GenomeNet

Database: UniProt
Entry: Q6FXK7_CANGA
LinkDB: Q6FXK7_CANGA
Original site: Q6FXK7_CANGA 
ID   Q6FXK7_CANGA            Unreviewed;      1470 AA.
AC   Q6FXK7;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   SubName: Full=Candida glabrata strain CBS138 chromosome B complete sequence {ECO:0000313|EMBL:CAG58088.1};
GN   OrderedLocusNames=CAGL0B05049g {ECO:0000313|CGD:CAL0127736,
GN   ECO:0000313|EMBL:CAG58088.1};
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG58088.1, ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG58088.1, 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., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., 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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; CR380948; CAG58088.1; -; Genomic_DNA.
DR   RefSeq; XP_445188.1; XM_445188.1.
DR   STRING; 284593.Q6FXK7; -.
DR   EnsemblFungi; CAGL0B05049g-T; CAGL0B05049g-T-p1; CAGL0B05049g.
DR   GeneID; 2886515; -.
DR   KEGG; cgr:CAGL0B05049g; -.
DR   CGD; CAL0127736; CAGL0B05049g.
DR   VEuPathDB; FungiDB:CAGL0B05049g; -.
DR   eggNOG; KOG0298; Eukaryota.
DR   HOGENOM; CLU_001592_2_0_1; -.
DR   InParanoid; Q6FXK7; -.
DR   OMA; QLFEQMC; -.
DR   Proteomes; UP000002428; Chromosome B.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:EnsemblFungi.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
DR   GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IEA:EnsemblFungi.
DR   CDD; cd18070; DEXQc_SHPRH; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR   PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          343..551
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1164..1202
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   1470 AA;  170477 MW;  EF90A89C4188437A CRC64;
     MHTDSVNCRI VGFSEVEYGT AITEREKASS WLKNKRLIHV GILTLTILRP TEGYPSDLKE
     MNVSILPIQT ESEDKKMSMF RLKLYNQKGI LLFSLEPETE TSTINHYFRI LNEKYIDQKV
     ILNNEKLRSE AGIKQKRKKR KIAFGLIQPT RNYKDILVTK QALTFNQNSK VWQIHVSFSV
     IANQDKRNKF TADVNALLQD ISTSLIPASN ELYLPKMTSN YVQSHFNQYI ISCTNERLKN
     LRANRQYTAV DSVINGKLFP FQKDSLLWLL EKEHYFDCNV SKTTTSDQKH EDSVSELLYF
     LNHSVSFGYS TIKDLVSKQF YFWNKYTGYI LSQEEVRSLK SSFNEYEVGA KGVLAEEMGL
     GKTLEILALI CINKRKYKAD EPLDFVSESG KVISKCSTTL IVCPGSILKQ WIDEMQSTHP
     AIKIYHYGGF IAVKKEFACD NINTIVQKLS QYDIVITSYN VVSNEVHYAQ FNNAFRQNRR
     RHVQYDYSSP LSLMQFYRII LDELQMLHSG STKAAICTSL LHRVHTWGVS GTPIQKVRDF
     QTILSYLKIH PFSEFPELIK NLDNASVGLT EMYSAENGCP INEIEVIKNG INTNLSDLFY
     IFKQYDIAIR HSKANVSSQI KIPKQHLLLI PLKFTPIEWE SYLEVWKSFL EDSGFNPDGT
     NSTHLTNQQL NQWLHKLRYI CCHAVLPHSA SINNITTANE IHTLNDILKK MKAEAEDKVE
     SLYREQFQLL IRSAQFDIEE QGRYNFAIDC LLSLEKNIFD RLKPLTKSSN DILNFLEYLD
     IADSHASSKS CRHLLELLHQ CYFFIATAYY YLGSYQIECK QDAGIPIRQD DLCNDETLKN
     HFSPDEIKSI AYHKNLEDEY YSRAENIRRS ILKGRIAKFE QELDEVQKSH FPTKAIMLIK
     FEELPNCSIS LSTNKCYSKL LDLFSKLDEQ AIQSNRQINL LYDLLSMPII KEYDSDTPEK
     THEYASSIED QDKIYALFDC LEKLISNREE IVRAEEEVTP PKISLSLYEN LSTYHTELLK
     DQILISGTPF KTIFDDLENV RIVHRISKKQ SNDKSFEASL LSYKKCLKKI RKENAQLRSY
     LQALNTVYNA KVDYYAYLQR ISDSVVPLSQ LDSTTLSSLR KFISNVNKKQ ELQRKIVSTE
     SRVKYLHNLS TLTYEAQKNT TMECSICLQP ITNGAMVNCG HLFCTSCIFS WLKNRKTCPL
     CKHPTSNCEV YNFTFKLESG SSRKTKCDNK TRHHRYPNMQ NFENTLDSLF LTKYERFKQS
     KTTADIIIKE SYGSKIDFII KLVLFLLHQS EIEDATRPQI LMYSQSFDFM KVVSQVLSLH
     NINNICCLQN NRNVGDMIAR FKKTSDITCL LLNIRSLGAG LNLLNARHIF LLDPILNVNE
     EIQAMSRNNR IGQRQETYVW NFMLENTVEE SIMRYKCVLE NQNRHKREER SMPMYEQSEQ
     LDVTDSEVCI SDFSNEVVSE QHIRNCLFLK
//
DBGET integrated database retrieval system