strand β1), Arg477 (β3), Tyr515 (αB) and Arg521 (β5) in one sub-patch, and residues His486 (αA), Thr478 (β3), Val524 (β5) and Phe534 (β6) in the other sub-patch (Fig 4B).	RESULTS
4	23	first surface patch	site	The first surface patch is electropositive in nature (Fig 4C), and residues Arg477 and Tyr515 are also conserved in the SHARP SPOC domain (Fig 1B).	RESULTS
27	42	electropositive	protein_state	The first surface patch is electropositive in nature (Fig 4C), and residues Arg477 and Tyr515 are also conserved in the SHARP SPOC domain (Fig 1B).	RESULTS
76	82	Arg477	residue_name_number	The first surface patch is electropositive in nature (Fig 4C), and residues Arg477 and Tyr515 are also conserved in the SHARP SPOC domain (Fig 1B).	RESULTS
87	93	Tyr515	residue_name_number	The first surface patch is electropositive in nature (Fig 4C), and residues Arg477 and Tyr515 are also conserved in the SHARP SPOC domain (Fig 1B).	RESULTS
103	112	conserved	protein_state	The first surface patch is electropositive in nature (Fig 4C), and residues Arg477 and Tyr515 are also conserved in the SHARP SPOC domain (Fig 1B).	RESULTS
120	125	SHARP	protein	The first surface patch is electropositive in nature (Fig 4C), and residues Arg477 and Tyr515 are also conserved in the SHARP SPOC domain (Fig 1B).	RESULTS
126	130	SPOC	structure_element	The first surface patch is electropositive in nature (Fig 4C), and residues Arg477 and Tyr515 are also conserved in the SHARP SPOC domain (Fig 1B).	RESULTS
20	34	phosphorylated	protein_state	In fact, one of the phosphorylated residues of the SMRT peptide interacts with this surface patch (Fig 3A), suggesting that the FPA SPOC domain might also interact with a phosphorylated segment here.	RESULTS
51	55	SMRT	protein	In fact, one of the phosphorylated residues of the SMRT peptide interacts with this surface patch (Fig 3A), suggesting that the FPA SPOC domain might also interact with a phosphorylated segment here.	RESULTS
56	63	peptide	chemical	In fact, one of the phosphorylated residues of the SMRT peptide interacts with this surface patch (Fig 3A), suggesting that the FPA SPOC domain might also interact with a phosphorylated segment here.	RESULTS
84	97	surface patch	site	In fact, one of the phosphorylated residues of the SMRT peptide interacts with this surface patch (Fig 3A), suggesting that the FPA SPOC domain might also interact with a phosphorylated segment here.	RESULTS
128	131	FPA	protein	In fact, one of the phosphorylated residues of the SMRT peptide interacts with this surface patch (Fig 3A), suggesting that the FPA SPOC domain might also interact with a phosphorylated segment here.	RESULTS
132	136	SPOC	structure_element	In fact, one of the phosphorylated residues of the SMRT peptide interacts with this surface patch (Fig 3A), suggesting that the FPA SPOC domain might also interact with a phosphorylated segment here.	RESULTS
171	185	phosphorylated	protein_state	In fact, one of the phosphorylated residues of the SMRT peptide interacts with this surface patch (Fig 3A), suggesting that the FPA SPOC domain might also interact with a phosphorylated segment here.	RESULTS
19	39	second surface patch	site	In comparison, the second surface patch is more hydrophobic in nature (Fig 4C).	RESULTS
48	59	hydrophobic	protein_state	In comparison, the second surface patch is more hydrophobic in nature (Fig 4C).	RESULTS
2	11	conserved	protein_state	A conserved surface patch of FPA SPOC domain.	FIG
12	25	surface patch	site	A conserved surface patch of FPA SPOC domain.	FIG
29	32	FPA	protein	A conserved surface patch of FPA SPOC domain.	FIG
33	37	SPOC	structure_element	A conserved surface patch of FPA SPOC domain.	FIG
38	41	FPA	protein	Two views of the molecular surface of FPA SPOC domain colored based on sequence conservation among plant FPA homologs.	FIG
42	46	SPOC	structure_element	Two views of the molecular surface of FPA SPOC domain colored based on sequence conservation among plant FPA homologs.	FIG
99	104	plant	taxonomy_domain	Two views of the molecular surface of FPA SPOC domain colored based on sequence conservation among plant FPA homologs.	FIG
105	108	FPA	protein	Two views of the molecular surface of FPA SPOC domain colored based on sequence conservation among plant FPA homologs.	FIG
16	25	conserved	protein_state	Residues in the conserved surface patch of FPA SPOC domain.	FIG
26	39	surface patch	site	Residues in the conserved surface patch of FPA SPOC domain.	FIG
43	46	FPA	protein	Residues in the conserved surface patch of FPA SPOC domain.	FIG
47	51	SPOC	structure_element	Residues in the conserved surface patch of FPA SPOC domain.	FIG
81	96	first sub-patch	site	The side chains of the residues are shown in stick models, colored orange in the first sub-patch and green in the second. (C).	FIG
21	24	FPA	protein	Molecular surface of FPA SPOC domain colored based on electrostatic potential.	FIG
25	29	SPOC	structure_element	Molecular surface of FPA SPOC domain colored based on electrostatic potential.	FIG
