ID MCM5_YEAST Reviewed; 775 AA. AC P29496; D6VYS1; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 04-NOV-2026, entry version 220. DE RecName: Full=Minichromosome maintenance protein 5; DE EC=3.6.4.12; DE AltName: Full=Cell division control protein 46; GN Name=MCM5; Synonyms=CDC46; OrderedLocusNames=YLR274W; GN ORFNames=L9328.1; 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. RX PubMed=2044962; DOI=10.1101/gad.5.6.958; RA Hennessy K.M., Lee A., Chen E., Botstein D.; RT "A group of interacting yeast DNA replication genes."; RL Genes Dev. 5:958-969(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169871; DOI=10.1038/387s087; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., RA Zollner A., Hani J., Hoheisel J.D.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; RL Nature 387:87-90(1997). RN [3] RP RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7 RP COMPLEX, AND MUTAGENESIS OF LYS-422. 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 [4] 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 [5] 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 [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 IDENTIFICATION OF CDC46 WITH MCM5. RX PubMed=1438234; DOI=10.1073/pnas.89.21.10459; RA Chen Y., Hennessy K.M., Botstein D., Tye B.-K.; RT "CDC46/MCM5, a yeast protein whose subcellular localization is cell cycle- RT regulated, is involved in DNA replication at autonomously replicating RT sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 89:10459-10463(1992). 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 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). 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; specifically the MCM2- CC MCM5 association is proposed to be reversible and to mediate a open CC ring conformation which may facilitate DNA loading. Once loaded onto CC DNA, double hexamers can slide on dsDNA in the absence of ATPase CC activity. {ECO:0000269|PubMed:19896182, ECO:0000269|PubMed:19910535}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + phosphate + H(+); 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 P29496; P25651: CSM1; NbExp=2; IntAct=EBI-10549, EBI-22001; CC P29496; P24279: MCM3; NbExp=6; IntAct=EBI-10549, EBI-10541; CC P29496; Q12146: PSF3; NbExp=2; IntAct=EBI-10549, EBI-30392; CC P29496; Q12306: SMT3; NbExp=3; IntAct=EBI-10549, EBI-17490; CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Mobilized from the cytoplasm to the CC nucleus as mitosis is completed. Remains in the nucleus until the CC initiation of the next round of replication. CC -!- MISCELLANEOUS: Present with 10300 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; U09242; AAA18027.1; -; Unassigned_DNA. DR EMBL; U17245; AAB67364.1; -; Genomic_DNA. DR EMBL; BK006945; DAA09587.1; -; Genomic_DNA. DR PIR; A39631; A39631. DR RefSeq; NP_013376.1; NM_001182161.1. DR PDB; 28VY; EM; 2.70 A; 5=1-775. DR PDB; 3JA8; EM; 3.80 A; 5=1-775. DR PDB; 3JC5; EM; 4.70 A; 5=1-775. DR PDB; 3JC6; EM; 3.70 A; 5=1-775. DR PDB; 3JC7; EM; 4.80 A; 5=1-775. DR PDB; 5BK4; EM; 3.90 A; 5/D=1-775. DR PDB; 5U8S; EM; 6.10 A; 5=1-775. DR PDB; 5U8T; EM; 4.90 A; 5=1-775. DR PDB; 5V8F; EM; 3.90 A; 5=1-775. DR PDB; 5XF8; EM; 7.10 A; 5=1-775. DR PDB; 6EYC; EM; 3.80 A; 5=1-775. DR PDB; 6F0L; EM; 4.77 A; 5/D=1-775. DR PDB; 6HV9; EM; 4.98 A; 5=1-775. DR PDB; 6PTJ; EM; 3.80 A; 5=1-775. DR PDB; 6PTN; EM; 5.80 A; 5/l=1-775. DR PDB; 6PTO; EM; 7.00 A; 5/I/k=1-775. DR PDB; 6RQC; EM; 4.40 A; 5=1-775. DR PDB; 6SKL; EM; 3.70 A; 5=1-775. DR PDB; 6SKO; EM; 3.40 A; 5=1-775. DR PDB; 6U0M; EM; 3.90 A; 5=24-693. DR PDB; 6WGF; EM; 7.70 A; 5=1-775. DR PDB; 6WGG; EM; 8.10 A; 5=1-775. DR PDB; 6WGI; EM; 10.00 A; 5=1-775. DR PDB; 7P30; EM; 3.00 A; 5/D=1-775. DR PDB; 7P5Z; EM; 