SNF2_YEAST
ID SNF2_YEAST Reviewed; 1703 AA.
AC P22082; D6W2Y8;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Transcription regulatory protein SNF2;
DE EC=3.6.4.-;
DE AltName: Full=ATP-dependent helicase SNF2;
DE AltName: Full=Regulatory protein GAM1;
DE AltName: Full=Regulatory protein SWI2;
DE AltName: Full=SWI/SNF complex component SNF2;
DE AltName: Full=Transcription factor TYE3;
GN Name=SNF2; Synonyms=GAM1, RIC1, SWI2, TYE3; OrderedLocusNames=YOR290C;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1901413; DOI=10.1073/pnas.88.7.2687;
RA Laurent B.C., Treitel M.A., Carlson M.;
RT "Functional interdependence of the yeast SNF2, SNF5, and SNF6 proteins in
RT transcriptional activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:2687-2691(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 38626 / AH22 / NRRL Y-12843;
RX PubMed=1886612; DOI=10.1007/bf00282476;
RA Yoshimoto H., Yamashita I.;
RT "The GAM1/SNF2 gene of Saccharomyces cerevisiae encodes a highly charged
RT nuclear protein required for transcription of the STA1 gene.";
RL Mol. Gen. Genet. 228:270-280(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26787 / X2180-1B;
RX PubMed=7608126; DOI=10.1093/jb/117.2.362;
RA Kodaki T., Hosaka K., Nikawa J., Yamashita S.;
RT "The SNF2/SWI2/GAM1/TYE3/RIC1 gene is involved in the coordinate regulation
RT of phospholipid synthesis in Saccharomyces cerevisiae.";
RL J. Biochem. 117:362-368(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8896271;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1059::aid-yea994%3e3.0.co;2-7;
RA Cheret G., Bernardi A., Sor F.J.;
RT "DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of
RT Saccharomyces cerevisiae.";
RL Yeast 12:1059-1064(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-309.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9153758;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<479::aid-yea104>3.0.co;2-g;
RA Poirey R., Cziepluch C., Tobiasch E., Pujol A., Kordes E., Jauniaux J.-C.;
RT "Sequence and analysis of a 36.2 kb fragment from the right arm of yeast
RT chromosome XV reveals 19 open reading frames including SNF2 (5' end), CPA1,
RT SLY41, a putative transport ATPase, a putative ribosomal protein and an
RT SNF2 homologue.";
RL Yeast 13:479-482(1997).
RN [8]
RP MUTAGENESIS.
RX PubMed=8871545; DOI=10.1093/nar/24.19.3685;
RA Richmond E., Peterson C.L.;
RT "Functional analysis of the DNA-stimulated ATPase domain of yeast
RT SWI2/SNF2.";
RL Nucleic Acids Res. 24:3685-3692(1996).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-716 AND SER-1340,
RP AND 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; THR-383 AND SER-716, AND
RP IDENTIFICATION BY MASS 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).
RN [13]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-543, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [14]
RP 3D-STRUCTURE MODELING OF THE SWI/SNF COMPLEX, AND ELECTRON MICROSCOPY OF
RP THE SWI/SNF COMPLEX.
RX PubMed=12524530; DOI=10.1038/nsb888;
RA Smith C.L., Horowitz-Scherer R., Flanagan J.F., Woodcock C.L.,
RA Peterson C.L.;
RT "Structural analysis of the yeast SWI/SNF chromatin remodeling complex.";
RL Nat. Struct. Biol. 10:141-145(2003).
CC -!- FUNCTION: Involved in transcriptional activation. Catalytic component
CC of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex,
CC which is required for the positive and negative regulation of gene
CC expression of a large number of genes. It changes chromatin structure
CC by altering DNA-histone contacts within a nucleosome, leading
CC eventually to a change in nucleosome position, thus facilitating or
CC repressing binding of gene-specific transcription factors.
CC -!- SUBUNIT: Component of the SWI/SNF global transcription activator
CC complex. The 1.14 MDa SWI/SNF complex is composed of 11 different
CC subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73,
CC ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82;
CC and three copies of TAF14/SWP29.
