SPT6_YEAST
ID SPT6_YEAST Reviewed; 1451 AA.
AC P23615; D6VUP7;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Transcription elongation factor SPT6;
DE AltName: Full=Chromatin elongation factor SPT6;
GN Name=SPT6; Synonyms=CRE2, SSN20; OrderedLocusNames=YGR116W; ORFNames=G6169;
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 [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=2201908; DOI=10.1128/mcb.10.9.4935-4941.1990;
RA Swanson M.S., Carlson M., Winston F.;
RT "SPT6, an essential gene that affects transcription in Saccharomyces
RT cerevisiae, encodes a nuclear protein with an extremely acidic amino
RT terminus.";
RL Mol. Cell. Biol. 10:4935-4941(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8905931;
RX DOI=10.1002/(sici)1097-0061(19960930)12:12<1273::aid-yea21>3.0.co;2-j;
RA Hansen M., Albers M., Backes U., Coblenz A., Leuther H., Neu R.,
RA Schreer A., Schaefer B., Zimmermann M., Wolf K.;
RT "The sequence of a 23.4 kb segment on the right arm of chromosome VII from
RT Saccharomyces cerevisiae reveals CLB6, SPT6, RP28A and NUP57 genes, a Ty3
RT element and 11 new open reading frames.";
RL Yeast 12:1273-1277(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
RP DOMAIN SH2.
RX PubMed=8108857; DOI=10.1016/0968-0004(93)90006-9;
RA McLennan A.J., Shaw G.;
RT "A yeast SH2 domain.";
RL Trends Biochem. Sci. 18:464-465(1993).
RN [6]
RP FUNCTION IN TRANSCRIPTION ELONGATION.
RX PubMed=9450930; DOI=10.1101/gad.12.3.357;
RA Hartzog G.A., Wada T., Handa H., Winston F.;
RT "Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA
RT polymerase II in Saccharomyces cerevisiae.";
RL Genes Dev. 12:357-369(1998).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
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 [9]
RP FUNCTION.
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 [10]
RP FUNCTION, AND INTERACTION WITH CTR9.
RX PubMed=15531585; DOI=10.1074/jbc.m411108200;
RA Kaplan C.D., Holland M.J., Winston F.;
RT "Interaction between transcription elongation factors and mRNA 3'-end
RT formation at the Saccharomyces cerevisiae GAL10-GAL7 locus.";
RL J. Biol. Chem. 280:913-922(2005).
RN [11]
RP FUNCTION IN NUCLEOSOME REASSEMBLY.
RX PubMed=16455495; DOI=10.1016/j.molcel.2005.12.010;
RA Adkins M.W., Tyler J.K.;
RT "Transcriptional activators are dispensable for transcription in the
RT absence of Spt6-mediated chromatin reassembly of promoter regions.";
RL Mol. Cell 21:405-416(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; SER-134; SER-136; SER-155
RP AND SER-206, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; SER-134; SER-136; SER-155
RP AND SER-206, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; SER-134; SER-136;
RP SER-148; SER-155; SER-206 AND SER-295, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Plays a role in maintenance of chromatin structure during RNA
CC polymerase II transcription elongation thereby repressing transcription
CC initiation from cryptic promoters. Mediates the reassembly of
CC nucleosomes onto the promoters of at least a selected set of genes
CC during repression; the nucleosome reassembly is essential for
CC transcriptional repression. Essential for viability.
CC {ECO:0000269|PubMed:12934008, ECO:0000269|PubMed:15531585,
CC ECO:0000269|PubMed:16455495, ECO:0000269|PubMed:9450930}.
CC -!- SUBUNIT: Interacts with CTR9. {ECO:0000269|PubMed:15531585}.
CC -!- INTERACTION:
CC P23615; Q06505: SPN1; NbExp=7; IntAct=EBI-17947, EBI-32596;
CC P23615; P27692: SPT5; NbExp=2; IntAct=EBI-17947, EBI-17937;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:2201908}. Chromosome {ECO:0000269|PubMed:19683497}.