3.30 A; 5/D=1-775. DR PDB; 7PMK; EM; 3.20 A; 5=1-775. DR PDB; 7PMN; EM; 3.20 A; 5=1-775. DR PDB; 7PT6; EM; 3.20 A; 5/E=1-775. DR PDB; 7PT7; EM; 3.80 A; 5/E=1-775. DR PDB; 7V3U; EM; 3.20 A; 5/E=1-775. DR PDB; 7V3V; EM; 2.90 A; 5/E=1-775. DR PDB; 7W8G; EM; 2.52 A; 5/E=1-775. DR PDB; 8B9A; EM; 3.50 A; 5=1-775. DR PDB; 8B9B; EM; 3.50 A; 5=1-775. DR PDB; 8B9C; EM; 4.60 A; 5=1-775. DR PDB; 8KG6; EM; 3.07 A; 5=1-775. DR PDB; 8KG8; EM; 4.23 A; 5=1-775. DR PDB; 8KG9; EM; 4.52 A; 5=1-775. DR PDB; 8P5E; EM; 3.90 A; 5=1-775. DR PDB; 8P62; EM; 3.90 A; 5=1-775. DR PDB; 8P63; EM; 3.70 A; 5=1-775. DR PDB; 8RIF; EM; 2.79 A; 5/D=1-775. DR PDB; 8RIG; EM; 3.41 A; 5=1-775. DR PDB; 8W7M; EM; 4.12 A; 5=1-775. DR PDB; 8W7S; EM; 7.39 A; 5=1-775. DR PDB; 8XGC; EM; 3.70 A; 5=1-775. DR PDB; 9BCX; EM; 6.10 A; 5=1-775. DR PDB; 9E2W; EM; 3.30 A; 5=1-775. DR PDB; 9E2X; EM; 3.50 A; 5=1-775. DR PDB; 9E2Y; EM; 3.20 A; 5=1-775. DR PDB; 9GJP; EM; 3.40 A; 5=1-775. DR PDB; 9GJW; EM; 3.30 A; 5=1-775. DR PDB; 9GM5; EM; 3.70 A; 5=1-775. DR PDB; 9I3I; EM; 4.40 A; 5=1-775. DR PDB; 9RHI; EM; 3.20 A; 5=1-775. DR PDB; 9RHJ; EM; 3.40 A; 5/d=1-775. DR PDB; 9RHL; EM; 3.10 A; 5/d=1-775. DR PDB; 9RHM; EM; 3.70 A; 5/d=1-775. DR SMR; P29496; -. DR BioGRID; 31542; 293. DR ComplexPortal; CPX-2944; MCM complex. DR DIP; DIP-2406N; -. DR IntAct; P29496; 81. DR STRING; 4932.YLR274W; -. DR iPTMnet; P29496; -. DR PaxDb; 4932-YLR274W; -. DR PeptideAtlas; P29496; -. DR EnsemblFungi; YLR274W_mRNA; YLR274W; YLR274W. DR GeneID; 850980; -. DR KEGG; sce:YLR274W; -. DR VEuPathDB; FungiDB:YLR274W; -. DR AGR; SGD:S000004264; -. DR SGD; S000004264; MCM5. DR eggNOG; KOG0481; Eukaryota. DR HOGENOM; CLU_000995_7_2_1; -. DR InParanoid; P29496; -. DR OMA; AANPNIF; -. DR OrthoDB; 10036721at2759; -. DR BioCyc; YEAST:G3O-32373-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 EvolutionaryTrace; P29496; -. DR PRO; PR:P29496; -. DR CDD; cd17756; MCM5; 1. DR FunFam; 2.20.28.10:FF:000014; DNA helicase; 1. DR FunFam; 3.30.1640.10:FF:000015; DNA helicase; 1. DR FunFam; 3.40.50.300:FF:000241; DNA helicase; 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; IPR031327; MCM. DR InterPro; IPR008048; MCM5. DR InterPro; IPR054125; MCM5_C. 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:SF42; DNA REPLICATION LICENSING FACTOR MCM5; 1. DR Pfam; PF00493; MCM; 1. DR Pfam; PF21933; MCM5_C; 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; PR01661; MCMPROTEIN5. 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_CTD; 1. DR GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD. 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:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0003682; F:chromatin binding; IDA:SGD. DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC. DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD. DR GO; GO:0006260; P:DNA replication; IDA:ComplexPortal. DR GO; GO:0006270; P:DNA replication initiation; IMP:SGD. DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD. DR GO; GO:0031507; P:heterochromatin formation; IMP:SGD. DR GO; GO:0033260; P:nuclear DNA replication; 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:0030174; P:regulation of DNA-templated DNA replication initiation; IMP:SGD. DR GO; GO:0031509; P:subtelomeric heterochromatin formation; IMP:SGD. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IDA:SGD. DR Proteomes; UP000002311; Chromosome XII. DR RNAct; P29496; protein. DR BioGRID-ORCS; 850980; 1 hit in 10 CRISPR screens. DR AlphaFoldDB; P29496; -. DR EMDB; EMD-10227; -. DR EMDB; EMD-10230; -. DR EMDB; EMD-13176; -. DR EMDB; EMD-13211; -. DR EMDB; EMD-13539; -. DR EMDB; EMD-13619; -. DR EMDB; EMD-13620; -. DR EMDB; EMD-13624; -. DR EMDB; EMD-13629; -. DR EMDB; EMD-13640; -. DR EMDB; EMD-13644; -. DR EMDB; EMD-13647; -. DR EMDB; EMD-13648; -. DR EMDB; EMD-13656; -. DR EMDB; EMD-15924; -. DR EMDB; EMD-17449; -. DR EMDB; EMD-17458; -. DR EMDB; EMD-17459; -. DR EMDB; EMD-19186; -. DR EMDB; EMD-19187; -. DR EMDB; EMD-20471; -. DR EMDB; EMD-20472; -. DR EMDB; EMD-20473; -. DR EMDB; EMD-20607; -. 