(data stored in SCRATCH zone)

SWISSPROT: Q6BMW4_DEBHA

ID   Q6BMW4_DEBHA            Unreviewed;       732 AA.
AC   Q6BMW4;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   10-APR-2019, entry version 105.
DE   RecName: Full=DNA helicase {ECO:0000256|SAAS:SAAS00536514};
DE            EC=3.6.4.12 {ECO:0000256|SAAS:SAAS00536514};
GN   OrderedLocusNames=DEHA2F02112g {ECO:0000313|EMBL:CAG88763.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88763.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88763.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
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:
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|SAAS:SAAS01116611};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00536536}.
CC   -!- SIMILARITY: Belongs to the MCM family.
CC       {ECO:0000256|RuleBase:RU004070, ECO:0000256|SAAS:SAAS01112249}.
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DR   EMBL; CR382138; CAG88763.2; -; Genomic_DNA.
DR   RefSeq; XP_460456.2; XM_460456.1.
DR   STRING; 4959.XP_460456.2; -.
DR   EnsemblFungi; CAG88763; CAG88763; DEHA2F02112g.
DR   GeneID; 2903959; -.
DR   KEGG; dha:DEHA2F02112g; -.
DR   HOGENOM; HOG000224128; -.
DR   InParanoid; Q6BMW4; -.
DR   KO; K02209; -.
DR   OMA; LPRKCTT; -.
DR   OrthoDB; 266497at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
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:0000784; C:nuclear chromosome, telomeric region; 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: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:0017116; F:single-stranded DNA-dependent ATP-dependent DNA helicase activity; 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:0000727; P:double-strand break repair via break-induced replication; IEA:EnsemblFungi.
DR   GO; GO:0006343; P:establishment of chromatin silencing; IEA:EnsemblFungi.
DR   GO; GO:0031939; P:negative regulation of chromatin silencing at telomere; IEA:EnsemblFungi.
DR   GO; GO:0051097; P:negative regulation of helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IEA:EnsemblFungi.
DR   GO; GO:0030174; P:regulation of DNA-dependent DNA replication initiation; IEA:EnsemblFungi.
DR   InterPro; IPR031327; MCM.
DR   InterPro; IPR008048; MCM5.
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; PR01661; MCMPROTEIN5.
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; Q6BMW4.
DR   SWISS-2DPAGE; Q6BMW4.
KW   ATP-binding {ECO:0000256|RuleBase:RU004070,
KW   ECO:0000256|SAAS:SAAS01112253};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   DNA replication {ECO:0000256|SAAS:SAAS00619122};
KW   DNA-binding {ECO:0000256|RuleBase:RU004070,
KW   ECO:0000256|SAAS:SAAS01112237};
KW   Helicase {ECO:0000256|SAAS:SAAS00536375};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00536681};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU004070,
KW   ECO:0000256|SAAS:SAAS01112230};
KW   Nucleus {ECO:0000256|SAAS:SAAS00536508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   DOMAIN      325    531       MCM. {ECO:0000259|PROSITE:PS50051}.
SQ   SEQUENCE   732 AA;  82220 MW;  842322F16334CB7C CRC64;
     MSYERSEVYG AQVLPGEDPE DNSFNEITKA FRSFILEFRL NSQFIYRDQL RENLLIKNYF
     LKVNSEHLIG FNEELNKKLT DDPAEMIPLF ENAITDIGKR IAYLSNEEVP TDFPNCQLIL
     FSNASKTSIR DLDSDHISKI VRVSGIIISS SVLSSRATQV QLLCRNCKHT MRQKISSGFG
     SLNLPNRCQG THNFDDTSTQ DKCPSDPYTI VHDKSTFIDQ QVLKLQESPD MVPVGEMPRH
     IILQADRYMT NQVVPGTRVT IVGIYSIYQA KQKSSSNVNT VAIRNPYLKI LGIQTDVDNS
     ISGQGLTFTE EEEEEFLKIS RLPNLYDVFS KSIAPSIYGN EDIKKAITCL LMGGSKKILP
     DGMRLRGDIN VLLLGDPGTA KSQLLKFVEK ISPISVYTSG KGSSAAGLTA SVQRDQVTRD
     FYLEGGAMVL ADGGVVCIDE FDKMRDEDRV AIHEAMEQQT ISIAKAGITT ILNSRTSVLA
     AANPIFGRYD DLKSPGENID FQTTILSRFD MIFIVKDDHN EARDISIAQH VMNVHTGNAN
     NNQDQNQEGE IPIDVMKRYI QYVKLKCAPR LSPEASERLS SHFVSIRRRL QINEVEMNER
     SSIPITIRQL EAIIRITESL AKLRLSPIAL EEHVEEAIRL FTASTMDAVD QGVSSGGLIT
     TGDMNKEINK VEQELRRRLP IGWSTAYKTL RREIVDSGKA SPGALDKALY ILERHEVIRF
     RHQRQNILRC GV
//

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