62	65	FPA	protein	Testing the requirement of specific conserved amino acids for FPA functions	RESULTS
45	54	conserved	protein_state	We next examined the potential impact of the conserved surface patch on FPA function in vivo.	RESULTS
55	68	surface patch	site	We next examined the potential impact of the conserved surface patch on FPA function in vivo.	RESULTS
72	75	FPA	protein	We next examined the potential impact of the conserved surface patch on FPA function in vivo.	RESULTS
3	10	mutated	experimental_method	We mutated two residues, Arg477 and Tyr515, of the surface patch, which are also conserved in the SHARP SPOC domain (Fig 1B) and were found to be functionally important.	RESULTS
25	31	Arg477	residue_name_number	We mutated two residues, Arg477 and Tyr515, of the surface patch, which are also conserved in the SHARP SPOC domain (Fig 1B) and were found to be functionally important.	RESULTS
36	42	Tyr515	residue_name_number	We mutated two residues, Arg477 and Tyr515, of the surface patch, which are also conserved in the SHARP SPOC domain (Fig 1B) and were found to be functionally important.	RESULTS
51	64	surface patch	site	We mutated two residues, Arg477 and Tyr515, of the surface patch, which are also conserved in the SHARP SPOC domain (Fig 1B) and were found to be functionally important.	RESULTS
81	90	conserved	protein_state	We mutated two residues, Arg477 and Tyr515, of the surface patch, which are also conserved in the SHARP SPOC domain (Fig 1B) and were found to be functionally important.	RESULTS
98	103	SHARP	protein	We mutated two residues, Arg477 and Tyr515, of the surface patch, which are also conserved in the SHARP SPOC domain (Fig 1B) and were found to be functionally important.	RESULTS
104	108	SPOC	structure_element	We mutated two residues, Arg477 and Tyr515, of the surface patch, which are also conserved in the SHARP SPOC domain (Fig 1B) and were found to be functionally important.	RESULTS
4	13	mutations	experimental_method	The mutations were introduced into a transgene designed to express FPA from its native control elements (promoter, introns and 3′ UTR).	RESULTS
19	29	introduced	experimental_method	The mutations were introduced into a transgene designed to express FPA from its native control elements (promoter, introns and 3′ UTR).	RESULTS
67	70	FPA	protein	The mutations were introduced into a transgene designed to express FPA from its native control elements (promoter, introns and 3′ UTR).	RESULTS
35	53	stably transformed	experimental_method	The resulting transgenes were then stably transformed into an fpa-8 mutant background so that the impact of the mutations on FPA function could be assessed.	RESULTS
62	67	fpa-8	gene	The resulting transgenes were then stably transformed into an fpa-8 mutant background so that the impact of the mutations on FPA function could be assessed.	RESULTS
68	74	mutant	protein_state	The resulting transgenes were then stably transformed into an fpa-8 mutant background so that the impact of the mutations on FPA function could be assessed.	RESULTS
112	121	mutations	experimental_method	The resulting transgenes were then stably transformed into an fpa-8 mutant background so that the impact of the mutations on FPA function could be assessed.	RESULTS
125	128	FPA	protein	The resulting transgenes were then stably transformed into an fpa-8 mutant background so that the impact of the mutations on FPA function could be assessed.	RESULTS
35	56	expression constructs	experimental_method	Control transformation of the same expression constructs into fpa-8 designed to express wild-type FPA protein restored FPA protein expression levels to near wild-type levels (panel A in S1 Fig) and rescued the function of FPA in controlling RNA 3′-end formation, for example in FPA pre-mRNA (panel B in S1 Fig).	RESULTS
62	67	fpa-8	gene	Control transformation of the same expression constructs into fpa-8 designed to express wild-type FPA protein restored FPA protein expression levels to near wild-type levels (panel A in S1 Fig) and rescued the function of FPA in controlling RNA 3′-end formation, for example in FPA pre-mRNA (panel B in S1 Fig).	RESULTS
88	97	wild-type	protein_state	Control transformation of the same expression constructs into fpa-8 designed to express wild-type FPA protein restored FPA protein expression levels to near wild-type levels (panel A in S1 Fig) and rescued the function of FPA in controlling RNA 3′-end formation, for example in FPA pre-mRNA (panel B in S1 Fig).	RESULTS
98	101	FPA	protein	Control transformation of the same expression constructs into fpa-8 designed to express wild-type FPA protein restored FPA protein expression levels to near wild-type levels (panel A in S1 Fig) and rescued the function of FPA in controlling RNA 3′-end formation, for example in FPA pre-mRNA (panel B in S1 Fig).	RESULTS
