ID MCM3_YEAST Reviewed; 971 AA. AC P24279; D3DLL7; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 27-MAR-2024, entry version 220. DE RecName: Full=DNA replication licensing factor MCM3; DE EC=3.6.4.12; DE AltName: Full=Minichromosome maintenance protein 3; GN Name=MCM3; OrderedLocusNames=YEL032W; ORFNames=SYGP-ORF23; 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]. RX PubMed=2233713; DOI=10.1128/mcb.10.11.5707-5720.1990; RA Gibson S.T., Suroski R.T., Tye B.K.; RT "The phenotype of the minichromosome maintenance mutant mcm3 is RT characteristic of mutants defective in DNA replication."; RL Mol. Cell. Biol. 10:5707-5720(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169868; RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., RA Botstein D., Davis R.W.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V."; RL Nature 387:78-81(1997). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-868, 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 [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777 AND SER-781, AND RP IDENTIFICATION BY 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 [5] RP RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7 RP COMPLEX, AND MUTAGENESIS OF LYS-415. RX PubMed=18657510; DOI=10.1016/j.molcel.2008.05.020; RA Bochman M.L., Schwacha A.; RT "The Mcm2-7 complex has in vitro helicase activity."; RL Mol. Cell 31:287-293(2008). RN [6] 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 [7] RP IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, AND RP ELECTRON MICROSCOPY OF THE MCM2-7 COMPLEX. RX PubMed=19896182; DOI=10.1016/j.cell.2009.10.015; RA Remus D., Beuron F., Tolun G., Griffith J.D., Morris E.P., Diffley J.F.; RT "Concerted loading of Mcm2-7 double hexamers around DNA during DNA RT replication origin licensing."; RL Cell 139:719-730(2009). RN [8] RP IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, AND RP ELECTRON MICROSCOPY OF THE MCM2-7 COMPLEX. RX PubMed=19910535; DOI=10.1073/pnas.0911500106; RA Evrin C., Clarke P., Zech J., Lurz R., Sun J., Uhle S., Li H., Stillman B., RA Speck C.; RT "A double-hexameric MCM2-7 complex is loaded onto origin DNA during RT licensing of eukaryotic DNA replication."; RL Proc. Natl. Acad. Sci. U.S.A. 106:20240-20245(2009). RN [9] 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 [10] 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 [11] RP INTERACTION WITH CSM1. RX PubMed=15023545; DOI=10.1016/j.yexcr.2003.12.008; RA Wysocka M., Rytka J., Kurlandzka A.; RT "Saccharomyces cerevisiae CSM1 gene encoding a protein influencing RT chromosome segregation in meiosis I interacts with elements of the DNA RT replication complex."; RL Exp. Cell Res. 294:592-602(2004). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-761 AND SER-781, 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). CC -!- FUNCTION: Acts as a component of the MCM2-7 complex (MCM complex) which CC is the putative replicative helicase essential for 'once per cell CC cycle' DNA replication initiation and elongation in eukaryotic cells. CC The active ATPase sites in the MCM2-7 ring are formed through the CC interaction surfaces of two neighboring subunits such that a critical CC structure of a conserved arginine finger motif is provided in trans CC relative to the ATP-binding site of the Walker A box of the adjacent CC subunit. The six ATPase active sites, however, are likely to contribute CC differentially to the complex helicase activity. Once loaded onto DNA, CC double hexamers can slide on dsDNA in the absence of ATPase activity. CC Necessary for cell growth. {ECO:0000269|PubMed:19896182, CC ECO:0000269|PubMed:19910535}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; CC -!