CC -!- INTERACTION:
CC P22082; P02309: HHF2; NbExp=2; IntAct=EBI-17526, EBI-8113;
CC P22082; P38074: HMT1; NbExp=3; IntAct=EBI-17526, EBI-8394;
CC P22082; P38956: SNF11; NbExp=3; IntAct=EBI-17526, EBI-17560;
CC P22082; P32591: SWI3; NbExp=8; IntAct=EBI-17526, EBI-18622;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 217 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M61703; AAA35059.1; -; Genomic_DNA.
DR EMBL; X57837; CAA40969.1; -; Genomic_DNA.
DR EMBL; D90459; BAA14423.1; -; Genomic_DNA.
DR EMBL; X89633; CAA61793.1; -; Genomic_DNA.
DR EMBL; Z75198; CAA99517.1; -; Genomic_DNA.
DR EMBL; Z75199; CAA99519.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11054.1; -; Genomic_DNA.
DR PIR; S15047; S15047.
DR RefSeq; NP_014933.3; NM_001183709.3.
DR PDB; 4I6M; X-ray; 2.80 A; C=575-667.
DR PDB; 5X0X; EM; 3.97 A; O=666-1400.
DR PDB; 5X0Y; EM; 3.97 A; O=666-1400.
DR PDB; 5Z3L; EM; 4.31 A; O=666-1400.
DR PDB; 5Z3O; EM; 3.62 A; O=666-1400.
DR PDB; 5Z3U; EM; 4.31 A; O=666-1400.
DR PDB; 5Z3V; EM; 4.22 A; O=666-1400.
DR PDB; 6IY2; EM; 3.47 A; O=670-1348.
DR PDB; 6IY3; EM; 3.67 A; O=670-1348.
DR PDB; 6UXV; EM; 4.70 A; A=1-1703.
DR PDB; 6UXW; EM; 8.96 A; A=1-1703.
DR PDB; 7C4J; EM; 2.89 A; H=1-1703.
DR PDB; 7EGM; EM; 3.60 A; A=430-1400.
DR PDB; 7EGP; EM; 6.90 A; A=430-1400.
DR PDBsum; 4I6M; -.
DR PDBsum; 5X0X; -.
DR PDBsum; 5X0Y; -.
DR PDBsum; 5Z3L; -.
DR PDBsum; 5Z3O; -.
DR PDBsum; 5Z3U; -.
DR PDBsum; 5Z3V; -.
DR PDBsum; 6IY2; -.
DR PDBsum; 6IY3; -.
DR PDBsum; 6UXV; -.
DR PDBsum; 6UXW; -.
DR PDBsum; 7C4J; -.
DR PDBsum; 7EGM; -.
DR PDBsum; 7EGP; -.
DR AlphaFoldDB; P22082; -.
DR SMR; P22082; -.
DR BioGRID; 34678; 258.
DR ComplexPortal; CPX-1150; SWI/SNF chromatin remodelling complex.
DR DIP; DIP-1150N; -.
DR IntAct; P22082; 47.
DR MINT; P22082; -.
DR STRING; 4932.YOR290C; -.
DR iPTMnet; P22082; -.
DR MaxQB; P22082; -.
DR PaxDb; P22082; -.
DR PRIDE; P22082; -.
DR EnsemblFungi; YOR290C_mRNA; YOR290C; YOR290C.
DR GeneID; 854465; -.
DR KEGG; sce:YOR290C; -.
DR SGD; S000005816; SNF2.
DR VEuPathDB; FungiDB:YOR290C; -.
DR eggNOG; KOG0386; Eukaryota.
DR GeneTree; ENSGT00940000169728; -.
DR HOGENOM; CLU_000315_15_2_1; -.
DR InParanoid; P22082; -.
DR OMA; LRGFNNQ; -.
DR BioCyc; YEAST:G3O-33775-MON; -.
DR Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR PRO; PR:P22082; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P22082; protein.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:SGD.
DR GO; GO:0031492; F:nucleosomal DNA binding; IDA:SGD.
DR GO; GO:0000182; F:rDNA binding; IDA:SGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:SGD.
