ID MCM2_YEAST Reviewed; 868 AA. AC P29469; D6VPX7; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 2. DT 27-MAR-2024, entry version 215. DE RecName: Full=DNA replication licensing factor MCM2; DE EC=3.6.4.12; DE AltName: Full=Minichromosome maintenance protein 2; GN Name=MCM2; OrderedLocusNames=YBL023C; ORFNames=YBL0438; 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 MUTAGENESIS OF CYS-364 AND CYS-367. RX PubMed=2044961; DOI=10.1101/gad.5.6.944; RA Yan H., Gibson S., Tye B.K.; RT "Mcm2 and Mcm3, two proteins important for ARS activity, are related in RT structure and function."; RL Genes Dev. 5:944-957(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7725803; DOI=10.1002/yea.320101217; RA van Dyck L., Jonniaux J.-L., Barreiros T.D.M., Kleine K., Goffeau A.; RT "Analysis of a 17.4 kb DNA segment of yeast chromosome II encompassing the RT ribosomal protein L19 as well as proteins with homologies to components of RT the hnRNP and snRNP complexes and to the human proliferation-associated RT p120 antigen."; RL Yeast 10:1663-1673(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [4] RP RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7 RP COMPLEX, AND MUTAGENESIS OF LYS-549 AND ARG-676. 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 [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=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 [6] 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 [7] 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 [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-85. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8276800; DOI=10.1016/s0021-9258(17)42340-4; RA van Dyck L., Pearce D.A., Sherman F.; RT "PIM1 encodes a mitochondrial ATP-dependent protease that is required for RT mitochondrial function in the yeast Saccharomyces cerevisiae."; RL J. Biol. Chem. 269:238-242(1994). 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-14; SER-16; SER-23; SER-164 RP AND SER-170, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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; 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. 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. CC {ECO:0000269|PubMed:19896182, ECO:0000269|PubMed:19910535}. CC -!- INTERACTION: CC P29469; P09119: CDC6; NbExp=4; IntAct=EBI-10533, EBI-4447; CC P29469; Q08496: DIA2; NbExp=4; IntAct=EBI-10533, EBI-31943; CC P29469; P30665: MCM4; NbExp=15; IntAct=EBI-10533, EBI-4326; CC P29469; Q12306: SMT3; NbExp=2; IntAct=EBI-10533, EBI-17490; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- MISCELLANEOUS: Present with 1690 molecules/cell in log phase SD medium. CC {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. Specifically a MCM467 subcomplex is shown to CC have in vitro helicase activity which is inhibited by the MCM2 subunit. CC The MCM2-7 hexamer is the proposed 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; X77291; CAA54503.1; -; Genomic_DNA. DR EMBL; X53539; CAA37615.1; -; Genomic_DNA. DR EMBL; Z35784; CAA84842.1; -; Genomic_DNA. DR EMBL; X74544; CAA52635.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07097.1; -; Genomic_DNA. DR PIR; S45757; S45757. DR RefSeq; NP_009530.1; NM_001178263.1. DR PDB; 3JA8; EM; 3.80 A; 2=1-868. DR PDB; 3JC5; EM; 4.70 A; 2=1-868. DR PDB; 3JC6; EM; 3.70 A; 2=1-868. DR PDB; 3JC7; EM; 4.80 A; 2=1-868. DR PDB; 5BK4; EM; 3.90 A; 2/A=1-868. DR PDB; 5U8S; EM; 6.10 A; 2=1-868. DR PDB; 5U8T; EM; 4.90 A; 2=1-868. DR PDB; 5V8F; EM; 3.90 A; 2=1-868. DR PDB; 5XF8; EM; 7.10 A; 2=1-868. DR PDB; 6EYC; EM; 3.80 A; 2=1-868. DR PDB; 6F0L; EM; 4.77 A; 2/A=1-868. DR PDB; 6HV9; EM; 4.98 A; 2=1-868. DR PDB; 6PTJ; EM; 3.80 A; 2=1-868. DR PDB; 6PTN; EM; 5.80 A; 2/i=1-868. DR PDB; 6PTO; EM; 7.00 A; 2/F/h=1-868. DR PDB; 6RQC; EM; 4.40 A; 2=1-868. DR PDB; 6SKL; EM; 3.70 A; 2=1-868. DR PDB; 6SKO; EM; 3.40 A; 2=1-868. DR PDB; 6U0M; EM; 3.90 A; 2=201-864. DR PDB; 6WGF; EM; 7.70 A; 2=1-868. DR PDB; 6WGG; EM; 8.10 A; 2=1-868. DR PDB; 6WGI; EM; 10.00 A; 2=1-868. DR PDB; 7P30; EM; 3.00 A; 2/A=1-868. DR PDB; 7P5Z; EM; 3.30 A; 2/A=1-868. DR PDB; 7PMK; EM; 3.20 A; 2=1-868. DR PDB; 7PMN; EM; 3.20 A; 2=1-868. DR PDB; 7PT6; EM; 3.20 A; 2/B=1-868. DR PDB; 7PT7; EM; 3.80 A; 2/B=1-868. DR PDB; 7V3U; EM; 3.20 A; 2/B=1-868. DR PDB; 7V3V; EM; 2.90 A; 2/B=1-868. DR PDB; 7W8G; EM; 2.52 A; 2/B=1-868. DR PDB; 8B9A; EM; 3.50 A; 2=1-868. DR PDB; 8B9B; EM; 3.50 A; 2=1-868. DR PDB; 8B9C; EM; 4.60 A; 2=1-868. DR PDB; 8KG6; EM; 3.07 A; 2=1-868. DR PDB; 8KG8; EM; 4.23 A; 2=1-868. 