CC Note=Colocalizes with RNA polymerase II on chromatin (PubMed:2201908).
CC Recruited to the active transcribed loci (PubMed:2201908). Associates
CC with the coding region of HTA1 (PubMed:19683497).
CC {ECO:0000269|PubMed:19683497, ECO:0000269|PubMed:2201908}.
CC -!- MISCELLANEOUS: Present with 8890 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SPT6 family. {ECO:0000305}.
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DR EMBL; M34391; AAA35086.1; -; Genomic_DNA.
DR EMBL; Z72899; CAA97124.1; -; Genomic_DNA.
DR EMBL; Z72902; CAA97127.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08208.1; -; Genomic_DNA.
DR PIR; A36468; A36468.
DR RefSeq; NP_011631.1; NM_001181245.1.
DR PDB; 2L3T; NMR; -; A=1250-1440.
DR PDB; 3OAK; X-ray; 2.15 A; C/D=239-263.
DR PDB; 3PSF; X-ray; 2.59 A; A=235-1259.
DR PDB; 3PSI; X-ray; 3.30 A; A=239-1451.
DR PDB; 3PSJ; X-ray; 2.70 A; A=1247-1451.
DR PDB; 3PSK; X-ray; 2.10 A; A/B/C/D=1247-1451.
DR PDB; 5VKL; X-ray; 2.20 A; A=1247-1451.
DR PDB; 5VKO; X-ray; 1.80 A; A=1247-1451.
DR PDB; 7O3D; EM; 3.71 A; A=298-1451.
DR PDBsum; 2L3T; -.
DR PDBsum; 3OAK; -.
DR PDBsum; 3PSF; -.
DR PDBsum; 3PSI; -.
DR PDBsum; 3PSJ; -.
DR PDBsum; 3PSK; -.
DR PDBsum; 5VKL; -.
DR PDBsum; 5VKO; -.
DR PDBsum; 7O3D; -.
DR AlphaFoldDB; P23615; -.
DR BMRB; P23615; -.
DR SMR; P23615; -.
DR BioGRID; 33361; 188.
DR DIP; DIP-2630N; -.
DR IntAct; P23615; 21.
DR MINT; P23615; -.
DR STRING; 4932.YGR116W; -.
DR iPTMnet; P23615; -.
DR MaxQB; P23615; -.
DR PaxDb; P23615; -.
DR PRIDE; P23615; -.
DR EnsemblFungi; YGR116W_mRNA; YGR116W; YGR116W.
DR GeneID; 853011; -.
DR KEGG; sce:YGR116W; -.
DR SGD; S000003348; SPT6.
DR VEuPathDB; FungiDB:YGR116W; -.
DR eggNOG; KOG1856; Eukaryota.
DR GeneTree; ENSGT00510000047446; -.
DR HOGENOM; CLU_001680_0_1_1; -.
DR InParanoid; P23615; -.
DR OMA; LCNGFKT; -.
DR BioCyc; YEAST:G3O-30823-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR EvolutionaryTrace; P23615; -.
DR PRO; PR:P23615; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P23615; protein.
DR GO; GO:0000791; C:euchromatin; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0008023; C:transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IDA:SGD.
DR GO; GO:0031491; F:nucleosome binding; IDA:SGD.
DR GO; GO:0001073; F:transcription antitermination factor activity, DNA binding; IDA:SGD.
DR GO; GO:0000433; P:carbon catabolite repression of transcription from RNA polymerase II promoter by glucose; IMP:SGD.
DR GO; GO:0006325; P:chromatin organization; IMP:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IMP:SGD.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IDA:SGD.
DR GO; GO:0034728; P:nucleosome organization; IMP:SGD.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0000414; P:regulation of histone H3-K36 methylation; IDA:SGD.
