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Database: UniProt
Entry: A0A1L7XGQ3_9HELO
LinkDB: A0A1L7XGQ3_9HELO
Original site: A0A1L7XGQ3_9HELO 
ID   A0A1L7XGQ3_9HELO        Unreviewed;      1745 AA.
AC   A0A1L7XGQ3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   05-JUN-2019, entry version 13.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=PAC_14024 {ECO:0000313|EMBL:CZR64127.1};
OS   Phialocephala subalpina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiales incertae sedis; Phialocephala;
OC   Phialocephala fortinii species complex.
OX   NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR64127.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR64127.1, ECO:0000313|Proteomes:UP000184330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR64127.1,
RC   ECO:0000313|Proteomes:UP000184330};
RA   Ploux O.;
RL   Submitted (MAR-2016) 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}.
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DR   EMBL; FJOG01000025; CZR64127.1; -; Genomic_DNA.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000184330; 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; 1.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000184330};
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:UP000184330};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN       49    215       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      893   1077       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN     1145   1590       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1641   1712       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION      281    301       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1L7XGQ3}.
FT   REGION      453    499       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1L7XGQ3}.
FT   REGION      543    602       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1L7XGQ3}.
FT   REGION      620    640       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1L7XGQ3}.
FT   REGION      845    877       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1L7XGQ3}.
FT   COILED      412    432       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    453    473       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1L7XGQ3}.
FT   COMPBIAS    563    585       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1L7XGQ3}.
SQ   SEQUENCE   1745 AA;  197594 MW;  858F475A215EA781 CRC64;
     MDLFRLRLNN IDHYQSTPTR FDPLLRNNIK PSQLQKEPKV PVIRVFGATE TGQKVCAHIH
     GAFPYLYIEY TGSLTLDDVG AYVHRLHLSI DFALAVSYRR NTYDGNAKFV ARITLVKGIP
     FYGFHVGYRY YLKIYMLNPM VMTRLSDLLR QGVVMKKVFQ PYEAHLQYLL QWMADYNLYG
     CGFIDSKTVT FRSPVPQWDE MDDLSHLWHD RSIPKELVTD EATLPRVSHC AIEVDICVQD
     ILNRQHIKSR LLHHDFIERL NPLAPHEKLV HSMAGLWRDE TRRRRSRMSN PDPGSSAFPP
     EVMVSISADP RNSQRGGWIH EEEYRERIQA LIAEEENKSD GAKLSFNNFV KPTPFDSSVR
     TSLESVEDLY PENLRHALGV APGSTIGVVN YDVNDADGTE VDENRILGLV GADEDEAQYD
     SDEDVMREME LEQRKKEDKV EEQYLDSADV RKPEHNIDDE LRPGGEHYGD QFLDPKDAVV
     NGDMDSSSEA MPSPEDSFDG VLRLTTSLTE GSASLSLSAS ESIPGHGHKR SISAANLAEV
     SSKRQRLSFS PEDGDSNPES ALIGGSHGAT THQAQISTAS HLKSADVTSH ARYRTKAPTA
     NGLSAKSLSI VKSSSQESLK GAQLPLSQPL PFPVSKDPHD PAMALRLSQK SASQPSQSEV
     KKHVSFEPFL PSSRVDTTLL DSHSSALEPS SNTHSGLLET VLTNMNRNFT KLGSGVTLLL
     GELPPSELSV TSTMQDFNLP TVIYQDAFYS NETDVPERAR EWAGREFRLE SLTVPFLPEF
     DPTGTSEATF GEKPGVVSDK TKEDKMYQWQ RRHCTLRSWV IADPPPTYSE VAQWSHNEIE
     KRLQTTSERT PHLRAVASPR PRTKLSQIEG PTQKNKHGFK YTQNLKTTSA KHEAQYMSTM
     SLELHVNTRG NFVPNPEEDE VQCLFWCLQS DEAGLDSNGI TGGTHIGVVV LSDESTLPQK
     IAKQIAVEVQ GESSELDLII RMVEIVRNHD PDILTGYEVH GGSWGYLIER ARLKYEYNLC
     DEFSRMKAQS HGRFGKDNDK WGFNNTSTIR VTGRHMINIW RAMRSELNLL QYTMENIVFH
     LLRRRVPHFT WADLTRWYTS GKPWDLAKVV NYYITRVQLD LEILEQNELI PRTSEQARLL
     GVDFFSVFSR GSQFKVESLM FRIAKPENFL LVSPSRKQVG GQNALECLPL VMEPQSAFYN
     SPLLVLDFQS LYPSVMIAYN YCYSTFLGRV VNWRGTNKMG FTEFKRQQGL LELLKDHINI
     APNGIMYTKP EIRKSLLAKM LGEILETRVM VKSGMKVDKD DKALQRLLNN RQLALKLIAN
     VTYGYTSASF SGRMPCSEIA DSIVQTARET LEKAIALIHS VKRWGAEVVY GDTDSLFVYL
     KGRTKDQAFD IGEEIAKTVT NMNPRPVKLK FEKVYLPCVL LAKKRYVGFK YECRNQTEPD
     FDAKGIETVR RDGTPAEQKI EEKALKILFR TSDLSQVKEY FQQQCEKIMK GSVSVQDFCF
     AREVKLGTYS DKGPPPPGAL ISTKRMLEDA RAEPQYGERV PYVVITGAPG ARLIDRCVAP
     EKLMESDHSE LDAEYYISKN LIPPLERIFN LVGANVRGWY DEMPKVQRIR RVDANLQLQG
     QSKELAIGKK TLESYMKSSS CLVCKEKLEL EGPICSGCLA DKPVSLLTLR KRLNDEERMF
     MNLRKICQSC SGISPLEDVR CDSKDCPVFY TRTRQKARLN TERAVVEPVM KELSGLIVDM
     HDLDW
//
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