119	122	FPA	protein	Control transformation of the same expression constructs into fpa-8 designed to express wild-type FPA protein restored FPA protein expression levels to near wild-type levels (panel A in S1 Fig) and rescued the function of FPA in controlling RNA 3′-end formation, for example in FPA pre-mRNA (panel B in S1 Fig).	RESULTS
131	148	expression levels	evidence	Control transformation of the same expression constructs into fpa-8 designed to express wild-type FPA protein restored FPA protein expression levels to near wild-type levels (panel A in S1 Fig) and rescued the function of FPA in controlling RNA 3′-end formation, for example in FPA pre-mRNA (panel B in S1 Fig).	RESULTS
157	166	wild-type	protein_state	Control transformation of the same expression constructs into fpa-8 designed to express wild-type FPA protein restored FPA protein expression levels to near wild-type levels (panel A in S1 Fig) and rescued the function of FPA in controlling RNA 3′-end formation, for example in FPA pre-mRNA (panel B in S1 Fig).	RESULTS
222	225	FPA	protein	Control transformation of the same expression constructs into fpa-8 designed to express wild-type FPA protein restored FPA protein expression levels to near wild-type levels (panel A in S1 Fig) and rescued the function of FPA in controlling RNA 3′-end formation, for example in FPA pre-mRNA (panel B in S1 Fig).	RESULTS
241	244	RNA	chemical	Control transformation of the same expression constructs into fpa-8 designed to express wild-type FPA protein restored FPA protein expression levels to near wild-type levels (panel A in S1 Fig) and rescued the function of FPA in controlling RNA 3′-end formation, for example in FPA pre-mRNA (panel B in S1 Fig).	RESULTS
278	281	FPA	protein	Control transformation of the same expression constructs into fpa-8 designed to express wild-type FPA protein restored FPA protein expression levels to near wild-type levels (panel A in S1 Fig) and rescued the function of FPA in controlling RNA 3′-end formation, for example in FPA pre-mRNA (panel B in S1 Fig).	RESULTS
282	290	pre-mRNA	chemical	Control transformation of the same expression constructs into fpa-8 designed to express wild-type FPA protein restored FPA protein expression levels to near wild-type levels (panel A in S1 Fig) and rescued the function of FPA in controlling RNA 3′-end formation, for example in FPA pre-mRNA (panel B in S1 Fig).	RESULTS
57	62	R477A	mutant	We examined independent transgenic lines expressing each R477A and Y515A mutation.	RESULTS
67	72	Y515A	mutant	We examined independent transgenic lines expressing each R477A and Y515A mutation.	RESULTS
73	81	mutation	experimental_method	We examined independent transgenic lines expressing each R477A and Y515A mutation.	RESULTS
53	56	FPA	protein	In each case, we confirmed that detectable levels of FPA protein expression were restored close to wild-type levels in protein blot analyses using antibodies that specifically recognize FPA (S2 Fig).	RESULTS
99	108	wild-type	protein_state	In each case, we confirmed that detectable levels of FPA protein expression were restored close to wild-type levels in protein blot analyses using antibodies that specifically recognize FPA (S2 Fig).	RESULTS
119	131	protein blot	experimental_method	In each case, we confirmed that detectable levels of FPA protein expression were restored close to wild-type levels in protein blot analyses using antibodies that specifically recognize FPA (S2 Fig).	RESULTS
186	189	FPA	protein	In each case, we confirmed that detectable levels of FPA protein expression were restored close to wild-type levels in protein blot analyses using antibodies that specifically recognize FPA (S2 Fig).	RESULTS
35	48	surface patch	site	We then examined the impact of the surface patch mutations on FPA’s function in controlling RNA 3′-end formation by determining whether the mutant proteins functioned in FPA autoregulation and the repression of FLC expression.	RESULTS
49	58	mutations	experimental_method	We then examined the impact of the surface patch mutations on FPA’s function in controlling RNA 3′-end formation by determining whether the mutant proteins functioned in FPA autoregulation and the repression of FLC expression.	RESULTS
62	65	FPA	protein	We then examined the impact of the surface patch mutations on FPA’s function in controlling RNA 3′-end formation by determining whether the mutant proteins functioned in FPA autoregulation and the repression of FLC expression.	RESULTS
140	146	mutant	protein_state	We then examined the impact of the surface patch mutations on FPA’s function in controlling RNA 3′-end formation by determining whether the mutant proteins functioned in FPA autoregulation and the repression of FLC expression.	RESULTS
170	173	FPA	protein	We then examined the impact of the surface patch mutations on FPA’s function in controlling RNA 3′-end formation by determining whether the mutant proteins functioned in FPA autoregulation and the repression of FLC expression.	RESULTS
