POB3_YEAST
ID POB3_YEAST Reviewed; 552 AA.
AC Q04636; D6VZA4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=FACT complex subunit POB3;
DE AltName: Full=Facilitates chromatin transcription complex subunit POB3;
GN Name=POB3; OrderedLocusNames=YML069W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP INTERACTION WITH POL1.
RX PubMed=9199353; DOI=10.1128/mcb.17.7.4178;
RA Wittmeyer J., Formosa T.;
RT "The Saccharomyces cerevisiae DNA polymerase alpha catalytic subunit
RT interacts with Cdc68/Spt16 and with Pob3, a protein similar to an HMG1-like
RT protein.";
RL Mol. Cell. Biol. 17:4178-4190(1997).
RN [4]
RP INTERACTION WITH SPT16.
RX PubMed=9832518; DOI=10.1093/genetics/150.4.1393;
RA Evans D.R.H., Brewster N.K., Xu Q., Rowley A., Altheim B.A., Johnston G.C.,
RA Singer R.A.;
RT "The yeast protein complex containing cdc68 and pob3 mediates core-promoter
RT repression through the cdc68 N-terminal domain.";
RL Genetics 150:1393-1405(1998).
RN [5]
RP INTERACTION WITH SPT16.
RX PubMed=9705338; DOI=10.1074/jbc.273.34.21972;
RA Brewster N.K., Johnston G.C., Singer R.A.;
RT "Characterization of the CP complex, an abundant dimer of Cdc68 and Pob3
RT proteins that regulates yeast transcriptional activation and chromatin
RT repression.";
RL J. Biol. Chem. 273:21972-21979(1998).
RN [6]
RP FUNCTION, INTERACTION WITH SPT16, AND SUBCELLULAR LOCATION.
RX PubMed=10413469; DOI=10.1021/bi982851d;
RA Wittmeyer J., Joss L., Formosa T.;
RT "Spt16 and Pob3 of Saccharomyces cerevisiae form an essential, abundant
RT heterodimer that is nuclear, chromatin-associated, and copurifies with DNA
RT polymerase alpha.";
RL Biochemistry 38:8961-8971(1999).
RN [7]
RP INTERACTION WITH SAS3.
RX PubMed=10817755;
RA John S., Howe L., Tafrov S.T., Grant P.A., Sternglanz R., Workman J.L.;
RT "The something about silencing protein, Sas3, is the catalytic subunit of
RT NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16
RT subunit of the yeast CP (Cdc68/Pob3)-FACT complex.";
RL Genes Dev. 14:1196-1208(2000).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF ARG-20; LEU-78; ARG-109; MET-419; SER-489 AND
RP LYS-547.
RX PubMed=10924459; DOI=10.1093/genetics/155.4.1593;
RA Schlesinger M.B., Formosa T.;
RT "POB3 is required for both transcription and replication in the yeast
RT Saccharomyces cerevisiae.";
RL Genetics 155:1593-1606(2000).
RN [9]
RP ASSOCIATION OF THE SPT16-POB3 DIMER WITH NHP6A/B AND NUCLEOSOMES, AND
RP FUNCTION OF THE FACT COMPLEX.
RX PubMed=11432837; DOI=10.1093/emboj/20.13.3506;
RA Formosa T., Eriksson P., Wittmeyer J., Ginn J., Yu Y., Stillman D.J.;
RT "Spt16-Pob3 and the HMG protein Nhp6 combine to form the nucleosome-binding
RT factor SPN.";
RL EMBO J. 20:3506-3517(2001).
RN [10]
RP ASSOCIATION OF THE SPT16-POB3 DIMER WITH NHP6A/B.
RX PubMed=11313475; DOI=10.1128/mcb.21.10.3491-3502.2001;
RA Brewster N.K., Johnston G.C., Singer R.A.;
RT "A bipartite yeast SSRP1 analog comprised of Pob3 and Nhp6 proteins
RT modulates transcription.";
RL Mol. Cell. Biol. 21:3491-3502(2001).
RN [11]
RP INTERACTION WITH PAF1 COMPLEX.
RX PubMed=11927560; DOI=10.1093/emboj/21.7.1764;
RA Squazzo S.L., Costa P.J., Lindstrom D.L., Kumer K.E., Simic R.,
RA Jennings J.L., Link A.J., Arndt K.M., Hartzog G.A.;
RT "The Paf1 complex physically and functionally associates with transcription
RT elongation factors in vivo.";
RL EMBO J. 21:1764-1774(2002).