DR GO; GO:0031440; P:regulation of mRNA 3'-end processing; IMP:SGD.
DR GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IMP:SGD.
DR GO; GO:0001178; P:regulation of transcriptional start site selection at RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0031564; P:transcription antitermination; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd09928; SH2_Cterm_SPT6_like; 1.
DR CDD; cd09918; SH2_Nterm_SPT6_like; 1.
DR Gene3D; 1.10.10.2740; -; 1.
DR Gene3D; 1.10.10.650; -; 1.
DR Gene3D; 1.10.3500.10; -; 2.
DR Gene3D; 3.30.420.140; -; 1.
DR Gene3D; 3.30.505.10; -; 2.
DR IDEAL; IID50042; -.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR028083; Spt6_acidic_N_dom.
DR InterPro; IPR042066; Spt6_death-like.
DR InterPro; IPR032706; Spt6_HHH.
DR InterPro; IPR028088; Spt6_HTH_DNA-bd_dom.
DR InterPro; IPR035420; Spt6_SH2.
DR InterPro; IPR035018; Spt6_SH2_C.
DR InterPro; IPR035019; Spt6_SH2_N.
DR InterPro; IPR028231; Spt6_YqgF.
DR InterPro; IPR023323; Tex-like_dom_sf.
DR InterPro; IPR023319; Tex-like_HTH_dom_sf.
DR InterPro; IPR017072; TF_Spt6.
DR InterPro; IPR006641; YqgF/RNaseH-like_dom.
DR InterPro; IPR037027; YqgF/RNaseH-like_dom_sf.
DR PANTHER; PTHR10145; PTHR10145; 1.
DR Pfam; PF14635; HHH_7; 1.
DR Pfam; PF14641; HTH_44; 1.
DR Pfam; PF14633; SH2_2; 1.
DR Pfam; PF14632; SPT6_acidic; 1.
DR Pfam; PF14639; YqgF; 1.
DR PIRSF; PIRSF036947; Spt6; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00732; YqgFc; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Nucleus; Phosphoprotein; Reference proteome;
KW SH2 domain; Transcription; Transcription regulation.
FT CHAIN 1..1451
FT /note="Transcription elongation factor SPT6"
FT /id="PRO_0000072173"
FT DOMAIN 1257..1354
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 1..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 8..12
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 77..85
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 120..125
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:3OAK"
FT HELIX 256..262
FT /evidence="ECO:0007829|PDB:3OAK"
FT HELIX 301..308
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 312..319
FT /evidence="ECO:0007829|PDB:3PSF"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 324..329
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:3PSF"
FT TURN 334..337
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 341..359
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 368..382
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 388..394
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:3PSF"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:3PSI"
FT HELIX 411..441
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 446..454
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 465..476
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 478..483
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 502..505
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 511..515
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 521..530
FT /evidence="ECO:0007829|PDB:3PSF"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:3PSI"
FT HELIX 545..554