211	214	FLC	gene	We then examined the impact of the surface patch mutations on FPA’s function in controlling RNA 3′-end formation by determining whether the mutant proteins functioned in FPA autoregulation and the repression of FLC expression.	RESULTS
0	3	FPA	protein	FPA autoregulates its expression by promoting cleavage and polyadenylation within intron 1 of its own pre-mRNA, resulting in a truncated transcript that does not encode functional protein.	RESULTS
102	110	pre-mRNA	chemical	FPA autoregulates its expression by promoting cleavage and polyadenylation within intron 1 of its own pre-mRNA, resulting in a truncated transcript that does not encode functional protein.	RESULTS
8	29	RNA gel blot analyses	experimental_method	We used RNA gel blot analyses to reveal that in each of three independent transgenic lines for each single mutant, rescue of proximally polyadenylated FPA pre-mRNA can be detected (Fig 5A and 5B).	RESULTS
107	113	mutant	protein_state	We used RNA gel blot analyses to reveal that in each of three independent transgenic lines for each single mutant, rescue of proximally polyadenylated FPA pre-mRNA can be detected (Fig 5A and 5B).	RESULTS
151	154	FPA	protein	We used RNA gel blot analyses to reveal that in each of three independent transgenic lines for each single mutant, rescue of proximally polyadenylated FPA pre-mRNA can be detected (Fig 5A and 5B).	RESULTS
155	163	pre-mRNA	chemical	We used RNA gel blot analyses to reveal that in each of three independent transgenic lines for each single mutant, rescue of proximally polyadenylated FPA pre-mRNA can be detected (Fig 5A and 5B).	RESULTS
79	82	FPA	protein	We therefore conclude that neither of these mutations disrupted the ability of FPA to promote RNA 3′-end formation in its own transcript.	RESULTS
21	24	FPA	protein	Impact of individual FPA SPOC domain mutations on alternative polyadenylation of FPA pre-mRNA.	FIG
25	29	SPOC	structure_element	Impact of individual FPA SPOC domain mutations on alternative polyadenylation of FPA pre-mRNA.	FIG
37	46	mutations	experimental_method	Impact of individual FPA SPOC domain mutations on alternative polyadenylation of FPA pre-mRNA.	FIG
81	84	FPA	protein	Impact of individual FPA SPOC domain mutations on alternative polyadenylation of FPA pre-mRNA.	FIG
85	93	pre-mRNA	chemical	Impact of individual FPA SPOC domain mutations on alternative polyadenylation of FPA pre-mRNA.	FIG
0	12	RNA gel blot	experimental_method	RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing either FPA::FPA R477A (A), or FPA::FPA Y515A (B) using poly(A)+ purified mRNAs.	FIG
25	27	WT	protein_state	RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing either FPA::FPA R477A (A), or FPA::FPA Y515A (B) using poly(A)+ purified mRNAs.	FIG
28	39	A. thaliana	species	RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing either FPA::FPA R477A (A), or FPA::FPA Y515A (B) using poly(A)+ purified mRNAs.	FIG
67	73	plants	taxonomy_domain	RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing either FPA::FPA R477A (A), or FPA::FPA Y515A (B) using poly(A)+ purified mRNAs.	FIG
74	79	fpa-8	gene	RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing either FPA::FPA R477A (A), or FPA::FPA Y515A (B) using poly(A)+ purified mRNAs.	FIG
84	89	fpa-8	gene	RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing either FPA::FPA R477A (A), or FPA::FPA Y515A (B) using poly(A)+ purified mRNAs.	FIG
90	97	mutants	protein_state	RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing either FPA::FPA R477A (A), or FPA::FPA Y515A (B) using poly(A)+ purified mRNAs.	FIG
116	119	FPA	protein	RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing either FPA::FPA R477A (A), or FPA::FPA Y515A (B) using poly(A)+ purified mRNAs.	FIG
121	130	FPA R477A	mutant	RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing either FPA::FPA R477A (A), or FPA::FPA Y515A (B) using poly(A)+ purified mRNAs.	FIG
139	142	FPA	protein	RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing either FPA::FPA R477A (A), or FPA::FPA Y515A (B) using poly(A)+ purified mRNAs.	FIG
144	153	FPA Y515A	mutant	RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing either FPA::FPA R477A (A), or FPA::FPA Y515A (B) using poly(A)+ purified mRNAs.	FIG
182	187	mRNAs	chemical	RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing either FPA::FPA R477A (A), or FPA::FPA Y515A (B) using poly(A)+ purified mRNAs.	FIG
45	48	FPA	protein	A probe corresponding to the 5’UTR region of FPA mRNA was used to detect FPA specific mRNAs.	FIG
49	53	mRNA	chemical	A probe corresponding to the 5’UTR region of FPA mRNA was used to detect FPA specific mRNAs.	FIG
73	76	FPA	protein	A probe corresponding to the 5’UTR region of FPA mRNA was used to detect FPA specific mRNAs.	FIG
86	91	mRNAs	chemical	A probe corresponding to the 5’UTR region of FPA mRNA was used to detect FPA specific mRNAs.	FIG
45	48	FPA	protein	A probe corresponding to the 5’UTR region of FPA mRNA was used to detect FPA specific mRNAs.	FIG
