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Database: UniProt
Entry: A0A165M1L4_9APHY
LinkDB: A0A165M1L4_9APHY
Original site: A0A165M1L4_9APHY 
ID   A0A165M1L4_9APHY        Unreviewed;      1528 AA.
AC   A0A165M1L4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   05-JUN-2019, entry version 16.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=DAEQUDRAFT_677323 {ECO:0000313|EMBL:KZT65126.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Daedalea.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT65126.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT65126.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT65126.1,
RC   ECO:0000313|Proteomes:UP000076727};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K.,
RA   Labutti K., Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T.,
RA   Yoshinaga Y., Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi
RT   Provides Insights into the Origins of Lignocellulose Decay
RT   Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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; KV429111; KZT65126.1; -; Genomic_DNA.
DR   EnsemblFungi; KZT65126; KZT65126; DAEQUDRAFT_677323.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000076727; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IEA:InterPro.
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:0019985; P:translesion synthesis; IEA:InterPro.
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;
KW   4Fe-4S {ECO:0000256|RuleBase:RU000442};
KW   Complete proteome {ECO:0000313|Proteomes:UP000076727};
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:UP000076727};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN       44    180       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      679    852       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      920   1365       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1420   1489       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION      415    511       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A165M1L4}.
FT   REGION      634    675       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A165M1L4}.
FT   COMPBIAS    441    458       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A165M1L4}.
FT   COMPBIAS    487    511       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A165M1L4}.
FT   COMPBIAS    639    675       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A165M1L4}.
SQ   SEQUENCE   1528 AA;  172034 MW;  306EE76373B44FC2 CRC64;
     MSSPLPTLRV RVNQIDHHLV APGPLDNSTL PRVPVVRIYG QSTTGQKACV HVHQVYPYFF
     VEYTGKMNPD SVSHYITKLS YSLNHAISVS MKRNPHSPKS QFVRAIVLTK GVHFYGFHAS
     YSPFLKVYIT DPNFVNRAVT ILRSGTVMKT RFRVYESHIS FILQFMCDFC LYGCGWMDLG
     EVWERGVGES SDDLHVTNDG NDPDESNHMQ AFKVSPYFRQ SRMPLEVDVA THQILNRHRL
     SARNIHHRLS IPGPPLPSEP LVLSVRELWE DERQRRIVKG LPPSPEIPKD PSENSRGRGA
     AWVAEARWWE EVRNRIERER GKEKVLHSSR NWEKWVMTTF ESIEALWEDE WRTWKSGREE
     AINPYAATQM DSRASPQVPT DNPTEVEVDE EMLSSQMMES LVQEAEDDWQ KLRGGYGERD
     ENVTDDWDAT EDGPPPEDQL GYDPEDNRGF DKDVIGGPMK RTHTQASDDS VDATPRPSKR
     RRTAMPPNKT WGSSYGSVPS SGLTSSGKSS AHTITLSSNS AIKGYRYALP PPSTTTLLSS
     VDEYGIPSKI YTSPYYSRAS DAPERPREYA GLVFNLKGGT GLSTLEEWTS STPDSIGHGG
     TGKRRLDPTG VTGWEYASTP PSVKEVRRWL RSPQGCKRSV QARPKQSSQI TGPTQANPYG
     MRATPLKSSK PSSRERQNMS IFSLEVFAPS AGDRLPDPDH DEVMAVFYSY QDSAEFPPED
     NESFTCQNGM IVVENDQVNA RRLRDMQFEA VSSELDLLNR LIDVVVDINP DIVSGWEVQA
     ASWGYLSVRA NTYGYDLGEQ ISRAPGRHMG GGSDQWGMRT TSTFKVVGRH VLNLWRIMRA
     EQSLTSYTFE NVAFHVLRRR TPRYTSRTLT QWYYSTTPRH TASVLQYFST RTSMVLEIMD
     AAEVVTKNAE FARVFGVDFF SVLSRGSQFK VESFMFRIAK PESFVLLSPS KQDVGKQNAA
     ECMPLIMEPL SAFYTSPLVV LDFQSLYPSI MIAYNYCYST CLGRITDFKG QSKFGVTDLR
     QPAGLLATLE DHINVAPNGI MYVKQDVRKG LLGRMLTELL DTRVMVKQAM KGIKDNKALR
     RVLDARQLGL KYIANVTYGY TSATYSGRMP AVEIADSIVQ SGRETLEKAI RVIHAETKWG
     ARVVYGDTDS LFIYLQGRTK EQAFRIGYDI AETITAMNPA PVKLKFEKVY LPCVLMAKKR
     YVGFKFESPD EAEPGFDAKG IETVRRDGIP AQQKMAETCL KILFRTQDLS KVKEYCCQTW
     ARILENKASI QDFIFAKEVR MGTYSDKAPP PPGVTVAARR MLEDPNDEPQ YGDRIPYVIV
     RGDPDSRLVD RAASPEELLS NPQKHLDAAY YISRVLVPPL ERVFNLVGAD VRAWYDEMPR
     ARRADQPESV LLSPRKARRH RDAGAANPFK IDEHFLTSRC LVCTAFAPGG LCDSCRAHPQ
     ETISGLLSRL HVAEDKLRNV QTVCSSCCGI PAAEPVRCES LDCPWLYERK KVENKVEALD
     VVAELIAELQ EAEDGREDVA GDDTSSSG
//
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