RN [12]
RP FUNCTION OF THE FACT COMPLEX.
RX PubMed=12524332; DOI=10.1093/genetics/162.4.1557;
RA Formosa T., Ruone S., Adams M.D., Olsen A.E., Eriksson P., Yu Y.,
RA Rhoades A.R., Kaufman P.D., Stillman D.J.;
RT "Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause
RT dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin
RT structure.";
RL Genetics 162:1557-1571(2002).
RN [13]
RP INTERACTION WITH CHD1; CTR9; PAF1; CDC73; CKA1; CKA2; CKB1; CKB2 AND
RP HISTONES.
RX PubMed=12242279; DOI=10.1128/mcb.22.20.6979-6992.2002;
RA Krogan N.J., Kim M., Ahn S.H., Zhong G., Kobor M.S., Cagney G., Emili A.,
RA Shilatifard A., Buratowski S., Greenblatt J.F.;
RT "RNA polymerase II elongation factors of Saccharomyces cerevisiae: a
RT targeted proteomics approach.";
RL Mol. Cell. Biol. 22:6979-6992(2002).
RN [14]
RP INTERACTION WITH CHD1.
RX PubMed=12682017; DOI=10.1093/emboj/cdg179;
RA Simic R., Lindstrom D.L., Tran H.G., Roinick K.L., Costa P.J.,
RA Johnson A.D., Hartzog G.A., Arndt K.M.;
RT "Chromatin remodeling protein Chd1 interacts with transcription elongation
RT factors and localizes to transcribed genes.";
RL EMBO J. 22:1846-1856(2003).
RN [15]
RP ASSOCIATION OF THE SPT16-POB3 DIMER WITH NHP6A/B.
RX PubMed=12952948; DOI=10.1074/jbc.m307291200;
RA Ruone S., Rhoades A.R., Formosa T.;
RT "Multiple Nhp6 molecules are required to recruit Spt16-Pob3 to form yFACT
RT complexes and to reorganize nucleosomes.";
RL J. Biol. Chem. 278:45288-45295(2003).
RN [16]
RP FUNCTION OF THE FACT COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=14585989; DOI=10.1128/mcb.23.22.8323-8333.2003;
RA Mason P.B., Struhl K.;
RT "The FACT complex travels with elongating RNA polymerase II and is
RT important for the fidelity of transcriptional initiation in vivo.";
RL Mol. Cell. Biol. 23:8323-8333(2003).
RN [17]
RP ERRATUM OF PUBMED:14585989.
RA Mason P.B., Struhl K.;
RL Mol. Cell. Biol. 24:6536-6536(2004).
RN [18]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [19]
RP FUNCTION OF THE FACT COMPLEX.
RX PubMed=12934008; DOI=10.1126/science.1087374;
RA Kaplan C.D., Laprade L., Winston F.;
RT "Transcription elongation factors repress transcription initiation from
RT cryptic sites.";
RL Science 301:1096-1099(2003).
RN [20]
RP SUBCELLULAR LOCATION.
RX PubMed=14739930; DOI=10.1038/sj.emboj.7600053;
RA Kim M., Ahn S.-H., Krogan N.J., Greenblatt J.F., Buratowski S.;
RT "Transitions in RNA polymerase II elongation complexes at the 3' ends of
RT genes.";
RL EMBO J. 23:354-364(2004).
RN [21]
RP FUNCTION OF THE FACT COMPLEX.
RX PubMed=15082784; DOI=10.1128/mcb.24.9.3907-3917.2004;
RA Rhoades A.R., Ruone S., Formosa T.;
RT "Structural features of nucleosomes reorganized by yeast FACT and its HMG
RT box component, Nhp6.";
RL Mol. Cell. Biol. 24:3907-3917(2004).
RN [22]
RP FUNCTION OF THE FACT COMPLEX.
RX PubMed=15987999; DOI=10.1128/mcb.25.14.5812-5822.2005;
RA Biswas D., Yu Y., Prall M., Formosa T., Stillman D.J.;
RT "The yeast FACT complex has a role in transcriptional initiation.";
RL Mol. Cell. Biol. 25:5812-5822(2005).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [24]
RP SUBCELLULAR LOCATION.