DR GO; GO:0035973; P:aggrephagy; IMP:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR GO; GO:0006261; P:DNA-templated DNA replication; IMP:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:1900189; P:positive regulation of cell adhesion involved in single-species biofilm formation; IMP:SGD.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:2000219; P:positive regulation of invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0031496; P:positive regulation of mating type switching; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0061412; P:positive regulation of transcription from RNA polymerase II promoter in response to amino acid starvation; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006979; P:response to oxidative stress; IMP:SGD.
DR GO; GO:0042148; P:strand invasion; IMP:SGD.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00384; AT_hook; 2.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51666; QLQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; ATP-binding; Bromodomain; Helicase; Hydrolase;
KW Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..1703
FT /note="Transcription regulatory protein SNF2"
FT /id="PRO_0000074358"
FT DOMAIN 247..282
FT /note="QLQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01001"
FT DOMAIN 588..661
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 779..944
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1091..1254
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1568..1638
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DNA_BIND 1446..1456
FT /note="A.T hook 1"
FT DNA_BIND 1502..1513
FT /note="A.T hook 2"
FT DNA_BIND 1516..1526
FT /note="A.T hook 3"
FT REGION 57..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1338..1531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 894..897
FT /note="DEGH box"
FT COMPBIAS 305..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1370..1412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1524
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 792..799
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 383
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 543
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT HELIX 427..434
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 465..471
FT /evidence="ECO:0007829|PDB:7C4J"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:7C4J"
FT TURN 481..483
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 490..517
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 523..556
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 560..563
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 593..657
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 672..681
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 685..688
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 744..747
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 769..783
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 798..811
FT /evidence="ECO:0007829|PDB:6IY2"
FT STRAND 819..822
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 825..827
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 828..838
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 851..861
FT /evidence="ECO:0007829|PDB:6IY2"
FT TURN 862..864
FT /evidence="ECO:0007829|PDB:6IY2"
FT STRAND 867..869
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 874..878
FT /evidence="ECO:0007829|PDB:6IY2"
FT TURN 879..881
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 882..885
FT /evidence="ECO:0007829|PDB:6IY2"
FT STRAND 890..893
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 896..899
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 905..911
FT /evidence="ECO:0007829|PDB:6IY2"
FT STRAND 917..922
FT /evidence="ECO:0007829|PDB:6IY2"
FT STRAND 929..933
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 934..937
FT /evidence="ECO:0007829|PDB:6IY2"
FT TURN 938..940
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 944..947