FT /evidence="ECO:0007829|PDB:3PSF"
FT TURN 555..559
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 568..583
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 586..598
FT /evidence="ECO:0007829|PDB:3PSF"
FT STRAND 599..606
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 608..613
FT /evidence="ECO:0007829|PDB:3PSF"
FT TURN 615..617
FT /evidence="ECO:0007829|PDB:3PSF"
FT TURN 619..625
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 633..636
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 639..649
FT /evidence="ECO:0007829|PDB:3PSF"
FT STRAND 652..659
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 662..673
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 681..733
FT /evidence="ECO:0007829|PDB:3PSF"
FT STRAND 740..744
FT /evidence="ECO:0007829|PDB:3PSI"
FT STRAND 750..754
FT /evidence="ECO:0007829|PDB:3PSF"
FT TURN 760..762
FT /evidence="ECO:0007829|PDB:3PSF"
FT STRAND 765..770
FT /evidence="ECO:0007829|PDB:3PSF"
FT STRAND 776..782
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 793..806
FT /evidence="ECO:0007829|PDB:3PSF"
FT STRAND 809..813
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 819..833
FT /evidence="ECO:0007829|PDB:3PSF"
FT STRAND 839..841
FT /evidence="ECO:0007829|PDB:3PSI"
FT STRAND 846..848
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 854..858
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 861..866
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 872..885
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 887..892
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 896..900
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 908..910
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 913..931
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 935..939
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 942..945
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 946..950
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 956..968
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 978..981
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 987..993
FT /evidence="ECO:0007829|PDB:3PSF"
FT TURN 994..996
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 1015..1018
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 1023..1025
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 1026..1036
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 1041..1050
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 1055..1062
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 1066..1070
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 1075..1086
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 1091..1102
FT /evidence="ECO:0007829|PDB:3PSF"
FT STRAND 1103..1105
FT /evidence="ECO:0007829|PDB:3PSI"
FT HELIX 1117..1125
FT /evidence="ECO:0007829|PDB:3PSF"
FT TURN 1129..1131
FT /evidence="ECO:0007829|PDB:3PSI"
FT STRAND 1137..1145
FT /evidence="ECO:0007829|PDB:3PSI"
FT STRAND 1150..1153
FT /evidence="ECO:0007829|PDB:3PSI"
FT STRAND 1159..1162
FT /evidence="ECO:0007829|PDB:3PSI"
FT STRAND 1166..1169
FT /evidence="ECO:0007829|PDB:3PSI"
FT TURN 1177..1179
FT /evidence="ECO:0007829|PDB:3PSI"