RX PubMed=19683497; DOI=10.1016/j.molcel.2009.06.023;
RA Fillingham J., Kainth P., Lambert J.P., van Bakel H., Tsui K.,
RA Pena-Castillo L., Nislow C., Figeys D., Hughes T.R., Greenblatt J.,
RA Andrews B.J.;
RT "Two-color cell array screen reveals interdependent roles for histone
RT chaperones and a chromatin boundary regulator in histone gene repression.";
RL Mol. Cell 35:340-351(2009).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 220-478, FUNCTION, INTERACTION
RP WITH RFA1, AND MUTAGENESIS OF GLN-308 AND THR-311.
RX PubMed=16678108; DOI=10.1016/j.molcel.2006.03.025;
RA Vandemark A.P., Blanksma M., Ferris E., Heroux A., Hill C.P., Formosa T.;
RT "The structure of the yFACT Pob3-M domain, its interaction with the DNA
RT replication factor RPA, and a potential role in nucleosome deposition.";
RL Mol. Cell 22:363-374(2006).
CC -!- FUNCTION: Component of the FACT complex, a general chromatin factor
CC that acts to reorganize nucleosomes. The FACT complex is involved in
CC multiple processes that require DNA as a template such as mRNA
CC elongation, DNA replication and DNA repair. During transcription
CC elongation the FACT complex acts as a histone chaperone that both
CC destabilizes and restores nucleosomal structure. It facilitates the
CC passage of RNA polymerase II and transcription by promoting the
CC dissociation of one histone H2A-H2B dimer from the nucleosome, then
CC subsequently promotes the reestablishment of the nucleosome following
CC the passage of RNA polymerase II. Transcription elongation is promoted
CC by the repression of transcription initiation from cryptic sites. Also
CC acts in establishing transcription initiation complexes and promotes
CC SPT15/TBP-binding to a TATA box. Together with replication factor-A
CC protein (RPA), FACT may play a role in nucleosome deposition during DNA
CC replication. {ECO:0000269|PubMed:10413469, ECO:0000269|PubMed:10924459,
CC ECO:0000269|PubMed:11432837, ECO:0000269|PubMed:12524332,
CC ECO:0000269|PubMed:12934008, ECO:0000269|PubMed:14585989,
CC ECO:0000269|PubMed:15082784, ECO:0000269|PubMed:15987999,
CC ECO:0000269|PubMed:16678108}.
CC -!- SUBUNIT: Forms a stable heterodimer with SPT16. The SPT16-POB3 dimer
CC weakly associates with multiple molecules of NHP6 (NHP6A or NHP6B) to
CC form the FACT (yFACT or SNP) complex. The FACT complex interacts with
CC the CK2 (casein kinase II) complex subunits CKA1, CKA2, CKB1 and CKB2
CC and the components of the transcription machinery CHD1, CTR9, PAF1 and
CC CDC73. The FACT complex interacts with the PAF1 complex. SPT16
CC interacts with SAS3 and POL1. Interacts directly with RFA1.
CC {ECO:0000269|PubMed:10413469, ECO:0000269|PubMed:10817755,
CC ECO:0000269|PubMed:11927560, ECO:0000269|PubMed:12242279,
CC ECO:0000269|PubMed:12682017, ECO:0000269|PubMed:16678108,
CC ECO:0000269|PubMed:9199353, ECO:0000269|PubMed:9705338,
CC ECO:0000269|PubMed:9832518}.
CC -!- INTERACTION:
CC Q04636; P61830: HHT2; NbExp=2; IntAct=EBI-27863, EBI-8098;
CC Q04636; P22336: RFA1; NbExp=3; IntAct=EBI-27863, EBI-14971;
CC Q04636; P32558: SPT16; NbExp=8; IntAct=EBI-27863, EBI-4334;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10413469}. Chromosome
CC {ECO:0000269|PubMed:10413469, ECO:0000269|PubMed:14585989}.
CC Note=Colocalizes with RNA polymerase II on chromatin (PubMed:10413469,
CC PubMed:14585989, PubMed:14739930). Recruited to actively transcribed
CC loci (PubMed:14585989). Associates with the coding region of HTA1
CC (PubMed:19683497). {ECO:0000269|PubMed:10413469,
CC ECO:0000269|PubMed:14585989, ECO:0000269|PubMed:14739930,
CC ECO:0000269|PubMed:19683497}.
CC -!- MISCELLANEOUS: In contrast to the orthologous protein in animals and
CC plants, this protein does not contain a HMG box DNA-binding domain.
