(data stored in ACNUC8465 zone)

SWISSPROT: Q6FJL2_CANGA

ID   Q6FJL2_CANGA            Unreviewed;       812 AA.
AC   Q6FJL2;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 121.
DE   RecName: Full=DNA replication licensing factor MCM7 {ECO:0000256|RuleBase:RU365012};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU365012};
GN   Name=MCM7 {ECO:0000256|RuleBase:RU365012};
GN   OrderedLocusNames=CAGL0M05423g {ECO:0000313|CGD:CAL0136657,
GN   ECO:0000313|EMBL:CAG62558.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG62558.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Acts as component of the mcm2-7 complex (mcm complex)
CC       which is the putative replicative helicase essential for 'once per
CC       cell cycle' DNA replication initiation and elongation in
CC       eukaryotic cells. The active ATPase sites in the mcm2-7 ring are
CC       formed through the interaction surfaces of two neighboring
CC       subunits such that a critical structure of a conserved arginine
CC       finger motif is provided in trans relative to the ATP-binding site
CC       of the Walker A box of the adjacent subunit. The six ATPase active
CC       sites, however, are likely to contribute differentially to the
CC       complex helicase activity. {ECO:0000256|RuleBase:RU365012}.
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         Evidence={ECO:0000256|RuleBase:RU365012,
CC         ECO:0000256|SAAS:SAAS01116611};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365012,
CC       ECO:0000256|SAAS:SAAS00536536}.
CC   -!- SIMILARITY: Belongs to the MCM family.
CC       {ECO:0000256|RuleBase:RU004070}.
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DR   EMBL; CR380959; CAG62558.1; -; Genomic_DNA.
DR   RefSeq; XP_449582.1; XM_449582.1.
DR   STRING; 5478.XP_449582.1; -.
DR   EnsemblFungi; CAG62558; CAG62558; CAGL0M05423g.
DR   GeneID; 2891629; -.
DR   KEGG; cgr:CAGL0M05423g; -.
DR   CGD; CAL0136657; CAGL0M05423g.
DR   EuPathDB; FungiDB:CAGL0M05423g; -.
DR   eggNOG; KOG0482; Eukaryota.
DR   eggNOG; COG1241; LUCA.
DR   HOGENOM; HOG000224125; -.
DR   InParanoid; Q6FJL2; -.
DR   KO; K02210; -.
DR   OMA; AYTCDRC; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0071162; C:CMG complex; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0042555; C:MCM complex; IEA:EnsemblFungi.
DR   GO; GO:0097373; C:MCM core complex; IEA:EnsemblFungi.
DR   GO; GO:0005656; C:nuclear pre-replicative complex; IEA:EnsemblFungi.
DR   GO; GO:0031298; C:replication fork protection complex; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:1990163; F:ATP-dependent four-way junction helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:EnsemblFungi.
DR   GO; GO:1904931; F:MCM complex binding; IEA:EnsemblFungi.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0017116; F:single-stranded DNA-dependent ATP-dependent DNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0030466; P:chromatin silencing at silent mating-type cassette; IEA:EnsemblFungi.
DR   GO; GO:0006348; P:chromatin silencing at telomere; IEA:EnsemblFungi.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:EnsemblFungi.
DR   GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:EnsemblFungi.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:EnsemblFungi.
DR   GO; GO:0000727; P:double-strand break repair via break-induced replication; IEA:EnsemblFungi.
DR   GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IEA:EnsemblFungi.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR031327; MCM.
DR   InterPro; IPR008050; MCM7.
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   PANTHER; PTHR11630:SF26; PTHR11630:SF26; 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; PR01663; MCMPROTEIN7.
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   3: Inferred from homology;
DR   PRODOM; Q6FJL2.
DR   SWISS-2DPAGE; Q6FJL2.
KW   ATP-binding {ECO:0000256|RuleBase:RU004070,
KW   ECO:0000256|SAAS:SAAS01112253};
KW   Cell cycle {ECO:0000256|RuleBase:RU365012};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   DNA replication {ECO:0000256|RuleBase:RU365012,
KW   ECO:0000256|SAAS:SAAS00619122};
KW   DNA-binding {ECO:0000256|RuleBase:RU004070,
KW   ECO:0000256|SAAS:SAAS01112237};
KW   Helicase {ECO:0000256|RuleBase:RU365012,
KW   ECO:0000256|SAAS:SAAS00536375};
KW   Hydrolase {ECO:0000256|RuleBase:RU365012,
KW   ECO:0000256|SAAS:SAAS00536681};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU004070,
KW   ECO:0000256|SAAS:SAAS01112230};
KW   Nucleus {ECO:0000256|RuleBase:RU365012,
KW   ECO:0000256|SAAS:SAAS00536508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428}.
FT   DOMAIN      404    610       MCM. {ECO:0000259|PROSITE:PS50051}.
SQ   SEQUENCE   812 AA;  91457 MW;  31A4D531F6E3F87B CRC64;
     MSTALPSIQL SVDYQTLLSE ISDFLQHFKV DEVGAADDSA TIDADVNIDD AEELMKRGPK
     YMYLLQQIAN RERDTIEIEL NDVLRFQNEK FLEGGVAQDL VALIQKNANH FIDLFSRCID
     SVMPLPTKEI SYKDDVLDVI LNQRRLRNER MLSDRTNEIR SEMDTDTTSN DIMRELAQDE
     TETFPANLTR RYTVYFRPLT RSYAVRYNSK KYLTGSIPLS VRQIKGELLG ELITVRGIIT
     RVSDVKPAVT VIAYTCDQCG YEIFQEVNSK TFTPLVECTS RECSQNQTKG QLFMSTRASK
     FNAFQECKIQ ELSQQVPVGH IPRSLTIHVN GPLVRSVTPG DIVDIAGIFL PSPYTGFKAL
     KAGLLTETYL EAHHVRQHKK KFASFQMTPQ VRSNVDALAQ SGNVYERLAK SIAPEIYGNL
     DVKKALLLLL VGGVDKRVGD GMKIRGDINI CLMGDPGVAK SQLLKAICKI TPRGVYTTGK
     GSSGVGLTAA VMKDPVTDEM ILEGGALVLA DNGICCIDEF DKMDESDRTA IHEVMEQQTI
     SISKAGINTT LNARTSILAA ANPLYGRYNP RLSPLENINL PAALLSRFDV MFLLLDTPNR
     ENDEQLANHV AYVHMYNKQP DLDFEPIEPT MMREFIAYAR TMRPVMTAEI NDHVVSAYIR
     LRQDSKREMD SKFSFGQATP RTLLAIIRLS QALAKLRLSE TVDIDDVEEA LRLIRVSKES
     LYQENRKRDE DSNPTTKIFT IIKKMSQEGD YKGSLPYDSI VKTVRSRGFT MLQLNNCIQE
     YSFLNVWHLI NEGNTLKFVD DEDQSSQDIE MA
//

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