FT STRAND 1185..1194
FT /evidence="ECO:0007829|PDB:3PSI"
FT HELIX 1195..1197
FT /evidence="ECO:0007829|PDB:3PSI"
FT STRAND 1199..1203
FT /evidence="ECO:0007829|PDB:3PSI"
FT HELIX 1206..1209
FT /evidence="ECO:0007829|PDB:3PSI"
FT TURN 1222..1224
FT /evidence="ECO:0007829|PDB:3PSF"
FT HELIX 1227..1246
FT /evidence="ECO:0007829|PDB:3PSF"
FT TURN 1247..1249
FT /evidence="ECO:0007829|PDB:3PSK"
FT STRAND 1253..1255
FT /evidence="ECO:0007829|PDB:2L3T"
FT HELIX 1264..1271
FT /evidence="ECO:0007829|PDB:5VKO"
FT STRAND 1279..1283
FT /evidence="ECO:0007829|PDB:5VKO"
FT TURN 1285..1287
FT /evidence="ECO:0007829|PDB:2L3T"
FT STRAND 1290..1298
FT /evidence="ECO:0007829|PDB:5VKO"
FT STRAND 1301..1311
FT /evidence="ECO:0007829|PDB:5VKO"
FT STRAND 1313..1317
FT /evidence="ECO:0007829|PDB:5VKO"
FT STRAND 1320..1324
FT /evidence="ECO:0007829|PDB:5VKO"
FT STRAND 1327..1331
FT /evidence="ECO:0007829|PDB:5VKO"
FT HELIX 1332..1338
FT /evidence="ECO:0007829|PDB:5VKO"
FT HELIX 1340..1351
FT /evidence="ECO:0007829|PDB:5VKO"
FT HELIX 1361..1374
FT /evidence="ECO:0007829|PDB:5VKO"
FT STRAND 1380..1385
FT /evidence="ECO:0007829|PDB:5VKO"
FT STRAND 1387..1389
FT /evidence="ECO:0007829|PDB:5VKO"
FT STRAND 1392..1400
FT /evidence="ECO:0007829|PDB:5VKO"
FT STRAND 1406..1412
FT /evidence="ECO:0007829|PDB:5VKO"
FT STRAND 1414..1419
FT /evidence="ECO:0007829|PDB:5VKO"
FT STRAND 1422..1426
FT /evidence="ECO:0007829|PDB:5VKO"
FT HELIX 1427..1445
FT /evidence="ECO:0007829|PDB:5VKO"
SQ SEQUENCE 1451 AA; 168291 MW; 0BE9922A59BD0483 CRC64;
MEETGDSKLV PRDEEEIVND NDETKAPSEE EEGEDVFDSS EEDEDIDEDE DEARKVQEGF
IVNDDDENED PGTSISKKRR KHKRREREED DRLSEDDLDL LMENAGVERT KASSSSGKFK
RLKRVGDEGN AAESESDNVA ASRQDSTSKL EDFFSEDEEE EESGLRNGRN NEYGRDEEDH
ENRNRTADKG GILDELDDFI EDDEFSDEDD ETRQRRIQEK KLLREQSIKQ PTQITGLSSD
KIDEMYDIFG DGHDYDWALE IENEELENGN DNNEAEEEEI DEETGAIKST KKKISLQDIY
DLEDLKKNLM TEGDMKIRKT DIPERYQELR AGITDYGNMS SEDQELERNW IAEKISVDKN
FDANYDLTEF KEAIGNAIKF ITKENLEVPF IYAYRRNYIS SREKDGFLLT EDDLWDIVSL
DIEFHSLVNK KDYVQRFYAE LHIDDPIVTE YFKNQNTASI AELNSLQDIY DYLEFKYANE
INEMFINHTG KTGKKHLKNS SYEKFKASPL YQAVSDIGIS AEDVGENISS QHQIHPPVDH
PSSKPVEVIE SILNANSGDL QVFTSNTKLA IDTVQKYYSL ELSKNTKIRE KVRSDFSKYY
LADVVLTAKG KKEIQKGSLY EDIKYAINRT PMHFRRDPDV FLKMVEAESL NLLSVKLHMS
SQAQYIEHLF QIALETTNTS DIAIEWNNFR KLAFNQAMDK IFQDISQEVK DNLTKNCQKL
VAKTVRHKFM TKLDQAPFIP NVRDPKIPKI LSLTCGQGRF GADAIIAVYV NRKGDFIRDY
KIVDNPFDKT NPEKFEDTLD NIIQSCQPNA IGINGPNPKT QKFYKRLQEV LHKKQIVDSR
GHTIPIIYVE DEVAIRYQNS ERAAQEFPNK PPLVKYCIAL ARYMHSPLLE YANLTSEEVR
SLSIHPHQNL LSSEQLSWAL ETAFVDIVNL VSVEVNKATD NNYYASALKY ISGFGKRKAI
DFLQSLQRLN EPLLARQQLI THNILHKTIF MNSAGFLYIS WNEKRQKYED LEHDQLDSTR
IHPEDYHLAT KVAADALEYD PDTIAEKEEQ GTMSEFIELL REDPDRRAKL ESLNLESYAE
ELEKNTGLRK LNNLNTIVLE LLDGFEELRN DFHPLQGDEI FQSLTGESEK TFFKGSIIPV
RVERFWHNDI ICTTNSEVEC VVNAQRHAGA QLRRPANEIY EIGKTYPAKV IYIDYANITA
EVSLLDHDVK QQYVPISYSK DPSIWDLKQE LEDAEEERKL MMAEARAKRT HRVINHPYYF
PFNGRQAEDY LRSKERGEFV IRQSSRGDDH LVITWKLDKD LFQHIDIQEL EKENPLALGK
VLIVDNQKYN DLDQIIVEYL QNKVRLLNEM TSSEKFKSGT KKDVVKFIED YSRVNPNKSV
YYFSLNHDNP GWFYLMFKIN ANSKLYTWNV KLTNTGYFLV NYNYPSVIQL CNGFKTLLKS
NSSKNRMNNY R