CC This function may instead be provided by the HMG box of the associated
CC NHP6A/NHP6B proteins in the FACT complex of yeast.
CC -!- MISCELLANEOUS: Present with 22400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z38114; CAA86251.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09828.1; -; Genomic_DNA.
DR PIR; S48328; S48328.
DR RefSeq; NP_013642.1; NM_001182428.1.
DR PDB; 2GCJ; X-ray; 2.55 A; A/B/C/D=220-478.
DR PDB; 2GCL; X-ray; 2.21 A; A/B=220-478.
DR PDB; 3F5R; X-ray; 1.70 A; A=1-168.
DR PDB; 4PQ0; X-ray; 1.65 A; A=232-473.
DR PDB; 7NKY; EM; 3.20 A; O=1-552.
DR PDBsum; 2GCJ; -.
DR PDBsum; 2GCL; -.
DR PDBsum; 3F5R; -.
DR PDBsum; 4PQ0; -.
DR PDBsum; 7NKY; -.
DR AlphaFoldDB; Q04636; -.
DR SMR; Q04636; -.
DR BioGRID; 35097; 709.
DR ComplexPortal; CPX-3215; FACT complex.
DR DIP; DIP-4083N; -.
DR IntAct; Q04636; 50.
DR MINT; Q04636; -.
DR STRING; 4932.YML069W; -.
DR iPTMnet; Q04636; -.
DR MaxQB; Q04636; -.
DR PaxDb; Q04636; -.
DR PRIDE; Q04636; -.
DR DNASU; 854933; -.
DR EnsemblFungi; YML069W_mRNA; YML069W; YML069W.
DR GeneID; 854933; -.
DR KEGG; sce:YML069W; -.
DR SGD; S000004534; POB3.
DR VEuPathDB; FungiDB:YML069W; -.
DR eggNOG; KOG0526; Eukaryota.
DR HOGENOM; CLU_017374_3_0_1; -.
DR InParanoid; Q04636; -.
DR OMA; SKQPGKC; -.
DR BioCyc; YEAST:G3O-32664-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SCE-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR EvolutionaryTrace; Q04636; -.
DR PRO; PR:Q04636; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04636; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0035101; C:FACT complex; IDA:SGD.
DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0034724; P:DNA replication-independent chromatin organization; IDA:SGD.
DR GO; GO:0006261; P:DNA-templated DNA replication; IMP:SGD.
DR GO; GO:0034728; P:nucleosome organization; IC:ComplexPortal.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IDA:SGD.
DR GO; GO:1902275; P:regulation of chromatin organization; IC:ComplexPortal.
DR Gene3D; 2.30.29.220; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR013719; DUF1747.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR035417; POB3_N.
DR InterPro; IPR000969; SSrcognition.
DR InterPro; IPR024954; SSRP1_dom.
DR InterPro; IPR038167; SSRP1_sf.
DR Pfam; PF17292; POB3_N; 1.
DR Pfam; PF08512; Rtt106; 1.
DR Pfam; PF03531; SSrecog; 1.
DR PRINTS; PR00887; SSRCOGNITION.
DR SMART; SM01287; Rtt106; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; DNA damage; DNA repair; DNA replication; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..552
FT /note="FACT complex subunit POB3"
FT /id="PRO_0000203250"
FT REGION 190..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..536
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 20
FT /note="R->H: In pob3-11; causes severe defects in rate of
FT growth; when associated with C-109."
FT /evidence="ECO:0000269|PubMed:10924459"
FT MUTAGEN 78
FT /note="L->R: In pob3-1; causes severe defects in rate of
FT growth; when associated with K-419 and T-489."
FT /evidence="ECO:0000269|PubMed:10924459"
FT MUTAGEN 109
FT /note="R->C: In pob3-11; causes severe defects in rate of
FT growth; when associated with H-20."
FT /evidence="ECO:0000269|PubMed:10924459"
FT MUTAGEN 308
FT /note="Q->A,D: No effect."
FT /evidence="ECO:0000269|PubMed:16678108"
FT MUTAGEN 308
FT /note="Q->K: Confers sensitivity to HU indicating a
FT disturbed activity in DNA replication; confers a
FT SPT- phenotype indicating a disturbed activity in
FT transcription."
