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Database: UniProt
Entry: A0A0F7TK92_9EURO
LinkDB: A0A0F7TK92_9EURO
Original site: A0A0F7TK92_9EURO 
ID   A0A0F7TK92_9EURO        Unreviewed;      1717 AA.
AC   A0A0F7TK92;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   05-JUN-2019, entry version 20.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=PMG11_05882 {ECO:0000313|EMBL:CEJ57178.1};
OS   Penicillium brasilianum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=104259 {ECO:0000313|EMBL:CEJ57178.1, ECO:0000313|Proteomes:UP000042958};
RN   [1] {ECO:0000313|EMBL:CEJ57178.1, ECO:0000313|Proteomes:UP000042958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) 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; CDHK01000005; CEJ57178.1; -; Genomic_DNA.
DR   EnsemblFungi; CEJ57178; CEJ57178; PMG11_05882.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000042958; 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   Complete proteome {ECO:0000313|Proteomes:UP000042958};
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:UP000042958};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN       49    218       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      932   1048       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN     1115   1561       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1614   1686       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION      281    316       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0F7TK92}.
FT   REGION      401    441       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0F7TK92}.
FT   REGION      508    540       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0F7TK92}.
FT   REGION      558    659       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0F7TK92}.
FT   COMPBIAS    418    435       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0F7TK92}.
FT   COMPBIAS    560    592       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0F7TK92}.
FT   COMPBIAS    622    659       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0F7TK92}.
SQ   SEQUENCE   1717 AA;  195037 MW;  5DE3F5D44438E181 CRC64;
     MEPFRVRLNC IDHYQATASE LDPPLPFRDG VSEKDYRPRV PVIRVFGATE TGQRICVHVH
     GAFPYLYIEY NGSLAPEAVN SVIRTLHLSI DHALAVSYRR NAYDRKTAYV AHITLVKGIP
     FYGYHVGYRT FFKIYLLNPF YITRLADLLH QGAVMKRPLQ PYESHLQYVP QWMCDYNLYG
     CGYMNCSKVK FRAPVPEYLE LSNLHHRWHD RSISPESILD DPALQKQSHC PLEVDVCVQD
     ILNRFDVKER PLHHDFTELL RPAAINERLV PSVAGLWQDE TKRRKKRMGL TDPDSTPFGP
     EDLVSMSADP RNQAKGGWVH EDEFRELVLQ IAANERSEDN ERDTSFESFL SPDSEKVNIK
     TALTSVQDFY PDRLHESTLN GRQYERQDVD EAKAEISVDE GLALSSQVDG NYASEPELDQ
     PRTDEAGEEK SHNQPHPYET PVLEESFYDG IFDELTEPSE VQPEHAHQPN VLDLHSSGTL
     TNIPPAFEMG LKADIQAQRQ LNEKAKGFKR AHTEITSDKA APSVKKPRFL TEPDDINAQE
     NGIEDAYDLE AAKRASYPSK HLAASQSSES RSSSSQKTIR PSKATAQVHN SRINFPVVKD
     PNDPLTILRF SQDDGHSSSK KDLEYQPMQN SCPSASATSA TQGDATGASS SLPRSSSTMG
     RSVIALDPHV AALKSTIHGS FDFQRDAVLC LPRFAGPATN EVVSTMNDFG RPAVIYQKAY
     YSNEADVPER PRQYAGREFS LDSDTIQFLP EFDPSGNIPA MFGEQQPSIL VDREKKEKID
     QQLRESCTAR FWEFAPVPPS RSEVVDWFEQ IEASSRKATT APVKHKPCPA KNVEALSQIE
     GPTQRNPYGF KYSQNAKSTS VEHQTMYMST MSLEAHVNTR GTLSANPDED EISCLFWCLQ
     SEDEDIEVNS YLPDVHVGMI YQGEGDRPEA KISKSLRIEV EHEPTELDLI NRLVDIVRYH
     DPDIITGYEV HNGSWGYVIE RARKKYDFDL CAELSRVKSQ SKSKFGKDDD RWGFEHASSI
     QMTGRHMINI WRAMRGELNL LQYTMENVVF HLLQRRIPHY SAKDLTQWYQ SGKPRNMLKV
     VEYFTSRVQM NLEIMEANEL IPRTSEQARL LGIDFYSVFA RGSQFKVESL MFRIAKPENF
     LLVSPSRKQV GQQNALECLP LVMEPQSNFY TSPLLVLDFQ SLYPSVMIAY NYCYSTFLGR
     AVQWRGRDKM GFLDYKREPR LLELLKDKIN IAPNGMIYAK QEVRQSLLAK MLTEILETRV
     MVKSGMKADK DDKALQRLLN NRQLALKLIA NVTYGYTSAS FSGRMPCSEI ADSIVQSGRE
     TLEKAIAFIH SVERWGAEVV YGDTDSLFVY LKGRTRDQAF DIGEEIAQAV TDMNPRPIKL
     KFEKVYHPCV LLAKKRYVGF KYEHRKQAEP EFDAKGIETV RRDGTPAEQK IEEKALKLLF
     RTADLSQVKS YFQRQCSKIM QGRVSIQDFC FAREVRLGSY SERGTLPAGA MISTKRMLED
     PRLEPQYGER VPYVVVTGAP GSRLIDRCVA PETLLHDAQL DLDAEYYITK NLIPPLERIF
     NLVGANVRQW YDEMPKVQRI RRVDVSSTSA LSRSNREFAI SKKTLESYMR SSSCIICRAK
     LSDAAVPVCS ECLQQPHLAL LNVVSQLQRA EKRVLDLEAV CRSCMGVPPG DTIACDSMDC
     PVFYSRTRDA AGLRHIKATL EPVVEILEKK GDDGLDW
//
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