FT /evidence="ECO:0007829|PDB:6IY2"
FT TURN 948..952
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 953..956
FT /evidence="ECO:0007829|PDB:6IY2"
FT TURN 957..959
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 970..974
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 977..986
FT /evidence="ECO:0007829|PDB:6IY2"
FT TURN 996..1000
FT /evidence="ECO:0007829|PDB:6IY2"
FT STRAND 1007..1013
FT /evidence="ECO:0007829|PDB:6IY2"
FT TURN 1017..1020
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 1021..1030
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 1051..1060
FT /evidence="ECO:0007829|PDB:6IY2"
FT STRAND 1064..1066
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 1069..1072
FT /evidence="ECO:0007829|PDB:6IY2"
FT TURN 1080..1082
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 1087..1102
FT /evidence="ECO:0007829|PDB:6IY2"
FT STRAND 1106..1109
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 1113..1125
FT /evidence="ECO:0007829|PDB:6IY2"
FT STRAND 1130..1132
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 1140..1149
FT /evidence="ECO:0007829|PDB:6IY2"
FT STRAND 1158..1160
FT /evidence="ECO:0007829|PDB:6IY2"
FT STRAND 1177..1182
FT /evidence="ECO:0007829|PDB:6IY2"
FT STRAND 1185..1187
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 1188..1197
FT /evidence="ECO:0007829|PDB:6IY2"
FT STRAND 1207..1213
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 1217..1228
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 1233..1238
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 1240..1242
FT /evidence="ECO:0007829|PDB:6IY2"
FT TURN 1247..1251
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 1252..1258
FT /evidence="ECO:0007829|PDB:6IY2"
FT TURN 1259..1262
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 1264..1268
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 1280..1286
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 1291..1306
FT /evidence="ECO:0007829|PDB:6IY2"
FT HELIX 1338..1345
FT /evidence="ECO:0007829|PDB:6IY2"
SQ SEQUENCE 1703 AA; 194051 MW; 84B8BC595C8F3E6D CRC64;
MNIPQRQFSN EEVNRCYLRW QHLRNEHGMN APSVPEFIYL TKVLQFAAKQ RQELQMQRQQ
QGISGSQQNI VPNSSDQAEL PNNASSHISA SASPHLAPNM QLNGNETFST SAHQSPIMQT
QMPLNSNGGN NMLPQRQSSV GSLNATNFSP TPANNGENAA EKPDNSNHNN LNLNNSELQP
QNRSLQEHNI QDSNVMPGSQ INSPMPQQAQ MQQAQFQAQQ AQQAQQAQQA QQAQARLQQG
RRLPMTMFTA EQSELLKAQI TSLKCLVNRK PIPFEFQAVI QKSINHPPDF KRMLLSLSEF
ARRRQPTDQN NQSNLNGGNN TQQPGTNSHY NNTNTDNVSG LTRNAPLDSK DENFASVSPA
GPSSVHNAKN GTLDKNSQTV SGTPITQTES KKEENETISN VAKTAPNSNK THTEQNNPPK
PQKPVPLNVL QDQYKEGIKV VDIDDPDMMV DSFTMPNISH SNIDYQTLLA NSDHAKFTIE
PGVLPVGIDT HTATDIYQTL IALNLDTTVN DCLDKLLNDE CTESTRENAL YDYYALQLLP
LQKAVRGHVL QFEWHQNSLL TNTHPNFLSK IRNINVQDAL LTNQLYKNHE LLKLERKKTE
AVARLKSMNK SAINQYNRRQ DKKNKRLKFG HRLIATHTNL ERDEQKRAEK KAKERLQALK
ANDEEAYIKL LDQTKDTRIT HLLRQTNAFL DSLTRAVKDQ QKYTKEMIDS HIKEASEEVD
DLSMVPKMKD EEYDDDDDNS NVDYYNVAHR IKEDIKKQPS ILVGGTLKDY QIKGLQWMVS
LFNNHLNGIL ADEMGLGKTI QTISLLTYLY EMKNIRGPYL VIVPLSTLSN WSSEFAKWAP
TLRTISFKGS PNERKAKQAK IRAGEFDVVL TTFEYIIKER ALLSKVKWVH MIIDEGHRMK
NAQSKLSLTL NTHYHADYRL ILTGTPLQNN LPELWALLNF VLPKIFNSVK SFDEWFNTPF
ANTGGQDKIE LSEEETLLVI RRLHKVLRPF LLRRLKKDVE KELPDKVEKV VKCKMSALQQ
IMYQQMLKYR RLFIGDQNNK KMVGLRGFNN QIMQLKKICN HPFVFEEVED QINPTRETND
DIWRVAGKFE LLDRILPKLK ATGHRVLIFF QMTQIMDIME DFLRYINIKY LRLDGHTKSD
ERSELLRLFN APDSEYLCFI LSTRAGGLGL NLQTADTVII FDTDWNPHQD LQAQDRAHRI
GQKNEVRILR LITTNSVEEV ILERAYKKLD IDGKVIQAGK FDNKSTSEEQ EALLRSLLDA
EEERRKKRES GVEEEEELKD SEINEILARN DEEMAVLTRM DEDRSKKEEE LGVKSRLLEK
SELPDIYSRD IGAELKREES ESAAVYNGRG ARERKTATYN DNMSEEQWLR QFEVSDDEKN
DKQARKQRTK KEDKSEAIDG NGEIKGENID ADNDGPRINN ISAEDRADTD LAMNDDDFLS
KKRKAGRPRG RPKKVKLEGS ENSEPPALES SPVTGDNSPS EDFMDIPKPR TAGKTSVKSA
RTSTRGRGRG RGRGRGRGRG RGRPPKARNG LDYVRTPAAA TSPIDIREKV AKQALDLYHF
ALNYENEAGR KLSDIFLSKP SKALYPDYYM IIKYPVAFDN INTHIETLAY NSLKETLQDF
HLIFSNARIY NTEGSVVYED SLELEKVVTK KYCEIMGDNS QLDFTEFDEQ YGTRPLVLPP
VVTSSVAESF TDEADSSMTE ASV
