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Database: UniProt
Entry: W3X3H7_PESFW
LinkDB: W3X3H7_PESFW
Original site: W3X3H7_PESFW 
ID   W3X3H7_PESFW            Unreviewed;      1100 AA.
AC   W3X3H7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   05-JUN-2019, entry version 36.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=PFICI_08217 {ECO:0000313|EMBL:ETS80688.1};
OS   Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Xylariomycetidae; Xylariales; Sporocadaceae;
OC   Pestalotiopsis.
OX   NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS80688.1, ECO:0000313|Proteomes:UP000030651};
RN   [1] {ECO:0000313|Proteomes:UP000030651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX   PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA   Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA   Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT   "Genomic and transcriptomic analysis of the endophytic fungus
RT   Pestalotiopsis fici reveals its lifestyle and high potential for
RT   synthesis of natural products.";
RL   BMC Genomics 16:28-28(2015).
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; KI912113; ETS80688.1; -; Genomic_DNA.
DR   RefSeq; XP_007834989.1; XM_007836798.1.
DR   STRING; 393283.XP_007834989.1; -.
DR   EnsemblFungi; ETS80688; ETS80688; PFICI_08217.
DR   GeneID; 19273230; -.
DR   KEGG; pfy:PFICI_08217; -.
DR   KO; K02327; -.
DR   OMA; CLVNYTE; -.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000030651; 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   Complete proteome {ECO:0000313|Proteomes:UP000030651};
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:UP000030651};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN      126    468       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      532    963       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1001   1075       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION        1     61       Disordered. {ECO:0000256|MobiDB-lite:
FT                                W3X3H7}.
FT   REGION       76     98       Disordered. {ECO:0000256|MobiDB-lite:
FT                                W3X3H7}.
FT   COMPBIAS     34     61       Polar. {ECO:0000256|MobiDB-lite:W3X3H7}.
FT   COMPBIAS     76     94       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                W3X3H7}.
SQ   SEQUENCE   1100 AA;  124220 MW;  24CC05CC78D5B04E CRC64;
     MSAAATLPQK RVFGGARPPS SPGTKKRRLE PLTSSPASRL NSSQPAPGSK LGSAQTKSTF
     ESEVLEKLSQ DISDLKQNNS EKDQSWERPP VTDFNPKRDN LTFQQIEAEE GTLHGGKATV
     KLFGVTENGH SVMLHVTDFK HYLYVAAPVS FQPKDCEPFK AFLESQIAQH QPAIYSCQLA
     LRENIYGFQG NTKSPYIKIT VTDPKFINRV RSTIEKGDAN WKGMWKGAEG DIMTFDNLQY
     VLRFMVDTKI PGMSWVECPA KQYSLIPEQE KQSNCQIEAE IPYTHLISHE PKGEWSKMAP
     LRILSFDIEC AGRKGIFPEA DMDPVIQIAN VVTRYGESKP FIRNVFCLDT TSPIVATQIL
     DFDKEQDMLM AWKHFLDKVD PDLITGYNIA NFDFPYLLDR ARHLKCKDFD YWTRLKSVKS
     QAKETNFSSK QMGNRDTKAT NTNGRLQLDL LQLIQRDHHL RSYTLNSVCA HFLGEQKEDV
     HHTMITELFN GTPESRRRLA LYCLKDAYLP QRLMDKLSCL ANYTEMARVT GVPFNFLLSR
     GQQIKFLSQL YRKALEQKLV IPNMRSQGSD EQYEGATVIE PTRGYYDVPI ATLDFASLYP
     SIMQAHNLCY TTLINARAVE KFGLKKDEDY IVTPNGDLFV TTKQRKGLLA QILEELLMAR
     KQAKRELAVE TDPFKKAVLN GRQLALKISA NSVYGLTGAT TGKLPCLEIA SSTTSYGRQM
     IEKTKDEVEK KYCIANGYSH DAQVIYGDTD SVMVKFGTTE LAEAMKLGEE AANYVSSKFI
     KPIKLEFEKV YFPYLLINKK RYAGLYWTKT EKYDKMDTKG IETVRRDNCL LVQTVIEKVL
     RMILIDRDVP GAQEYVKDMI ADLLQNKVDM SKLVITKALT KEVYDGKQAH VELAARMKKR
     DAGSAPGLGD RVAYVMIRGA AGAKNFEKSE DPIYVLENNL PIDTRYYLDN QLAKPLGRIF
     EPILGETKAK SLLTGDHTRS ISVAAPTVGG LMKFAKKTMT CMGCKKPLVG KEESAGAVCS
     NCAPRVGELY NKTLGRVSDL EVRFGRLWTQ CQRCQGSMHC EVICSSKDCP IFYMRMKAKK
     DLEDAGKELK RFDLDQAAIW
//
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