FT /evidence="ECO:0000269|PubMed:16678108"
FT MUTAGEN 308
FT /note="Q->R: Confers sensitivity to HU indicating a
FT disturbed activity in DNA replication."
FT /evidence="ECO:0000269|PubMed:16678108"
FT MUTAGEN 311
FT /note="T->A: No change of sensitivity to HU; confers a
FT SPT- phenotype indicating a disturbed activity in
FT transcription."
FT /evidence="ECO:0000269|PubMed:16678108"
FT MUTAGEN 419
FT /note="M->K: In pob3-1; causes severe defects in rate of
FT growth; when associated with R-78 and T-489."
FT /evidence="ECO:0000269|PubMed:10924459"
FT MUTAGEN 489
FT /note="S->T: In pob3-1; causes severe defects in rate of
FT growth; when associated with R-78 and K-419."
FT /evidence="ECO:0000269|PubMed:10924459"
FT MUTAGEN 547
FT /note="K->M: In pob3-21; causes severe defects in rate of
FT growth."
FT /evidence="ECO:0000269|PubMed:10924459"
FT STRAND 1..10
FT /evidence="ECO:0007829|PDB:3F5R"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:7NKY"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:3F5R"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3F5R"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:3F5R"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:3F5R"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:3F5R"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:3F5R"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:3F5R"
FT STRAND 61..73
FT /evidence="ECO:0007829|PDB:3F5R"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:3F5R"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3F5R"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:3F5R"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:3F5R"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:7NKY"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:7NKY"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:7NKY"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:7NKY"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:7NKY"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:7NKY"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:7NKY"
FT STRAND 242..252
FT /evidence="ECO:0007829|PDB:4PQ0"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:4PQ0"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:4PQ0"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:4PQ0"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:4PQ0"
FT STRAND 282..289
FT /evidence="ECO:0007829|PDB:4PQ0"
FT STRAND 293..308
FT /evidence="ECO:0007829|PDB:4PQ0"
FT STRAND 311..321
FT /evidence="ECO:0007829|PDB:4PQ0"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:4PQ0"
FT HELIX 334..340
FT /evidence="ECO:0007829|PDB:4PQ0"
FT TURN 341..344
FT /evidence="ECO:0007829|PDB:4PQ0"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:4PQ0"
FT HELIX 353..365
FT /evidence="ECO:0007829|PDB:4PQ0"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:7NKY"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:4PQ0"
FT STRAND 391..397
FT /evidence="ECO:0007829|PDB:4PQ0"
FT STRAND 399..408
FT /evidence="ECO:0007829|PDB:4PQ0"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:4PQ0"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:4PQ0"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:4PQ0"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:7NKY"
FT STRAND 434..441
FT /evidence="ECO:0007829|PDB:4PQ0"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:4PQ0"
FT STRAND 447..454
FT /evidence="ECO:0007829|PDB:4PQ0"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:4PQ0"
FT HELIX 458..467
FT /evidence="ECO:0007829|PDB:4PQ0"
SQ SEQUENCE 552 AA; 62994 MW; 02C04F620C7B1450 CRC64;
MSTDFDRIYL NQSKFSGRFR IADSGLGWKI STSGGSAANQ ARKPFLLPAT ELSTVQWSRG
CRGYDLKINT KNQGVIQLDG FSQDDYNLIK NDFHRRFNIQ VEQREHSLRG WNWGKTDLAR
NEMVFALNGK PTFEIPYARI NNTNLTSKNE VGIEFNIQDE EYQPAGDELV EMRFYIPGVI
QTNVDENMTK KEESSNEVVP KKEDGAEGED VQMAVEEKSM AEAFYEELKE KADIGEVAGD
AIVSFQDVFF TTPRGRYDID IYKNSIRLRG KTYEYKLQHR QIQRIVSLPK ADDIHHLLVL
AIEPPLRQGQ TTYPFLVLQF QKDEETEVQL NLEDEDYEEN YKDKLKKQYD AKTHIVLSHV
LKGLTDRRVI VPGEYKSKYD QCAVSCSFKA NEGYLYPLDN AFFFLTKPTL YIPFSDVSMV
NISRAGQTST SSRTFDLEVV LRSNRGSTTF ANISKEEQQL LEQFLKSKNL RVKNEDREVQ
ERLQTALGSD SDEEDINMGS AGEDDESVDE DFQVSSDNDA DEVAEEFDSD AALSDAEGGS
DEERPSKKPK VE