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; 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; 7V3U; -. DR PDBsum; 7V3V; -. DR PDBsum; 7W8G; -. DR PDBsum; 8B9A; -. DR PDBsum; 8B9B; -. DR PDBsum; 8B9C; -. DR PDBsum; 8KG6; -. DR PDBsum; 8KG8; -. DR AlphaFoldDB; P29469; -. 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-15924; -. 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-4980; -. DR EMDB; EMD-6671; -. DR EMDB; EMD-8518; -. DR EMDB; EMD-8519; -. DR EMDB; EMD-8540; -. DR EMDB; EMD-9400; -. DR SMR; P29469; -. DR BioGRID; 32675; 255. DR ComplexPortal; CPX-2944; MCM complex. DR DIP; DIP-2291N; -. DR IntAct; P29469; 53. DR MINT; P29469; -. DR STRING; 4932.YBL023C; -. DR iPTMnet; P29469; -. DR MaxQB; P29469; -. DR PaxDb; 4932-YBL023C; -. DR PeptideAtlas; P29469; -. DR EnsemblFungi; YBL023C_mRNA; YBL023C; YBL023C. DR GeneID; 852258; -. DR KEGG; sce:YBL023C; -. DR AGR; SGD:S000000119; -. DR SGD; S000000119; MCM2. DR VEuPathDB; FungiDB:YBL023C; -. DR eggNOG; KOG0477; Eukaryota. DR GeneTree; ENSGT01050000244824; -. DR HOGENOM; CLU_000995_0_0_1; -. DR InParanoid; P29469; -. DR OMA; TYERVTT; -. DR OrthoDB; 5476523at2759; -. DR BioCyc; YEAST:G3O-28926-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; 852258; 0 hits in 10 CRISPR screens. DR PRO; PR:P29469; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; P29469; Protein. 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; IDA: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:RHEA. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006974; P:DNA damage response; 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 CDD; cd17753; MCM2; 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; IPR008045; MCM2. 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:SF44; DNA REPLICATION LICENSING FACTOR MCM2; 1. DR Pfam; PF00493; MCM; 1. DR Pfam; PF12619; MCM2_N; 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; PR01658; MCMPROTEIN2. 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; Cell cycle; DNA replication; DNA-binding; KW Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger. FT CHAIN 1..868 FT /note="DNA replication licensing factor MCM2" FT /id="PRO_0000194091" FT DOMAIN 493..700 FT /note="MCM" FT ZN_FING 341..367 FT /note="C4-type" FT /evidence="ECO:0000255" FT REGION 1..65 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 87..106 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 704..728 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 675..678 FT /note="Arginine finger" FT COMPBIAS 1..15 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 19..33 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 49..65 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 704..727 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 543..550 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 16 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 23 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 164 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 170 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT VARIANT 392 FT /note="E -> K (in allele MCM2-1)" FT MUTAGEN 364 FT /note="C->Y,F,S,H: Loss of activity." FT /evidence="ECO:0000269|PubMed:2044961" FT MUTAGEN 367 FT /note="C->Y,F,S,H: Loss of activity." FT /evidence="ECO:0000269|PubMed:2044961" FT MUTAGEN 549 FT /note="K->A: Reduces MCM2-7 complex helicase activity. FT Abolishes MCM2-7 complex helicase activity; when associated FT with MCM5 A-422. Reduces MCM2-7 complex helicase activity; FT when associated with MCM3 A-415." FT /evidence="ECO:0000269|PubMed:18657510" FT MUTAGEN 676 FT /note="R->A: Loss of MCM2-7 complex helicase activity." FT /evidence="ECO:0000269|PubMed:18657510" FT CONFLICT 164 FT /note="S -> T (in Ref. 1; CAA37615)" FT /evidence="ECO:0000305" FT CONFLICT 172..173 FT /note="MD -> IH (in Ref. 1; CAA37615)" FT /evidence="ECO:0000305" FT CONFLICT 529 FT /note="G -> P (in Ref. 1; CAA37615)" FT /evidence="ECO:0000305" FT CONFLICT 578 FT /note="A -> R (in Ref. 1; CAA37615)" FT /evidence="ECO:0000305" FT CONFLICT 583 FT /note="D -> H (in Ref. 1; CAA37615)" FT /evidence="ECO:0000305" FT CONFLICT 712 FT /note="E -> Q (in Ref. 1; CAA37615)" FT /evidence="ECO:0000305" FT CONFLICT 733..747 FT /note="Missing (in Ref. 1; CAA37615)" FT /evidence="ECO:0000305" FT CONFLICT 859..868 FT /note="RSFAIYTLGH -> SLSQFIPWVTKTLLFLRISGYEDKKFSVSIHVLAILFS FT IYKFPLFFV (in Ref. 1; CAA37615)" FT /evidence="ECO:0000305" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 183..187 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 191..193 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 194..198 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 201..217 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 