MCM4_YEAST
ID MCM4_YEAST Reviewed; 933 AA.
AC P30665; D6W429;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=DNA replication licensing factor MCM4;
DE EC=3.6.4.12;
DE AltName: Full=Cell division control protein 54;
GN Name=MCM4; Synonyms=CDC54, HCD21; OrderedLocusNames=YPR019W;
GN ORFNames=YP9531.13;
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].
RA Dalton S.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7
RP COMPLEX, AND MUTAGENESIS OF LYS-574.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-56, 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 [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 571-646.
RX PubMed=1454522; DOI=10.1093/nar/20.21.5571;
RA Coxon A., Maundrell K., Kearsey S.E.;
RT "Fission yeast cdc21+ belongs to a family of proteins involved in an early
RT step of chromosome replication.";
RL Nucleic Acids Res. 20:5571-5577(1992).
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-52 AND SER-69, 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 Required for S phase execution. {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 P30665; P32354: MCM10; NbExp=3; IntAct=EBI-4326, EBI-5965;
CC P30665; P29469: MCM2; NbExp=15; IntAct=EBI-4326, EBI-10533;
CC P30665; P53091: MCM6; NbExp=7; IntAct=EBI-4326, EBI-10556;
CC P30665; P38132: MCM7; NbExp=3; IntAct=EBI-4326, EBI-4300;
CC P30665; Q12488: PSF1; NbExp=5; IntAct=EBI-4326, EBI-22066;
CC P30665; Q12306: SMT3; NbExp=2; IntAct=EBI-4326, EBI-17490;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 8800 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; U14731; AAA86310.1; -; Genomic_DNA.
DR EMBL; Z49919; CAA90164.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95015.1; -; Genomic_DNA.
DR EMBL; Z15032; CAA78750.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11445.1; -; Genomic_DNA.
DR PIR; S56050; S56050.
DR RefSeq; NP_015344.1; NM_001184116.1.
DR PDB; 3JA8; EM; 3.80 A; 4=1-933.
DR PDB; 3JC5; EM; 4.70 A; 4=1-933.
DR PDB; 3JC6; EM; 3.70 A; 4=1-933.
DR PDB; 3JC7; EM; 4.80 A; 4=1-933.
DR PDB; 5BK4; EM; 3.90 A; 4/C=1-933.
DR PDB; 5U8S; EM; 6.10 A; 4=1-933.
DR PDB; 5U8T; EM; 4.90 A; 4=1-933.
DR PDB; 5V8F; EM; 3.90 A; 4=1-933.
DR PDB; 5XF8; EM; 7.10 A; 4=1-933.
DR PDB; 6EYC; EM; 3.80 A; 4=1-933.
DR PDB; 6F0L; EM; 4.77 A; 4/C=1-933.
DR PDB; 6HV9; EM; 4.98 A; 4=1-933.
DR PDB; 6PTJ; EM; 3.80 A; 4=1-933.
DR PDB; 6PTN; EM; 5.80 A; 4/k=1-933.
DR PDB; 6PTO; EM; 7.00 A; 4/H/j=1-933.
DR PDB; 6RQC; EM; 4.40 A; 4=1-933.
DR PDB; 6SKL; EM; 3.70 A; 4=1-933.
DR PDB; 6SKO; EM; 3.40 A; 4=1-933.
DR PDB; 6U0M; EM; 3.90 A; 4=177-929.
DR PDB; 6WGF; EM; 7.70 A; 4=1-933.
DR PDB; 6WGG; EM; 8.10 A; 4=1-933.
DR PDB; 6WGI; EM; 10.00 A; 4=1-933.
DR PDB; 7P30; EM; 3.00 A; 4/C=1-933.
DR PDB; 7P5Z; EM; 3.30 A; 4/C=1-933.
DR PDB; 7PMK; EM; 3.20 A; 4=1-933.
DR PDB; 7PMN; EM; 3.20 A; 4=1-933.
DR PDB; 7V3U; EM; 3.20 A; 4/D=1-933.
DR PDB; 7V3V; EM; 2.90 A; 4/D=1-933.
DR PDB; 7W8G; EM; 2.52 A; 4/D=1-933.
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; P30665; -.
DR SMR; P30665; -.
DR BioGRID; 36196; 163.
DR ComplexPortal; CPX-2944; MCM complex.
DR DIP; DIP-2409N; -.
DR IntAct; P30665; 35.
DR MINT; P30665; -.
DR STRING; 4932.YPR019W; -.
DR iPTMnet; P30665; -.
DR MaxQB; P30665; -.
DR PaxDb; P30665; -.
DR PRIDE; P30665; -.
