(data stored in SCRATCH 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   30-AUG-2017, entry version 108.
DE   RecName: Full=DNA helicase {ECO:0000256|SAAS:SAAS00536514};
DE            EC=3.6.4.12 {ECO:0000256|SAAS:SAAS00536514};
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   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC       {ECO:0000256|SAAS:SAAS00536515}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00536536}.
CC   -!- SIMILARITY: Belongs to the MCM family.
CC       {ECO:0000256|RuleBase:RU004070}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CR380959; CAG62558.1; -; Genomic_DNA.
DR   RefSeq; XP_449582.1; XM_449582.1.
DR   ProteinModelPortal; Q6FJL2; -.
DR   STRING; 284593.XP_449582.1; -.
DR   EnsemblFungi; CAG62558; CAG62558; CAGL0M05423g.
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; VKIQEMA; -.
DR   OrthoDB; EOG092C0VUM; -.
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:0000790; C:nuclear chromatin; 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:0033679; F:3'-5' DNA/RNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi.
DR   GO; GO:1990518; F:single-stranded DNA-dependent ATP-dependent 3'-5' DNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0003727; F:single-stranded RNA binding; 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; IPR027925; MCM_N.
DR   InterPro; IPR033762; MCM_OB.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11630:SF78; PTHR11630:SF78; 1.
DR   Pfam; PF00493; MCM; 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; 2.
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:SAAS00628902};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   DNA replication {ECO:0000256|SAAS:SAAS00619122};
KW   DNA-binding {ECO:0000256|RuleBase:RU004070,
KW   ECO:0000256|SAAS:SAAS00628874};
KW   Helicase {ECO:0000256|SAAS:SAAS00536375};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00536681};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU004070,
KW   ECO:0000256|SAAS:SAAS00628914};
KW   Nucleus {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
//

If you have problems or comments...

PBIL Back to PBIL home page