MCM6_YEAST
ID MCM6_YEAST Reviewed; 1017 AA.
AC P53091; D6VTV3; Q870M9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=DNA replication licensing factor MCM6;
DE EC=3.6.4.12;
DE AltName: Full=Minichromosome maintenance protein 6;
GN Name=MCM6; OrderedLocusNames=YGL201C;
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;
RA Duina A.A., Winston F.;
RT "Sequence of the Saccharomyces cerevisiae MCM6 gene.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-766, 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 RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7
RP COMPLEX, AND MUTAGENESIS OF LYS-581.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-372, AND
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 [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=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 [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=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 [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 456-1017.
RC STRAIN=Sigma 1278B;
RX PubMed=9491083; DOI=10.1007/s004380050644;
RA Iraqui I., Vissers S., Cartiaux M., Urrestarazu A.;
RT "Characterisation of Saccharomyces cerevisiae ARO8 and ARO9 genes encoding
RT aromatic aminotransferases I and II reveals a new aminotransferase
RT subfamily.";
RL Mol. Gen. Genet. 257:238-248(1998).
RN [10]
RP INTERACTION WITH MCM10.
RX PubMed=9154825; DOI=10.1128/mcb.17.6.3261;
RA Merchant A.M., Kawasaki Y., Chen Y., Lei M., Tye B.K.;
RT "A lesion in the DNA replication initiation factor Mcm10 induces pausing of
RT elongation forks through chromosomal replication origins in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 17:3261-3271(1997).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION BY
RP 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 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 Required for the entry in S phase and for cell division.
CC {ECO:0000269|PubMed:19896182, 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 MCM10. {ECO:0000269|PubMed:19896182, ECO:0000269|PubMed:19910535,
CC ECO:0000269|PubMed:9154825}.
CC -!- INTERACTION:
CC P53091; P32354: MCM10; NbExp=5; IntAct=EBI-10556, EBI-5965;
CC P53091; P30665: MCM4; NbExp=7; IntAct=EBI-10556, EBI-4326;
CC P53091; Q12306: SMT3; NbExp=2; IntAct=EBI-10556, EBI-17490;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 13400 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. 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; AY258324; AAO89010.1; -; Genomic_DNA.
DR EMBL; Z72723; CAA96913.1; -; Genomic_DNA.
DR EMBL; Y13624; CAA73947.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07914.1; -; Genomic_DNA.
DR PIR; S64219; S64219.
DR RefSeq; NP_011314.2; NM_001181066.1.
DR PDB; 3JA8; EM; 3.80 A; 6=1-1017.
DR PDB; 3JC5; EM; 4.70 A; 6=1-1017.
DR PDB; 3JC6; EM; 3.70 A; 6=1-1017.
DR PDB; 3JC7; EM; 4.80 A; 6=1-1017.
DR PDB; 5BK4; EM; 3.90 A; 6/E=1-1017.
DR PDB; 5U8S; EM; 6.10 A; 6=1-1017.
DR PDB; 5U8T; EM; 4.90 A; 6=1-1017.
DR PDB; 5V8F; EM; 3.90 A; 6=1-1017.
DR PDB; 5XF8; EM; 7.10 A; 6=1-1017.
DR PDB; 6EYC; EM; 3.80 A; 6=1-1017.
DR PDB; 6F0L; EM; 4.77 A; 6/E=1-1017.
DR PDB; 6HV9; EM; 4.98 A; 6=1-1017.
DR PDB; 6PTJ; EM; 3.80 A; 6=1-1017.
DR PDB; 6PTN; EM; 5.80 A; 6/m=1-1017.
DR PDB; 6PTO; EM; 7.00 A; 6/J/l=1-1017.
DR PDB; 6RQC; EM; 4.40 A; 6=1-1017.
DR PDB; 6SKL; EM; 3.70 A; 6=1-1017.
DR PDB; 6SKO; EM; 3.40 A; 6=1-1017.
DR PDB; 6U0M; EM; 3.90 A; 6=103-840.
DR PDB; 6WGF; EM; 7.70 A; 6=1-1017.
DR PDB; 6WGG; EM; 8.10 A; 6=1-1017.
DR PDB; 6WGI; EM; 10.00 A; 6=1-1017.
DR PDB; 7P30; EM; 3.00 A; 6/E=1-1017.
DR PDB; 7P5Z; EM; 3.30 A; 6/E=1-1017.
DR PDB; 7PMK; EM; 3.20 A; 6=1-1017.
DR PDB; 7PMN; EM; 3.20 A; 6=1-1017.
DR PDB; 7V3U; EM; 3.20 A; 6/F=1-1017.
DR PDB; 7V3V; EM; 2.90 A; 6/F=1-1017.
DR PDB; 7W8G; EM; 2.52 A; 6/F=1-1017.
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; 7V3U; -.
DR PDBsum; 7V3V; -.
DR PDBsum; 7W8G; -.
DR AlphaFoldDB; P53091; -.
DR SMR; P53091; -.
DR BioGRID; 33056; 203.
DR ComplexPortal; CPX-2944; MCM complex.
DR DIP; DIP-1294N; -.
DR IntAct; P53091; 59.