49	53	mRNA	chemical	A probe corresponding to the 5’UTR region of FPA mRNA was used to detect FPA specific mRNAs.	FIG
73	76	FPA	protein	A probe corresponding to the 5’UTR region of FPA mRNA was used to detect FPA specific mRNAs.	FIG
86	91	mRNAs	chemical	A probe corresponding to the 5’UTR region of FPA mRNA was used to detect FPA specific mRNAs.	FIG
39	42	FPA	protein	Proximally and distally polyadenylated FPA transcripts are marked with arrows.	FIG
103	106	FPA	protein	The ratio of distal:proximal polyadenylated forms is given under each lane. (C,D) Impact of individual FPA SPOC domain mutations on FLC transcript levels.	FIG
107	111	SPOC	structure_element	The ratio of distal:proximal polyadenylated forms is given under each lane. (C,D) Impact of individual FPA SPOC domain mutations on FLC transcript levels.	FIG
119	128	mutations	experimental_method	The ratio of distal:proximal polyadenylated forms is given under each lane. (C,D) Impact of individual FPA SPOC domain mutations on FLC transcript levels.	FIG
132	135	FLC	gene	The ratio of distal:proximal polyadenylated forms is given under each lane. (C,D) Impact of individual FPA SPOC domain mutations on FLC transcript levels.	FIG
0	7	qRT-PCR	experimental_method	qRT-PCR analysis was performed with total RNA purified from Col-0, fpa-8, 35S::FPA:YFP and FPA::FPA R477A (C), FPA::FPA Y515A (D) plants.	FIG
42	45	RNA	chemical	qRT-PCR analysis was performed with total RNA purified from Col-0, fpa-8, 35S::FPA:YFP and FPA::FPA R477A (C), FPA::FPA Y515A (D) plants.	FIG
67	72	fpa-8	gene	qRT-PCR analysis was performed with total RNA purified from Col-0, fpa-8, 35S::FPA:YFP and FPA::FPA R477A (C), FPA::FPA Y515A (D) plants.	FIG
79	82	FPA	protein	qRT-PCR analysis was performed with total RNA purified from Col-0, fpa-8, 35S::FPA:YFP and FPA::FPA R477A (C), FPA::FPA Y515A (D) plants.	FIG
83	86	YFP	experimental_method	qRT-PCR analysis was performed with total RNA purified from Col-0, fpa-8, 35S::FPA:YFP and FPA::FPA R477A (C), FPA::FPA Y515A (D) plants.	FIG
91	94	FPA	protein	qRT-PCR analysis was performed with total RNA purified from Col-0, fpa-8, 35S::FPA:YFP and FPA::FPA R477A (C), FPA::FPA Y515A (D) plants.	FIG
96	105	FPA R477A	mutant	qRT-PCR analysis was performed with total RNA purified from Col-0, fpa-8, 35S::FPA:YFP and FPA::FPA R477A (C), FPA::FPA Y515A (D) plants.	FIG
111	114	FPA	protein	qRT-PCR analysis was performed with total RNA purified from Col-0, fpa-8, 35S::FPA:YFP and FPA::FPA R477A (C), FPA::FPA Y515A (D) plants.	FIG
116	125	FPA Y515A	mutant	qRT-PCR analysis was performed with total RNA purified from Col-0, fpa-8, 35S::FPA:YFP and FPA::FPA R477A (C), FPA::FPA Y515A (D) plants.	FIG
130	136	plants	taxonomy_domain	qRT-PCR analysis was performed with total RNA purified from Col-0, fpa-8, 35S::FPA:YFP and FPA::FPA R477A (C), FPA::FPA Y515A (D) plants.	FIG
0	10	Histograms	evidence	Histograms show mean values ±SE for three independent PCR amplifications of three biological replicates.	FIG
54	57	PCR	experimental_method	Histograms show mean values ±SE for three independent PCR amplifications of three biological replicates.	FIG
0	10	Histograms	evidence	Histograms show mean values ±SE for three independent PCR amplifications of three biological replicates.	FIG
54	57	PCR	experimental_method	Histograms show mean values ±SE for three independent PCR amplifications of three biological replicates.	FIG
78	81	FPA	protein	We next examined whether the corresponding mutations disrupted the ability of FPA to control FLC expression.	RESULTS
93	96	FLC	gene	We next examined whether the corresponding mutations disrupted the ability of FPA to control FLC expression.	RESULTS
8	15	RT-qPCR	experimental_method	We used RT-qPCR to measure the expression of FLC mRNA and found that in each independent transgenic line encoding each mutated FPA protein, the elevated levels of FLC detected in fpa-8 mutants were restored to near wild-type levels by expression of the FPA SPOC conserved patch mutant proteins (Fig 5C and 5D).	RESULTS
45	48	FLC	gene	We used RT-qPCR to measure the expression of FLC mRNA and found that in each independent transgenic line encoding each mutated FPA protein, the elevated levels of FLC detected in fpa-8 mutants were restored to near wild-type levels by expression of the FPA SPOC conserved patch mutant proteins (Fig 5C and 5D).	RESULTS
49	53	mRNA	chemical	We used RT-qPCR to measure the expression of FLC mRNA and found that in each independent transgenic line encoding each mutated FPA protein, the elevated levels of FLC detected in fpa-8 mutants were restored to near wild-type levels by expression of the FPA SPOC conserved patch mutant proteins (Fig 5C and 5D).	RESULTS
119	126	mutated	protein_state	We used RT-qPCR to measure the expression of FLC mRNA and found that in each independent transgenic line encoding each mutated FPA protein, the elevated levels of FLC detected in fpa-8 mutants were restored to near wild-type levels by expression of the FPA SPOC conserved patch mutant proteins (Fig 5C and 5D).	RESULTS
