(data stored in SCRATCH zone)

SWISSPROT: Q6FK10_CANGA

ID   Q6FK10_CANGA            Unreviewed;      1481 AA.
AC   Q6FK10;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 113.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   OrderedLocusNames=CAGL0M02035g {ECO:0000313|CGD:CAL0137211,
GN   ECO:0000313|EMBL:CAG62410.1};
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:CAG62410.1, 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:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; CR380959; CAG62410.1; -; Genomic_DNA.
DR   RefSeq; XP_449434.1; XM_449434.1.
DR   STRING; 5478.XP_449434.1; -.
DR   EnsemblFungi; CAG62410; CAG62410; CAGL0M02035g.
DR   GeneID; 2891760; -.
DR   KEGG; cgr:CAGL0M02035g; -.
DR   CGD; CAL0137211; CAGL0M02035g.
DR   EuPathDB; FungiDB:CAGL0M02035g; -.
DR   eggNOG; KOG0968; Eukaryota.
DR   eggNOG; COG0417; LUCA.
DR   HOGENOM; HOG000194392; -.
DR   InParanoid; Q6FK10; -.
DR   KO; K02350; -.
DR   OMA; AHIHGAF; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IEA:EnsemblFungi.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0070987; P:error-free translesion synthesis; IEA:EnsemblFungi.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IEA:EnsemblFungi.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR042087; DNA_pol_B_C.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR030559; PolZ_Rev3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   PANTHER; PTHR45812; PTHR45812; 2.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 2.
DR   Pfam; PF14260; zf-C4pol; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FK10.
DR   SWISS-2DPAGE; Q6FK10.
KW   4Fe-4S {ECO:0000256|RuleBase:RU000442};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU000442};
KW   Iron {ECO:0000256|RuleBase:RU000442};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU000442};
KW   Metal-binding {ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU000442};
KW   Nucleus {ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN       66    217       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      585    824       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      891   1340       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1376   1456       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
SQ   SEQUENCE   1481 AA;  170384 MW;  17BD087BB4D25618 CRC64;
     MISGEETDSI QDGANEVEFD SFDLQLNNYD HYMAYPTSLD RTHGSSLPLK KFHKVPVIRI
     FGCLRTGHQL LCHVHGIFPY FFVKYDGKED DTSIIINEKC AKLHQLLEQI LRDKMKSKGS
     RNDKQDETNL NELVYIANVS VVKGVPFYGY HVGWTPFYKI SLLNPSLSEQ VCNIIREQNV
     LQNGQNEVYE SQFPYLLKFT ADFNLFACSW INFKKVYFRA PVLNEMLNMD EIMMTKELRV
     LLDRFHSKDT VLKKTMFPRI GNGLLEIDVI PQFIKNIDQI KIRNIHHDLS EKKESVNYLD
     DGPYVSSTKN MLKDVEIQRK LYSLEEYKKA ADISRNENDM IWNSSHQFEM FLRKALSSVK
     VSDKDSNFLS GHFNANDFLK TPFEMIDELW PTKFESSIDL NDENERHDKN DQLLDVGEDF
     DKAEERDEDI LGEPNEDDYI EKEMHSQDNG QFINVSTSVI STTQSLDKLL TQSIVKNQRK
     LKIGNVLSDL GNVATNYHNY FPSNIKKYYR YKQCNISYSS MNEDLQDNGL PINDYMGPFF
     SDPCDLHKKD YQYAGKQFDI TSTHLMKRYP LDFKEDLVRL TKQRLDNDVL FASWKYLKMP
     PSFNDVAESV TRKERARHSI SQIKKPTATK SLGNTSSIKR SESIHDNLTH FSLEIHVNTR
     GDLLPDPRKD EVSVIFWKVD SDTFPFSIDL QLEGIMYTNK LERENLIETL ESISGGVPIM
     EYEDEFSMFD ALTDLILLFD PDLLSGYEIH NSSWGYIFER SLSVHKFNIA NEISRVNMGA
     QFKLRDSWGF KKSSGISITG RYVLNIWRLL RKEIAVTQYS FENMVHLLLK IRLPKYSCSH
     LTSLWSNFKT GNELKTFLNY YLTRVRLNIG ILKKISFTLN VMEEARLIGI DFQSVYNRGS
     QYKVESFLIR ICKSENYILL SPSKVAVQKQ KPLECVPLVM EPESAFYKSP LLVLDFQSLY
     PSIMSGYNYC YSTMMGRVRE LDGTKRTLGV TNFELKSELL KKLRDDIRIA PNGVIYAKEH
     LRKSTLSKML SEILEIRFMI KKTISDLGSD HQALKKLLES KQLALKLLAN VTYGYTSASF
     SGRMPCSDLA DSIVQTGRET LEKAVKMIES TASWGAKVVY GDTDSLFVYL PGKTKEDAFR
     IGAEISNSIT ASNPKPITLK FEKVYFPCIL LSKKRYVGYS YLSSSQLNPH FDAKGIETVR
     RDGTPAQQKV VENALRILFE TKDLSKVKNY VVDTFTKIRS GNISIQDFCF AKEIKLGHYK
     SESTMPPGAV VAKRLKKQDS RAEPQYKERL SYLVVKGKSG QILRERCVSV SEYFSNDHFA
     LDSEYYITKT LIPPLDRLFN IVGISVSDWN QEGPMFVEGS IKPYTGADNI PTSTRCKACE
     QNTVSGDSYL CDNCVSNEKM AASKLIIKIQ ASASKLKVLN DICRICSRQY TGDMGLLSSN
     NALKCVSYDC PNYYSKLKAQ RLMQSKHYYS WNELLHNMDH W
//

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