DR EnsemblFungi; YPR019W_mRNA; YPR019W; YPR019W.
DR GeneID; 856130; -.
DR KEGG; sce:YPR019W; -.
DR SGD; S000006223; MCM4.
DR VEuPathDB; FungiDB:YPR019W; -.
DR eggNOG; KOG0478; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR HOGENOM; CLU_000995_7_1_1; -.
DR InParanoid; P30665; -.
DR OMA; KNTIRIC; -.
DR BioCyc; YEAST:G3O-34179-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:P30665; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P30665; 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:SGD.
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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0004386; F:helicase activity; EXP:Reactome.
DR GO; GO:0003697; F:single-stranded DNA binding; IMP:SGD.
DR GO; GO:0006270; P:DNA replication initiation; IGI: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:SGD.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
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:0034214; P:protein hexamerization; IMP:SGD.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:ComplexPortal.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008047; MCM_4.
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 InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR11630; PTHR11630; 1.
DR PANTHER; PTHR11630:SF66; PTHR11630:SF66; 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; PR01660; MCMPROTEIN4.
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..933
FT /note="DNA replication licensing factor MCM4"
FT /id="PRO_0000194105"
FT DOMAIN 518..725
FT /note="MCM"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 700..703
FT /note="Arginine finger"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 568..575
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 574
FT /note="K->A: Loss of MCM2-7 complex helicase activity."
FT /evidence="ECO:0000269|PubMed:18657510"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 187..198
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 225..235
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 265..286
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 293..298
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 324..335
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 339..349
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 389..401
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 414..420
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 432..442
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 458..468
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 506..513
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 518..525
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 534..545
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 553..555
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 564..568
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 574..584
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 589..594
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 598..601
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 604..606
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 615..617
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 620..623
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 624..626
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 627..633
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 634..636
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 639..650
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 651..658
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 661..666
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 670..674
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 677..680
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 684..686
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 688..691
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 692..694
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 696..700
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 703..708
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 714..726
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 727..729
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 746..757
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 764..779
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 795..810
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 811..813
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 815..817
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 819..833
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 840..843
FT /evidence="ECO:0007829|PDB:6SKO"
FT TURN 847..851
FT /evidence="ECO:0007829|PDB:6SKO"
SQ SEQUENCE 933 AA; 105003 MW; 382D542AE38975E3 CRC64;
MSQQSSSPTK EDNNSSSPVV PNPDSVPPQL SSPALFYSSS SSQGDIYGRN NSQNLSQGEG
NIRAAIGSSP LNFPSSSQRQ NSDVFQSQGR QGRIRSSASA SGRSRYHSDL RSDRALPTSS
SSLGRNGQNR VHMRRNDIHT SDLSSPRRIV DFDTRSGVNT LDTSSSSAPP SEASEPLRII
WGTNVSIQEC TTNFRNFLMS FKYKFRKILD EREEFINNTT DEELYYIKQL NEMRELGTSN
LNLDARNLLA YKQTEDLYHQ LLNYPQEVIS IMDQTIKDCM VSLIVDNNLD YDLDEIETKF
YKVRPYNVGS CKGMRELNPN DIDKLINLKG LVLRSTPVIP DMKVAFFKCN VCDHTMAVEI
DRGVIQEPAR CERIDCNEPN SMSLIHNRCS FADKQVIKLQ ETPDFVPDGQ TPHSISLCVY
DELVDSCRAG DRIEVTGTFR SIPIRANSRQ RVLKSLYKTY VDVVHVKKVS DKRLDVDTST
IEQELMQNKV DHNEVEEVRQ ITDQDLAKIR EVAAREDLYS LLARSIAPSI YELEDVKKGI
LLQLFGGTNK TFTKGGRYRG DINILLCGDP STSKSQILQY VHKITPRGVY TSGKGSSAVG
LTAYITRDVD TKQLVLESGA LVLSDGGVCC IDEFDKMSDS TRSVLHEVME QQTISIAKAG
IITTLNARSS ILASANPIGS RYNPNLPVTE NIDLPPPLLS RFDLVYLVLD KVDEKNDREL
AKHLTNLYLE DKPEHISQDD VLPVEFLTMY ISYAKEHIHP IITEAAKTEL VRAYVGMRKM
GDDSRSDEKR ITATTRQLES MIRLAEAHAK MKLKNVVELE DVQEAVRLIR SAIKDYATDP
KTGKIDMNLV QTGKSVIQRK LQEDLSREIM NVLKDQASDS MSFNELIKQI NEHSQDRVES
SDIQEALSRL QQEDKVIVLG EGVRRSVRLN NRV