127	130	FPA	protein	We used RT-qPCR to measure the expression of FLC mRNA and found that in each independent transgenic line encoding each mutated FPA protein, the elevated levels of FLC detected in fpa-8 mutants were restored to near wild-type levels by expression of the FPA SPOC conserved patch mutant proteins (Fig 5C and 5D).	RESULTS
163	166	FLC	gene	We used RT-qPCR to measure the expression of FLC mRNA and found that in each independent transgenic line encoding each mutated FPA protein, the elevated levels of FLC detected in fpa-8 mutants were restored to near wild-type levels by expression of the FPA SPOC conserved patch mutant proteins (Fig 5C and 5D).	RESULTS
179	184	fpa-8	gene	We used RT-qPCR to measure the expression of FLC mRNA and found that in each independent transgenic line encoding each mutated FPA protein, the elevated levels of FLC detected in fpa-8 mutants were restored to near wild-type levels by expression of the FPA SPOC conserved patch mutant proteins (Fig 5C and 5D).	RESULTS
185	192	mutants	protein_state	We used RT-qPCR to measure the expression of FLC mRNA and found that in each independent transgenic line encoding each mutated FPA protein, the elevated levels of FLC detected in fpa-8 mutants were restored to near wild-type levels by expression of the FPA SPOC conserved patch mutant proteins (Fig 5C and 5D).	RESULTS
215	224	wild-type	protein_state	We used RT-qPCR to measure the expression of FLC mRNA and found that in each independent transgenic line encoding each mutated FPA protein, the elevated levels of FLC detected in fpa-8 mutants were restored to near wild-type levels by expression of the FPA SPOC conserved patch mutant proteins (Fig 5C and 5D).	RESULTS
253	256	FPA	protein	We used RT-qPCR to measure the expression of FLC mRNA and found that in each independent transgenic line encoding each mutated FPA protein, the elevated levels of FLC detected in fpa-8 mutants were restored to near wild-type levels by expression of the FPA SPOC conserved patch mutant proteins (Fig 5C and 5D).	RESULTS
257	261	SPOC	structure_element	We used RT-qPCR to measure the expression of FLC mRNA and found that in each independent transgenic line encoding each mutated FPA protein, the elevated levels of FLC detected in fpa-8 mutants were restored to near wild-type levels by expression of the FPA SPOC conserved patch mutant proteins (Fig 5C and 5D).	RESULTS
262	271	conserved	protein_state	We used RT-qPCR to measure the expression of FLC mRNA and found that in each independent transgenic line encoding each mutated FPA protein, the elevated levels of FLC detected in fpa-8 mutants were restored to near wild-type levels by expression of the FPA SPOC conserved patch mutant proteins (Fig 5C and 5D).	RESULTS
272	277	patch	site	We used RT-qPCR to measure the expression of FLC mRNA and found that in each independent transgenic line encoding each mutated FPA protein, the elevated levels of FLC detected in fpa-8 mutants were restored to near wild-type levels by expression of the FPA SPOC conserved patch mutant proteins (Fig 5C and 5D).	RESULTS
278	284	mutant	protein_state	We used RT-qPCR to measure the expression of FLC mRNA and found that in each independent transgenic line encoding each mutated FPA protein, the elevated levels of FLC detected in fpa-8 mutants were restored to near wild-type levels by expression of the FPA SPOC conserved patch mutant proteins (Fig 5C and 5D).	RESULTS
11	24	surface patch	site	Since each surface patch mutation appeared to be insufficient to disrupt FPA functions on its own, we combined both mutations into the same transgene.	RESULTS
25	33	mutation	experimental_method	Since each surface patch mutation appeared to be insufficient to disrupt FPA functions on its own, we combined both mutations into the same transgene.	RESULTS
73	76	FPA	protein	Since each surface patch mutation appeared to be insufficient to disrupt FPA functions on its own, we combined both mutations into the same transgene.	RESULTS
33	42	wild-type	protein_state	We could again confirm that near wild-type levels of FPA protein were expressed from three independent transgenic lines expressing the FPA R477A;Y515A doubly mutated protein in an fpa-8 mutant background (S3 Fig).	RESULTS
53	56	FPA	protein	We could again confirm that near wild-type levels of FPA protein were expressed from three independent transgenic lines expressing the FPA R477A;Y515A doubly mutated protein in an fpa-8 mutant background (S3 Fig).	RESULTS
135	150	FPA R477A;Y515A	mutant	We could again confirm that near wild-type levels of FPA protein were expressed from three independent transgenic lines expressing the FPA R477A;Y515A doubly mutated protein in an fpa-8 mutant background (S3 Fig).	RESULTS
151	165	doubly mutated	protein_state	We could again confirm that near wild-type levels of FPA protein were expressed from three independent transgenic lines expressing the FPA R477A;Y515A doubly mutated protein in an fpa-8 mutant background (S3 Fig).	RESULTS