- SUBUNIT: Component of the MCM2-7 complex. The complex forms a toroidal CC hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7- CC MCM3-MCM5; loaded onto DNA, forms a head-head double hexamer. Interacts CC with CSM1. {ECO:0000269|PubMed:15023545, ECO:0000269|PubMed:19896182, CC ECO:0000269|PubMed:19910535}. CC -!- INTERACTION: CC P24279; P25651: CSM1; NbExp=2; IntAct=EBI-10541, EBI-22001; CC P24279; P29496: MCM5; NbExp=5; IntAct=EBI-10541, EBI-10549; CC P24279; P38132: MCM7; NbExp=2; IntAct=EBI-10541, EBI-4300; CC P24279; Q12306: SMT3; NbExp=2; IntAct=EBI-10541, EBI-17490; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- MISCELLANEOUS: Present with 35100 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- MISCELLANEOUS: Early fractionation of eukaryotic MCM proteins yielded a CC variety of dimeric, trimeric and tetrameric complexes with unclear CC biological significance. The MCM2-7 hexamer is the proposed CC physiological active complex. CC -!- SIMILARITY: Belongs to the MCM 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; X53540; CAA37616.1; -; Genomic_DNA. DR EMBL; U18779; AAB65010.1; -; Genomic_DNA. DR EMBL; BK006939; DAA07621.1; -; Genomic_DNA. DR PIR; A36376; A36376. DR RefSeq; NP_010882.1; NM_001178847.1. DR PDB; 3JA8; EM; 3.80 A; 3=1-971. DR PDB; 3JC5; EM; 4.70 A; 3=1-971. DR PDB; 3JC6; EM; 3.70 A; 3=1-971. DR PDB; 3JC7; EM; 4.80 A; 3=1-971. DR PDB; 5BK4; EM; 3.90 A; 3/B=1-971. DR PDB; 5U8S; EM; 6.10 A; 3=1-971. DR PDB; 5U8T; EM; 4.90 A; 3=1-971. DR PDB; 5V8F; EM; 3.90 A; 3=1-971. DR PDB; 5XF8; EM; 7.10 A; 3=1-971. DR PDB; 6EYC; EM; 3.80 A; 3=1-971. DR PDB; 6F0L; EM; 4.77 A; 3/B=1-971. DR PDB; 6HV9; EM; 4.98 A; 3=1-971. DR PDB; 6PTJ; EM; 3.80 A; 3=1-971. DR PDB; 6PTN; EM; 5.80 A; 3/j=1-971. DR PDB; 6PTO; EM; 7.00 A; 3/G/i=1-971. DR PDB; 6RQC; EM; 4.40 A; 3=1-971. DR PDB; 6SKL; EM; 3.70 A; 3=1-971. DR PDB; 6SKO; EM; 3.40 A; 3=1-971. DR PDB; 6U0M; EM; 3.90 A; 3=17-738. DR PDB; 6WGC; EM; 4.30 A; 3=1-971. DR PDB; 6WGF; EM; 7.70 A; 3=1-971. DR PDB; 6WGG; EM; 8.10 A; 3=1-971. DR PDB; 6WGI; EM; 10.00 A; 3=1-971. DR PDB; 7P30; EM; 3.00 A; 3/B=1-971. DR PDB; 7P5Z; EM; 3.30 A; 3/B=1-971. DR PDB; 7PMK; EM; 3.20 A; 3=1-971. DR PDB; 7PMN; EM; 3.20 A; 3=1-971. DR PDB; 7PT6; EM; 3.20 A; 3/C=1-971. DR PDB; 7PT7; EM; 3.80 A; 3/C=1-971. DR PDB; 7QHS; EM; 3.30 A; 3=1-971. DR PDB; 7V3U; EM; 3.20 A; 3/C=1-971. DR PDB; 7V3V; EM; 2.90 A; 3/C=1-971. DR PDB; 7W8G; EM; 2.52 A; 3/C=1-971. DR PDB; 7Z13; EM; 3.40 A; 3/b=1-971. DR PDB; 8B9A; EM; 3.50 A; 3=1-971. DR PDB; 8B9B; EM; 3.50 A; 3=1-971. DR PDB; 8B9C; EM; 4.60 A; 3=1-971. DR PDB; 8KG6; EM; 3.07 A; 3=1-971. DR PDB; 8KG8; EM; 4.23 A; 3=1-971. DR PDB; 8KG9; EM; 4.52 A; 3=1-971. DR PDB; 8W7M; EM; 4.12 A; 3=1-971. DR PDBsum; 3JA8; -. DR PDBsum; 3JC5; -. DR PDBsum; 3JC6; -. DR PDBsum; 3JC7; -. DR PDBsum; 5BK4; -. DR PDBsum; 5U8S; -. DR PDBsum; 5U8T; -. DR PDBsum; 5V8F; -. DR PDBsum; 5XF8; -. DR PDBsum; 6EYC; -. DR PDBsum; 6F0L; -. DR PDBsum; 6HV9; -. DR PDBsum; 6PTJ; -. DR PDBsum; 6PTN; -. DR PDBsum; 6PTO; -. DR PDBsum; 6RQC; -. DR PDBsum; 6SKL; -. DR