226..237 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 240..245 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 246..250 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 251..253 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 254..262 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 264..282 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 286..288 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 294..298 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 306..308 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 311..313 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 316..327 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 331..345 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 347..352 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 362..364 FT /evidence="ECO:0007829|PDB:7PMK" FT TURN 365..368 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 373..391 FT /evidence="ECO:0007829|PDB:7PMK" FT TURN 394..396 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 405..411 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 412..414 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 423..433 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 436..442 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 448..457 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 478..488 FT /evidence="ECO:0007829|PDB:7PMK" FT TURN 490..492 FT /evidence="ECO:0007829|PDB:6SKO" FT HELIX 493..500 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 509..520 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 525..527 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 539..543 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 545..548 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 549..559 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 560..565 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 568..570 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 573..576 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 577..582 FT /evidence="ECO:0007829|PDB:7PMK" FT TURN 584..586 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 588..593 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 595..598 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 600..606 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 609..611 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 614..617 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 618..620 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 621..624 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 628..633 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 636..641 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 644..650 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 653..655 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 659..661 FT /evidence="ECO:0007829|PDB:6SKO" FT HELIX 663..666 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 671..676 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 679..683 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 689..705 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 740..752 FT /evidence="ECO:0007829|PDB:7PMK" FT TURN 753..755 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 760..773 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 783..796 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 807..823 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 827..829 FT /evidence="ECO:0007829|PDB:6SKO" FT HELIX 831..847 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 851..865 FT /evidence="ECO:0007829|PDB:7PMK" SQ SEQUENCE 868 AA; 98780 MW; F38FF682581B0EC0 CRC64; MSDNRRRRRE EDDSDSENEL PPSSPQQHFR GGMNPVSSPI GSPDMINPEG DDNEVDDVPD IDEVEEQMNE VDLMDDNMYE DYAADHNRDR YDPDQVDDRE QQELSLSERR RIDAQLNERD RLLRNVAYID DEDEEQEGAA QLDEMGLPVQ RRRRRRQYED LENSDDDLLS DMDIDPLREE LTLESLSNVK ANSYSEWITQ PNVSRTIARE LKSFLLEYTD ETGRSVYGAR IRTLGEMNSE SLEVNYRHLA ESKAILALFL AKCPEEMLKI FDLVAMEATE LHYPDYARIH SEIHVRISDF PTIYSLRELR ESNLSSLVRV TGVVTRRTGV FPQLKYVKFN CLKCGSILGP FFQDSNEEIR ISFCTNCKSK GPFRVNGEKT VYRNYQRVTL QEAPGTVPPG RLPRHREVIL LADLVDVSKP GEEVEVTGIY KNNYDGNLNA KNGFPVFATI IEANSIKRRE GNTANEGEEG LDVFSWTEEE EREFRKISRD RGIIDKIISS MAPSIYGHRD IKTAVACSLF GGVPKNVNGK HSIRGDINVL LLGDPGTAKS QILKYVEKTA HRAVFATGQG ASAVGLTASV RKDPITKEWT LEGGALVLAD KGVCLIDEFD KMNDQDRTSI HEAMEQQSIS ISKAGIVTTL QARCSIIAAA NPNGGRYNST LPLAQNVSLT EPILSRFDIL CVVRDLVDEE ADERLATFVV DSHVRSHPEN DEDREGEELK NNGESAIEQG EDEINEQLNA RQRRLQRQRK KEEEISPIPQ ELLMKYIHYA RTKIYPKLHQ MDMDKVSRVY ADLRRESIST GSFPITVRHL ESILRIAESF AKMRLSEFVS SYDLDRAIKV VVDSFVDAQK VSVRRQLRRS FAIYTLGH //