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Database: UniProt
Entry: W9WCU9_9EURO
LinkDB: W9WCU9_9EURO
Original site: W9WCU9_9EURO 
ID   W9WCU9_9EURO            Unreviewed;      1107 AA.
AC   W9WCU9;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   05-JUN-2019, entry version 32.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=A1O5_10908 {ECO:0000313|EMBL:EXJ65932.1};
OS   Cladophialophora psammophila CBS 110553.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ65932.1, ECO:0000313|Proteomes:UP000019471};
RN   [1] {ECO:0000313|EMBL:EXJ65932.1, ECO:0000313|Proteomes:UP000019471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ65932.1,
RC   ECO:0000313|Proteomes:UP000019471};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EXJ65932.1}.
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DR   EMBL; AMGX01000022; EXJ65932.1; -; Genomic_DNA.
DR   RefSeq; XP_007749672.1; XM_007751482.1.
DR   STRING; 1182553.XP_007749672.1; -.
DR   EnsemblFungi; EXJ65932; EXJ65932; A1O5_10908.
DR   GeneID; 19195599; -.
DR   Proteomes; UP000019471; Unassembled WGS sequence.
DR   GO; GO:0043625; C:delta DNA polymerase complex; IEA:EnsemblFungi.
DR   GO; GO:0000784; C:nuclear chromosome, telomeric region; 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:1904161; P:DNA synthesis involved in UV-damage excision repair; IEA:EnsemblFungi.
DR   GO; GO:1903459; P:mitotic DNA replication lagging strand elongation; 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; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
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;
KW   4Fe-4S {ECO:0000256|RuleBase:RU000442};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019471};
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:UP000019471};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN      133    475       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      539    970       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1008   1082       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION        1     59       Disordered. {ECO:0000256|MobiDB-lite:
FT                                W9WCU9}.
FT   REGION       82    101       Disordered. {ECO:0000256|MobiDB-lite:
FT                                W9WCU9}.
FT   COILED     1082   1102       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS      1     32       Polar. {ECO:0000256|MobiDB-lite:W9WCU9}.
FT   COMPBIAS     40     59       Polar. {ECO:0000256|MobiDB-lite:W9WCU9}.
FT   COMPBIAS     83    101       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                W9WCU9}.
SQ   SEQUENCE   1107 AA;  125667 MW;  70A1E16529B153EE CRC64;
     MSGSVADQPK KRVLTDTTNT HNALQSPPTA KKRKLNGNGP IVSFRSSQPG PNGFKSKLGL
     SQPKSQFEIE VLEKMTQDIA GLKENNSEKD QQWERPSLDD FNPDIDPLRF QQIEIEEGTL
     HGGKIALKMF GVSETGHSIL LHITDFLHYL YVAAPVNFQR SDIEGYKAYL ESQLAQHQPT
     IHSVQMVLRE NLFGFQGNQK SPYLKITVTD PKYINRLRTA IEDGHANYKG MWKGVESKIL
     TFDNIQYVLR FMIDTGVTGM SWVEVPPQKY HVLPQHDRQS NCQIEASCHY RDLIAHGHDG
     EWAKMAPLRI LSFDIECAGR KGVFPEANQD PVIQIANVVT KYGESKPFIR NVFVLDTCSL
     IVNTKIYEHK SESDMLMAWR HFLEEVDPDV IIGYNIANFD FPYLLDRAKH LKLTKFPYWS
     RLKSVASHAR DTNFSSKQMG NRDTKATNTN GRIQLDLLQL VQRDYQLRSY TLNSVCAHFL
     GEQKEDVHHT MITELYNGTP DSRRRLAVYC LKDAYLPQRL MDKLMCLVNY TEMARVTGVP
     FNYLLARGQQ VKFISQLFRK ALEQQLVIPN LRNEGTDEQY EGATVIEPLR GYYDVPVATL
     DFASLYPSII QAHNLCYTTL LNKNIIEKLN LKKDEDYILT PNGDLFCTAK VRKGLLTQIL
     EELLGARKRA KKELAVEKDP FKKAVLNGRQ LALKVSANSV YGITGATVGK LPCLAIASST
     TAYGRQMIEK TKSEVEQKYT MANGYSHDAQ VIYGDTDSVM VKFGEKDLKK TMELGREAAD
     FVSSKFIKPI KLEFEKVYFP YLLINKKRYA GLYWTNPEKH DKMDSKGIET VRRDNCRLVQ
     VVIETVLEKI LIDRDLDGAQ DYVKETIANL LQNKIDLSML VITKALSKSD YTAKQAHVEL
     AERMKKRDAG SAPALGDRVA YVMVKGASGS KNYENSEDPM YVLENNVPID TKYYLDNQLA
     NPLGRIFEPI LGERRANSLL AGDHTRSISV AAPTLGGLMK FAKKTQTCMG CKKPLVSAEE
     ANGAVCENCH PRIGELYNRQ VKKVGELEVR FARLWTQCQR CQGSMHSEVL CSSRDCPIFY
     MRMKARKEVE EQGKELARFD RDVGAIW
//
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