PDBsum; 6SKO; -. DR PDBsum; 6U0M; -. DR PDBsum; 6WGC; -. DR PDBsum; 6WGF; -. DR PDBsum; 6WGG; -. DR PDBsum; 6WGI; -. DR PDBsum; 7P30; -. DR PDBsum; 7P5Z; -. DR PDBsum; 7PMK; -. DR PDBsum; 7PMN; -. DR PDBsum; 7PT6; -. DR PDBsum; 7PT7; -. DR PDBsum; 7QHS; -. DR PDBsum; 7V3U; -. DR PDBsum; 7V3V; -. DR PDBsum; 7W8G; -. DR PDBsum; 7Z13; -. DR PDBsum; 8B9A; -. DR PDBsum; 8B9B; -. DR PDBsum; 8B9C; -. DR PDBsum; 8KG6; -. DR PDBsum; 8KG8; -. DR PDBsum; 8KG9; -. DR PDBsum; 8W7M; -. DR AlphaFoldDB; P24279; -. DR EMDB; EMD-0288; -. DR EMDB; EMD-10227; -. DR EMDB; EMD-10230; -. DR EMDB; EMD-13176; -. DR EMDB; EMD-13211; -. DR EMDB; EMD-13537; -. DR EMDB; EMD-13539; -. DR EMDB; EMD-13619; -. DR EMDB; EMD-13620; -. DR EMDB; EMD-13978; -. DR EMDB; EMD-14439; -. DR EMDB; EMD-15924; -. DR EMDB; EMD-20471; -. DR EMDB; EMD-20472; -. DR EMDB; EMD-20473; -. DR EMDB; EMD-20607; -. DR EMDB; EMD-21662; -. DR EMDB; EMD-21664; -. DR EMDB; EMD-21665; -. DR EMDB; EMD-21666; -. DR EMDB; EMD-31684; -. DR EMDB; EMD-31685; -. DR EMDB; EMD-32355; -. DR EMDB; EMD-4980; -. DR EMDB; EMD-6671; -. DR EMDB; EMD-8518; -. DR EMDB; EMD-8519; -. DR EMDB; EMD-8540; -. DR EMDB; EMD-9400; -. DR SMR; P24279; -. DR BioGRID; 36697; 414. DR ComplexPortal; CPX-2944; MCM complex. DR DIP; DIP-2407N; -. DR IntAct; P24279; 35. DR MINT; P24279; -. DR STRING; 4932.YEL032W; -. DR iPTMnet; P24279; -. DR MaxQB; P24279; -. DR PaxDb; 4932-YEL032W; -. DR PeptideAtlas; P24279; -. DR EnsemblFungi; YEL032W_mRNA; YEL032W; YEL032W. DR GeneID; 856680; -. DR KEGG; sce:YEL032W; -. DR AGR; SGD:S000000758; -. DR SGD; S000000758; MCM3. DR VEuPathDB; FungiDB:YEL032W; -. DR eggNOG; KOG0479; Eukaryota. DR GeneTree; ENSGT01050000244824; -. DR HOGENOM; CLU_000995_6_1_1; -. DR InParanoid; P24279; -. DR OMA; VLRTHRY; -. DR OrthoDB; 5476523at2759; -. DR BioCyc; YEAST:G3O-30154-MONOMER; -. DR Reactome; R-SCE-176187; Activation of ATR in response to replication stress. DR Reactome; R-SCE-68867; Assembly of the pre-replicative complex. DR Reactome; R-SCE-68962; Activation of the pre-replicative complex. DR Reactome; R-SCE-69052; Switching of origins to a post-replicative state. DR BioGRID-ORCS; 856680; 4 hits in 10 CRISPR screens. DR PRO; PR:P24279; -. DR Proteomes; UP000002311; Chromosome V. DR RNAct; P24279; Protein. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC. DR GO; GO:0071162; C:CMG complex; IDA:SGD. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0031261; C:DNA replication preinitiation complex; IPI:SGD. DR GO; GO:0042555; C:MCM complex; IDA:SGD. DR GO; GO:0005656; C:nuclear pre-replicative complex; IDA:SGD. DR GO; GO:0043596; C:nuclear replication fork; IDA:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0003682; F:chromatin binding; IDA:SGD. DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:1904931; F:MCM complex binding; IDA:SGD. DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central. DR GO; GO:0006270; P:DNA replication initiation; IMP:SGD. DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IMP:SGD. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:ComplexPortal. DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD. DR GO; GO:1902975; P:mitotic DNA replication initiation; IMP:SGD. DR GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IDA:SGD. DR GO; GO:0006279; P:premeiotic DNA replication; IDA:ComplexPortal. DR GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IMP:SGD. DR GO; GO:0031509; P:subtelomeric heterochromatin formation; IMP:SGD. DR CDD; cd17754; MCM3; 1. DR Gene3D; 2.20.28.10; -; 1. DR Gene3D; 3.30.1640.10; mini-chromosome maintenance (MCM) complex, chain A, domain 1; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR031327; MCM. DR InterPro; IPR008046; Mcm3. DR InterPro; IPR018525; MCM_CS. DR InterPro; IPR001208; MCM_dom. DR InterPro; IPR041562; MCM_lid. DR InterPro; IPR027925; MCM_N. DR InterPro; IPR033762; MCM_OB. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1. DR PANTHER; PTHR11630:SF46; DNA REPLICATION LICENSING FACTOR MCM3; 1. DR Pfam; PF00493; MCM; 1. DR Pfam; PF17855; MCM_lid; 1. DR Pfam; PF14551; MCM_N; 1. DR Pfam; PF17207; MCM_OB; 1. DR PRINTS; PR01657; MCMFAMILY. DR PRINTS; PR01659; MCMPROTEIN3. DR SMART; SM00382; AAA; 1. DR SMART; SM00350; MCM; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00847; MCM_1; 1. DR PROSITE; PS50051; MCM_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; DNA replication; DNA-binding; Helicase; KW Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome. FT CHAIN 1..971 FT /note="DNA replication licensing factor MCM3" FT /id="PRO_0000194099" FT DOMAIN 359..566 FT /note="MCM" FT REGION 52..78 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 594..614 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 749..825 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 842..893 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 541..544 FT /note="Arginine finger" FT COMPBIAS 58..74 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 772..803 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 842..856 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 869..893 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 409..416 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT MOD_RES 761 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 777 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT MOD_RES 781 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358, FT ECO:0007744|PubMed:19779198" FT MOD_RES 868 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17330950" FT MUTAGEN 415 FT /note="K->A: No effect on MCM2-7 complex helicase activity. FT Loss of MCM2-7 complex helicase activity; when associated FT with MCM5 A-422. Reduces MCM2-7 complex helicase activity; FT when associated with MCM2 A-549." FT /evidence="ECO:0000269|PubMed:18657510" FT HELIX 17..34 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 37..54 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 94..99 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 100..106 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 108..116 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 118..135 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 154..159 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:7PMK" FT TURN 168..170 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 178..187 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 193..203 FT /evidence="ECO:0007829|PDB:7PMK" FT TURN 204..206 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 209..213 FT /evidence="ECO:0007829|PDB:7PMK" FT TURN 217..219 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 240..243 FT /evidence="ECO:0007829|PDB:7PMK" FT TURN 245..247 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 248..259 FT /evidence="ECO:0007829|PDB:7PMK" FT