180	185	fpa-8	gene	We could again confirm that near wild-type levels of FPA protein were expressed from three independent transgenic lines expressing the FPA R477A;Y515A doubly mutated protein in an fpa-8 mutant background (S3 Fig).	RESULTS
186	192	mutant	protein_state	We could again confirm that near wild-type levels of FPA protein were expressed from three independent transgenic lines expressing the FPA R477A;Y515A doubly mutated protein in an fpa-8 mutant background (S3 Fig).	RESULTS
14	29	FPA R477A;Y515A	mutant	We found that FPA R477A;Y515A protein functioned like wild-type FPA to restore FPA pre-mRNA proximal polyadenylation (Fig 6A) and FLC expression to wild-type levels (Fig 6B).	RESULTS
54	63	wild-type	protein_state	We found that FPA R477A;Y515A protein functioned like wild-type FPA to restore FPA pre-mRNA proximal polyadenylation (Fig 6A) and FLC expression to wild-type levels (Fig 6B).	RESULTS
64	67	FPA	protein	We found that FPA R477A;Y515A protein functioned like wild-type FPA to restore FPA pre-mRNA proximal polyadenylation (Fig 6A) and FLC expression to wild-type levels (Fig 6B).	RESULTS
79	82	FPA	protein	We found that FPA R477A;Y515A protein functioned like wild-type FPA to restore FPA pre-mRNA proximal polyadenylation (Fig 6A) and FLC expression to wild-type levels (Fig 6B).	RESULTS
83	91	pre-mRNA	chemical	We found that FPA R477A;Y515A protein functioned like wild-type FPA to restore FPA pre-mRNA proximal polyadenylation (Fig 6A) and FLC expression to wild-type levels (Fig 6B).	RESULTS
130	133	FLC	gene	We found that FPA R477A;Y515A protein functioned like wild-type FPA to restore FPA pre-mRNA proximal polyadenylation (Fig 6A) and FLC expression to wild-type levels (Fig 6B).	RESULTS
148	157	wild-type	protein_state	We found that FPA R477A;Y515A protein functioned like wild-type FPA to restore FPA pre-mRNA proximal polyadenylation (Fig 6A) and FLC expression to wild-type levels (Fig 6B).	RESULTS
17	20	FPA	protein	Impact of double FPA SPOC domain mutations on alternative polyadenylation of FPA pre-mRNA and FLC expression.	FIG
21	25	SPOC	structure_element	Impact of double FPA SPOC domain mutations on alternative polyadenylation of FPA pre-mRNA and FLC expression.	FIG
33	42	mutations	experimental_method	Impact of double FPA SPOC domain mutations on alternative polyadenylation of FPA pre-mRNA and FLC expression.	FIG
77	80	FPA	protein	Impact of double FPA SPOC domain mutations on alternative polyadenylation of FPA pre-mRNA and FLC expression.	FIG
81	89	pre-mRNA	chemical	Impact of double FPA SPOC domain mutations on alternative polyadenylation of FPA pre-mRNA and FLC expression.	FIG
94	97	FLC	gene	Impact of double FPA SPOC domain mutations on alternative polyadenylation of FPA pre-mRNA and FLC expression.	FIG
4	16	RNA gel blot	experimental_method	(A) RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing FPA::FPA R477A;Y515A using poly(A)+ purified mRNAs.	FIG
29	31	WT	protein_state	(A) RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing FPA::FPA R477A;Y515A using poly(A)+ purified mRNAs.	FIG
32	43	A. thaliana	species	(A) RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing FPA::FPA R477A;Y515A using poly(A)+ purified mRNAs.	FIG
71	77	plants	taxonomy_domain	(A) RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing FPA::FPA R477A;Y515A using poly(A)+ purified mRNAs.	FIG
78	83	fpa-8	gene	(A) RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing FPA::FPA R477A;Y515A using poly(A)+ purified mRNAs.	FIG
88	93	fpa-8	gene	(A) RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing FPA::FPA R477A;Y515A using poly(A)+ purified mRNAs.	FIG
94	101	mutants	protein_state	(A) RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing FPA::FPA R477A;Y515A using poly(A)+ purified mRNAs.	FIG
113	116	FPA	protein	(A) RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing FPA::FPA R477A;Y515A using poly(A)+ purified mRNAs.	FIG
118	133	FPA R477A;Y515A	mutant	(A) RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing FPA::FPA R477A;Y515A using poly(A)+ purified mRNAs.	FIG
158	163	mRNAs	chemical	(A) RNA gel blot analysis of WT A. thaliana accession Columbia (Col-0) plants fpa-8 and fpa-8 mutants expressing FPA::FPA R477A;Y515A using poly(A)+ purified mRNAs.	FIG
65	68	FPA	protein	Black arrows indicate the proximally and distally polyadenylated FPA mRNAs.	FIG
69	74	mRNAs	chemical	Black arrows indicate the proximally and distally polyadenylated FPA mRNAs.	FIG
0	7	qRT-PCR	experimental_method	qRT-PCR analysis was performed with total RNA purified from Col-0, fpa-8, and FPA::FPA R477A;Y515A plants.	FIG
42	45	RNA	chemical	qRT-PCR analysis was performed with total RNA purified from Col-0, fpa-8, and FPA::FPA R477A;Y515A plants.	FIG
67	72	fpa-8	gene	qRT-PCR analysis was performed with total RNA purified from Col-0, fpa-8, and FPA::FPA R477A;Y515A plants.	FIG