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-37211; -. DR EMDB; EMD-37213; -. DR EMDB; EMD-37215; -. DR EMDB; EMD-37343; -. DR EMDB; EMD-37345; -. DR EMDB; EMD-38317; -. DR EMDB; EMD-47470; -. DR EMDB; EMD-47471; -. DR EMDB; EMD-47472; -. DR EMDB; EMD-4980; -. DR EMDB; EMD-51401; -. DR EMDB; EMD-51407; -. DR EMDB; EMD-51441; -. DR EMDB; EMD-53970; -. DR EMDB; EMD-53971; -. DR EMDB; EMD-53972; -. DR EMDB; EMD-53973; -. DR EMDB; EMD-56898; -. DR EMDB; EMD-6671; -. DR EMDB; EMD-8518; -. DR EMDB; EMD-8519; -. DR EMDB; EMD-8540; -. DR EMDB; EMD-9400; -. DR FunCoup; P29496; 1389. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell cycle; DNA replication; DNA-binding; KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome. FT CHAIN 1..775 FT /note="Minichromosome maintenance protein 5" FT /id="PRO_0000194111" FT DOMAIN 349..694 FT /note="MCM C-terminal AAA(+) ATPase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01410" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 416..423 FT /note="Walker A" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01410" FT MOTIF 480..483 FT /note="Walker B" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01410" FT BINDING 416..423 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT SITE 549 FT /note="Arginine finger" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01410" FT MUTAGEN 422 FT /note="K->A: Loss of MCM2-7 complex helicase activity." FT /evidence="ECO:0000269|PubMed:18657510" FT STRAND 8..12 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 21..23 FT /evidence="ECO:0007829|PDB:7P30" FT HELIX 24..37 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 40..43 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 45..56 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 60..64 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 65..71 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 73..81 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 83..104 FT /evidence="ECO:0007829|PDB:7W8G" FT TURN 105..108 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 132..135 FT /evidence="ECO:0007829|PDB:7V3U" FT STRAND 136..140 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 144..147 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 153..155 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 158..169 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 173..186 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 189..193 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 200..202 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 213..216 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 219..221 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 222..225 FT /evidence="ECO:0007829|PDB:8RIF" FT STRAND 229..231 FT /evidence="ECO:0007829|PDB:8RIF" FT STRAND 241..244 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 250..259 FT /evidence="ECO:0007829|PDB:7W8G" FT TURN 262..264 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 269..272 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 273..279 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 280..282 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 283..285 FT /evidence="ECO:0007829|PDB:7PT6" FT STRAND 291..301 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 321..323 FT /evidence="ECO:0007829|PDB:8RIF" FT STRAND 325..337 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 351..361 