TURN 262..264 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 273..279 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 280..282 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 291..302 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 317..328 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 344..354 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 359..366 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 375..385 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 394..396 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 405..409 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 415..425 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 426..433 FT /evidence="ECO:0007829|PDB:7PMK" FT TURN 434..436 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 439..442 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 443..448 FT /evidence="ECO:0007829|PDB:7PMK" FT TURN 450..452 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 455..459 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 461..464 FT /evidence="ECO:0007829|PDB:7PMK" FT TURN 465..467 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 468..474 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 475..477 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 480..483 FT /evidence="ECO:0007829|PDB:7PMK" FT TURN 484..486 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 487..492 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 493..499 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 502..507 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 510..516 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 519..522 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 529..532 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 537..540 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 543..549 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 555..569 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 653..666 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 673..687 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 700..715 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 719..721 FT /evidence="ECO:0007829|PDB:6SKO" FT HELIX 723..738 FT /evidence="ECO:0007829|PDB:7PMK" SQ SEQUENCE 971 AA; 107518 MW; 43DD4DACAF4456DC CRC64; MEGSTGFDGD ATTFFAPDAV FGDRVRRFQE FLDTFTSYRD SVRSIQVYNS NNAANYNDDQ DDADERDLLG DDDGDDLEKE KKAASSTSLN ILPHRIIISL DDLREFDRSF WSGILVEPAY FIPPAEKALT DLADSMDDVP HPNASAVSSR HPWKLSFKGS FGAHALSPRT LTAQHLNKLV SVEGIVTKTS LVRPKLIRSV HYAAKTGRFH YRDYTDATTT LTTRIPTPAI YPTEDTEGNK LTTEYGYSTF IDHQRITVQE MPEMAPAGQL PRSIDVILDD DLVDKTKPGD RVNVVGVFKS LGAGGMNQSN SNTLIGFKTL ILGNTVYPLH ARSTGVAARQ MLTDFDIRNI NKLSKKKDIF DILSQSLAPS IYGHDHIKKA ILLMLMGGVE KNLENGSHLR GDINILMVGD PSTAKSQLLR FVLNTASLAI ATTGRGSSGV GLTAAVTTDR ETGERRLEAG AMVLADRGVV CIDEFDKMTD VDRVAIHEVM EQQTVTIAKA GIHTTLNARC SVIAAANPVF GQYDVNRDPH QNIALPDSLL SRFDLLFVVT DDINEIRDRS ISEHVLRTHR YLPPGYLEGE PVRERLNLSL AVGEDADINP EEHSNSGAGV ENEGEDDEDH VFEKFNPLLQ AGAKLAKNKG NYNGTEIPKL VTIPFLRKYV QYAKERVIPQ LTQEAINVIV KNYTDLRNDD NTKKSPITAR TLETLIRLAT AHAKVRLSKT VNKVDAKVAA NLLRFALLGE DIGNDIDEEE SEYEEALSKR SPQKSPKKRQ RVRQPASNSG SPIKSTPRRS TASSVNATPS SARRILRFQD DEQNAGEDDN DIMSPLPADE EAELQRRLQL GLRVSPRRRE HLHAPEEGSS GPLTEVGTPR LPNVSSAGQD DEQQQSVISF DNVEPGTIST GRLSLISGII ARLMQTEIFE EESYPVASLF ERINEELPEE EKFSAQEYLA GLKIMSDRNN LMVADDKVWR V //