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Database: UniProt
Entry: A0A2H3JQG3_WOLCO
LinkDB: A0A2H3JQG3_WOLCO
Original site: A0A2H3JQG3_WOLCO 
ID   A0A2H3JQG3_WOLCO        Unreviewed;      1086 AA.
AC   A0A2H3JQG3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   05-JUN-2019, entry version 9.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=WOLCODRAFT_133199 {ECO:0000313|EMBL:PCH44386.1};
OS   Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Wolfiporia.
OX   NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH44386.1, ECO:0000313|Proteomes:UP000218811};
RN   [1] {ECO:0000313|EMBL:PCH44386.1, ECO:0000313|Proteomes:UP000218811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-104 {ECO:0000313|EMBL:PCH44386.1,
RC   ECO:0000313|Proteomes:UP000218811};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A.,
RA   Henrissat B., Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S.,
RA   Aerts A., Benoit I., Boyd A., Carlson A., Copeland A., Coutinho P.M.,
RA   de Vries R.P., Ferreira P., Findley K., Foster B., Gaskell J.,
RA   Glotzer D., Gorecki P., Heitman J., Hesse C., Hori C., Igarashi K.,
RA   Jurgens J.A., Kallen N., Kersten P., Kohler A., Kues U., Kumar T.K.,
RA   Kuo A., LaButti K., Larrondo L.F., Lindquist E., Ling A., Lombard V.,
RA   Lucas S., Lundell T., Martin R., McLaughlin D.J., Morgenstern I.,
RA   Morin E., Murat C., Nagy L.G., Nolan M., Ohm R.A., Patyshakuliyeva A.,
RA   Rokas A., Ruiz-Duenas F.J., Sabat G., Salamov A., Samejima M.,
RA   Schmutz J., Slot J.C., St John F., Stenlid J., Sun H., Sun S.,
RA   Syed K., Tsang A., Wiebenga A., Young D., Pisabarro A., Eastwood D.C.,
RA   Martin F., Cullen D., Grigoriev I.V., Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed
RT   from 31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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; KB468157; PCH44386.1; -; Genomic_DNA.
DR   EnsemblFungi; PCH44386; PCH44386; WOLCODRAFT_133199.
DR   OMA; CLVNYTE; -.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000218811; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005657; C:replication fork; IEA:EnsemblFungi.
DR   GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; 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:0043137; P:DNA replication, removal of RNA primer; IEA:EnsemblFungi.
DR   GO; GO:0045005; P:DNA-dependent DNA replication maintenance of fidelity; IEA:EnsemblFungi.
DR   GO; GO:0006278; P:RNA-dependent DNA biosynthetic process; 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:UP000218811};
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:UP000218811};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN      115    457       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      521    952       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN      989   1064       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION        1     49       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A2H3JQG3}.
FT   COILED     1064   1084       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS      1     22       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A2H3JQG3}.
SQ   SEQUENCE   1086 AA;  122384 MW;  9EDE8B2DCE9D5953 CRC64;
     MATTSPSSKE NVPLTRTATE TFKADSELPA AKRRRIGPAD SLSQTNRPSF ADVLERLKEE
     AGEAKDAEGG ADCWARPSLK EIDEKRDSII FQQIDVEDAV ESQSGGVGLR MFGVTESGHS
     VLAHITDFLP YFYIPAPRGF TNSDTYAFTE YLNNAGNGGV VRKVELVSKR SLWGYRGDDW
     IIFLKITLAD QRSLPKIRGL FERAECHFRD MFSDQVPTYE SNIAYTLRFM IDTKVVGMNW
     IEVPAGSYKL IRDTGKTDRK RSHCQIELSV RWDQVISHSP EGQWSKIAPL RILSFDIECA
     GRKGIFPEPN IDPVIQIANM VTRQGENKPF IRNVFTLNTC AHIAGSQVLS FDDEAKMLDA
     WQQFVEQVDP DVVIGYNIAN FDLPYLVDRA KNITASKFPY LGRMRGVKAQ TKETHFSSKA
     FGQRDSKETA LDGRLQIDVL QYMQREHKLR SYTLNSVCAQ FLGEQKEDVH HSVITELQNG
     GPESRRRLAV YCLKDAYLPQ RLIDKLMCFI NYTEMARVTG VPFKLLLSRG QSIKVLSQLF
     RKANDEGYIV PSLKGEGSDE QYEGATVIEP MKGYYDVPIA TLDFSSLYPS IMMAHNLCYT
     TLLDKKTIDR LGMVKDVDYI QTPNNDFFAK ASRRKGLLPT ILEDLISARK RAKADLKKET
     DPFKRAVLDG RQLALKISAN SVYGFTGATI GKLPCLPISS SVTAYGRQMI EKTKQEVEAE
     YCIANGHSHD AQVIYGDTDS VMVKFGPTDL PTVMALGSQA ADFVTAKFVK PIKLEFEKVY
     FPYLLISKKR YAGLYWTRPE KYDKMDTKGI ETVRRDNCRL VSTVIETCLH KMLIDRDVKG
     AEEYTKQIIS DLLQNKVDMS QLVITKALAK SDYAAKQAHV ELAERMKQRD AGSAPALGDR
     VAYVIIKGVK GAAAYEKSED PIYVLENNIP IDTKYYLENQ LSNPLMRIFE PILGEKASSL
     LSGDHTRTIQ IATPTVGGLM KFAVKTATCL GCKTPLRPNN CVKNGAVCNN CRPRLGELYQ
     KQVTTASEYQ VRFSRLWTQC QRCQGSLHQD VLCSSKDCPI FYMRKKAQKD VEDANTTLER
     FDHELW
//
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