DR MINT; P53091; -.
DR STRING; 4932.YGL201C; -.
DR iPTMnet; P53091; -.
DR MaxQB; P53091; -.
DR PaxDb; P53091; -.
DR PRIDE; P53091; -.
DR EnsemblFungi; YGL201C_mRNA; YGL201C; YGL201C.
DR GeneID; 852673; -.
DR KEGG; sce:YGL201C; -.
DR SGD; S000003169; MCM6.
DR VEuPathDB; FungiDB:YGL201C; -.
DR eggNOG; KOG0480; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR HOGENOM; CLU_000995_3_0_1; -.
DR InParanoid; P53091; -.
DR OMA; KYYIAQI; -.
DR BioCyc; YEAST:G3O-30681-MON; -.
DR Reactome; R-SCE-68867; Assembly of the pre-replicative complex.
DR Reactome; R-SCE-68949; Orc1 removal from chromatin.
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 PRO; PR:P53091; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53091; 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:0097373; C:MCM core 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:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IDA:SGD.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
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:SGD.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR GO; GO:1902969; P:mitotic DNA replication; IBA:GO_Central.
DR GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IDA:SGD.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:ComplexPortal.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008049; MCM6.
DR InterPro; IPR041024; Mcm6_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; PTHR11630; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF18263; MCM6_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; PR01662; MCMPROTEIN6.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 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; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1017
FT /note="DNA replication licensing factor MCM6"
FT /id="PRO_0000194117"
FT DOMAIN 525..732
FT /note="MCM"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 707..710
FT /note="Arginine finger"
FT COMPBIAS 1..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 575..582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 766
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MUTAGEN 581
FT /note="K->A: Loss of MCM2-7 complex helicase activity."
FT /evidence="ECO:0000269|PubMed:18657510"
FT CONFLICT 179
FT /note="P -> A (in Ref. 2; CAA96913)"
FT /evidence="ECO:0000305"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 106..121
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 174..192
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 286..297
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 301..314
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 351..362
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 394..405
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 407..410
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 441..445
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 450..461
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 501..505
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 510..520
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 525..532
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 541..551
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 571..575
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 582..591
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 592..599
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 600..602
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 605..608
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 609..613
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 622..625
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 627..630
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 631..633
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 634..639
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 641..643
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 646..650
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 653..657
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 659..665
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 668..673
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 676..681
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 695..698
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 703..706
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 709..715
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 721..734
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 738..740
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 748..758
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 767..784
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 787..790
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 797..813
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 817..819
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 821..835
FT /evidence="ECO:0007829|PDB:7PMK"
SQ SEQUENCE 1017 AA; 112978 MW; 03AB793134E64A50 CRC64;
MSSPFPADTP SSNRPSNSSP PPSSIGAGFG SSSGLDSQIG SRLHFPSSSQ PHVSNSQTGP
FVNDSTQFSS QRLQTDGSAT NDMEGNEPAR SFKSRALNHV KKVDDVTGEK VREAFEQFLE
DFSVQSTDTG EVEKVYRAQI EFMKIYDLNT IYIDYQHLSM RENGALAMAI SEQYYRFLPF
LQKGLRRVVR KYAPELLNTS DSLKRSEGDE GQADEDEQQD DDMNGSSLPR DSGSSAAPGN
GTSAMATRSI TTSTSPEQTE RVFQISFFNL PTVHRIRDIR SEKIGSLLSI SGTVTRTSEV
RPELYKASFT CDMCRAIVDN VEQSFKYTEP TFCPNPSCEN RAFWTLNVTR SRFLDWQKVR
IQENANEIPT GSMPRTLDVI LRGDSVERAK PGDRCKFTGV EIVVPDVTQL GLPGVKPSST
LDTRGISKTT EGLNSGVTGL RSLGVRDLTY KISFLACHVI SIGSNIGASS PDANSNNRET
ELQMAANLQA NNVYQDNERD QEVFLNSLSS DEINELKEMV KDEHIYDKLV RSIAPAVFGH
EAVKKGILLQ MLGGVHKSTV EGIKLRGDIN ICVVGDPSTS KSQFLKYVVG FAPRSVYTSG
KASSAAGLTA AVVRDEEGGD YTIEAGALML ADNGICCIDE FDKMDISDQV AIHEAMEQQT
ISIAKAGIHA TLNARTSILA AANPVGGRYN RKLSLRGNLN MTAPIMSRFD LFFVILDDCN
EKIDTELASH IVDLHMKRDE AIEPPFSAEQ LRRYIKYART FKPILTKEAR SYLVEKYKEL
RKDDAQGFSR SSYRITVRQL ESMIRLSEAI ARANCVDEIT PSFIAEAYDL LRQSIIRVDV
DDVEMDEEFD NIESQSHAAS GNNDDNDDGT GSGVITSEPP ADIEEGQSEA TARPGTSEKK
KTTVTYDKYV SMMNMIVRKI AEVDREGAEE LTAVDIVDWY LLQKENDLGS LAEYWEERRL
AFKVIKRLVK DRILMEIHGT RHNLRDLENE ENENNKTVYV IHPNCEVLDQ LEPQDSS