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 366..373 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 382..393 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 401..403 FT /evidence="ECO:0007829|PDB:9E2X" FT STRAND 412..416 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 418..421 FT /evidence="ECO:0007829|PDB:7P30" FT HELIX 422..432 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 433..440 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 441..443 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 446..449 FT /evidence="ECO:0007829|PDB:8KG6" FT STRAND 452..455 FT /evidence="ECO:0007829|PDB:7W8G" FT TURN 457..459 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 462..466 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 468..471 FT /evidence="ECO:0007829|PDB:7W8G" FT TURN 472..474 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 475..481 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 482..484 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 487..498 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 500..505 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 510..514 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 518..523 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 526..529 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 532..534 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 536..539 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 540..542 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 545..548 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 551..556 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 562..577 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 579..590 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 596..609 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 616..618 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 619..640 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 650..666 FT /evidence="ECO:0007829|PDB:7W8G" FT STRAND 670..672 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 674..684 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 685..689 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 690..694 FT /evidence="ECO:0007829|PDB:7W8G" FT TURN 696..698 FT /evidence="ECO:0007829|PDB:7W8G" FT HELIX 708..721 FT /evidence="ECO:0007829|PDB:8KG6" FT STRAND 727..729 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 730..736 FT /evidence="ECO:0007829|PDB:8KG6" FT TURN 739..741 FT /evidence="ECO:0007829|PDB:9GJP" FT HELIX 750..757 FT /evidence="ECO:0007829|PDB:8KG6" FT STRAND 758..760 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 762..764 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 765..767 FT /evidence="ECO:0007829|PDB:9GJP" FT STRAND 768..771 FT /evidence="ECO:0007829|PDB:8KG6" SQ SEQUENCE 775 AA; 86411 MW; 01D9DE208A091CF2 CRC64; MSFDRPEIYS APVLQGESPN DDDNTEIIKS FKNFILEFRL DSQFIYRDQL RNNILVKNYS LTVNMEHLIG YNEDIYKKLS DEPSDIIPLF ETAITQVAKR ISILSRAQSA NNNDKDPENT SMDTDSLLLN SLPTFQLILN SNANQIPLRD LDSEHVSKIV RLSGIIISTS VLSSRATYLS IMCRNCRHTT SITINNFNSI TGNTVSLPRS CLSTIESESS MANESNIGDE STKKNCGPDP YIIIHESSKF IDQQFLKLQE IPELVPVGEM PRNLTMTCDR YLTNKVIPGT RVTIVGIYSI YNSKNGAGSG RSGGGNGGSG VAIRTPYIKI LGIQSDVETS SIWNSVTMFT EEEEEEFLQL SRNPKLYEIL TNSIAPSIFG NEDIKKAIVC LLMGGSKKIL PDGMRLRGDI NVLLLGDPGT AKSQLLKFVE KVSPIAVYTS GKGSSAAGLT ASVQRDPMTR EFYLEGGAMV LADGGVVCID EFDKMRDEDR VAIHEAMEQQ TISIAKAGIT TVLNSRTSVL AAANPIYGRY DDLKSPGDNI DFQTTILSRF DMIFIVKDDH NEERDISIAN HVINIHTGNA NAMQNQQEEN GSEISIEKMK RYITYCRLKC APRLSPQAAE KLSSNFVTIR KQLLINELES TERSSIPITI RQLEAIIRIT ESLAKLELSP IAQERHVDEA IRLFQASTMD AASQDPIGGL NQASGTSLSE IRRFEQELKR RLPIGWSTSY QTLRREFVDT HRFSQLALDK ALYALEKHET IQLRHQGQNI YRSGV //