78	81	FPA	protein	qRT-PCR analysis was performed with total RNA purified from Col-0, fpa-8, and FPA::FPA R477A;Y515A plants.	FIG
83	98	FPA R477A;Y515A	mutant	qRT-PCR analysis was performed with total RNA purified from Col-0, fpa-8, and FPA::FPA R477A;Y515A plants.	FIG
99	105	plants	taxonomy_domain	qRT-PCR analysis was performed with total RNA purified from Col-0, fpa-8, and FPA::FPA R477A;Y515A plants.	FIG
46	50	SPOC	structure_element	Together our findings suggest that either the SPOC domain is not required for the role of FPA in regulating RNA 3′-end formation, or that this combination of mutations is not sufficient to critically disrupt the function of the FPA SPOC domain.	RESULTS
90	93	FPA	protein	Together our findings suggest that either the SPOC domain is not required for the role of FPA in regulating RNA 3′-end formation, or that this combination of mutations is not sufficient to critically disrupt the function of the FPA SPOC domain.	RESULTS
108	111	RNA	chemical	Together our findings suggest that either the SPOC domain is not required for the role of FPA in regulating RNA 3′-end formation, or that this combination of mutations is not sufficient to critically disrupt the function of the FPA SPOC domain.	RESULTS
158	167	mutations	experimental_method	Together our findings suggest that either the SPOC domain is not required for the role of FPA in regulating RNA 3′-end formation, or that this combination of mutations is not sufficient to critically disrupt the function of the FPA SPOC domain.	RESULTS
228	231	FPA	protein	Together our findings suggest that either the SPOC domain is not required for the role of FPA in regulating RNA 3′-end formation, or that this combination of mutations is not sufficient to critically disrupt the function of the FPA SPOC domain.	RESULTS
232	236	SPOC	structure_element	Together our findings suggest that either the SPOC domain is not required for the role of FPA in regulating RNA 3′-end formation, or that this combination of mutations is not sufficient to critically disrupt the function of the FPA SPOC domain.	RESULTS
24	33	mutations	experimental_method	Since the corresponding mutations in the SHARP SPOC domain do disrupt its recognition of unphosphorylated SMRT peptides, these observations may reinforce the idea that the features and functions of the FPA SPOC domain differ from those of the only other well-characterized SPOC domain.	RESULTS
41	46	SHARP	protein	Since the corresponding mutations in the SHARP SPOC domain do disrupt its recognition of unphosphorylated SMRT peptides, these observations may reinforce the idea that the features and functions of the FPA SPOC domain differ from those of the only other well-characterized SPOC domain.	RESULTS
47	51	SPOC	structure_element	Since the corresponding mutations in the SHARP SPOC domain do disrupt its recognition of unphosphorylated SMRT peptides, these observations may reinforce the idea that the features and functions of the FPA SPOC domain differ from those of the only other well-characterized SPOC domain.	RESULTS
89	105	unphosphorylated	protein_state	Since the corresponding mutations in the SHARP SPOC domain do disrupt its recognition of unphosphorylated SMRT peptides, these observations may reinforce the idea that the features and functions of the FPA SPOC domain differ from those of the only other well-characterized SPOC domain.	RESULTS
106	110	SMRT	protein	Since the corresponding mutations in the SHARP SPOC domain do disrupt its recognition of unphosphorylated SMRT peptides, these observations may reinforce the idea that the features and functions of the FPA SPOC domain differ from those of the only other well-characterized SPOC domain.	RESULTS
111	119	peptides	chemical	Since the corresponding mutations in the SHARP SPOC domain do disrupt its recognition of unphosphorylated SMRT peptides, these observations may reinforce the idea that the features and functions of the FPA SPOC domain differ from those of the only other well-characterized SPOC domain.	RESULTS
202	205	FPA	protein	Since the corresponding mutations in the SHARP SPOC domain do disrupt its recognition of unphosphorylated SMRT peptides, these observations may reinforce the idea that the features and functions of the FPA SPOC domain differ from those of the only other well-characterized SPOC domain.	RESULTS
206	210	SPOC	structure_element	Since the corresponding mutations in the SHARP SPOC domain do disrupt its recognition of unphosphorylated SMRT peptides, these observations may reinforce the idea that the features and functions of the FPA SPOC domain differ from those of the only other well-characterized SPOC domain.	RESULTS
273	277	SPOC	structure_element	Since the corresponding mutations in the SHARP SPOC domain do disrupt its recognition of unphosphorylated SMRT peptides, these observations may reinforce the idea that the features and functions of the FPA SPOC domain differ from those of the only other well-characterized SPOC domain.	RESULTS