MCM3_YEAST
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 03-AUG-2022, entry version 211.
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 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}.
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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; 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 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; 7V3U; -.
DR PDBsum; 7V3V; -.
DR PDBsum; 7W8G; -.
DR AlphaFoldDB; P24279; -.
DR SMR; P24279; -.
DR BioGRID; 36697; 407.
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; P24279; -.
DR PRIDE; P24279; -.
DR EnsemblFungi; YEL032W_mRNA; YEL032W; YEL032W.
DR GeneID; 856680; -.
DR KEGG; sce:YEL032W; -.
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; RNDQNTK; -.
DR BioCyc; YEAST:G3O-30154-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: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: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: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:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:ComplexPortal.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 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; PTHR11630; 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; 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; 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
