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Database: UniProt
Entry: A0A1V6NYS1_9EURO
LinkDB: A0A1V6NYS1_9EURO
Original site: A0A1V6NYS1_9EURO 
ID   A0A1V6NYS1_9EURO        Unreviewed;      1698 AA.
AC   A0A1V6NYS1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   05-JUN-2019, entry version 12.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=PENPOL_c002G01865 {ECO:0000313|EMBL:OQD69875.1};
OS   Penicillium polonicum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60169 {ECO:0000313|EMBL:OQD69875.1, ECO:0000313|Proteomes:UP000191408};
RN   [1] {ECO:0000313|Proteomes:UP000191408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 4502 {ECO:0000313|Proteomes:UP000191408};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J.,
RA   Nielsen K.F., Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential
RT   of secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OQD69875.1}.
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DR   EMBL; MDYM01000002; OQD69875.1; -; Genomic_DNA.
DR   Proteomes; UP000191408; 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:UP000191408};
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:UP000191408};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN       49    195       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      850   1032       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN     1098   1544       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1595   1667       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION      282    315       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1V6NYS1}.
FT   REGION      407    434       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1V6NYS1}.
FT   REGION      480    592       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1V6NYS1}.
FT   REGION      605    645       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1V6NYS1}.
FT   COMPBIAS    407    424       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1V6NYS1}.
FT   COMPBIAS    499    524       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1V6NYS1}.
FT   COMPBIAS    534    557       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1V6NYS1}.
FT   COMPBIAS    558    575       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1V6NYS1}.
FT   COMPBIAS    611    645       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1V6NYS1}.
SQ   SEQUENCE   1698 AA;  192493 MW;  2DC04EAE5377F132 CRC64;
     MEPFRVRLNC IDHYQATASE LDPPLPFRDE VSEKDFKPKV PVIRIFGATE TGQRVVVHVH
     GAFPYLYIEY NGSLTPEDVN SAIRTLHLSI DHALAVSFRR NAYDRRTAFV AHVTLVKGVP
     FYGYHVGWRF FFKIYLLNPF HTTRLVDLLH QGAVMKRPLQ PYEAHVQYIP QWMCDYNLYG
     CATMNCSQVK FRAPVPEYFE LSNLAHRWHD RSIPPESILD HPALQKQSNC ALEVDICVQD
     ILNRLDVKER PLHHDFTELL KPVAVNERLV PSMAGLWQDE TRRRKKRMGI TDPGSTPFGP
     EELVSMSADP RDQSRSGWIH EEEFREMAAQ LAANEKHQDG NNDTSFGTFL GTDDLAKNVK
     TALDSVKDFF PGTISTLAFD SSRSQQPGEN KVPEISVDEG LALSSQTDGQ YYSDSDQGGN
     SLEGRTEQDP EPKEDLLGES FYDEVFDEMP FSDVAAPAEP AETSNPKATM DGVYKEGISV
     AQEKRPGDLS QSRSVGPKRQ HFETLDSPHS PAKRPRHMPK HGLSDGPLES HNTQKHQQGD
     KQKNVSFDSK LDSHAETPSS EPKSSSSQRT VRPKAHSYTS GLKFPVVKDP SDPLTILRYS
     QDEASSSRKD LEPSQHLFSF PSGSATELPG ETSETQSSSE LHSSATVMGP VSLDPHLAET
     MKNIHQSFNF TPNRSLRFFK FASPTSTEVS STLNEHGRPS VVYQKAFYSD ETDVPERPRE
     YGGREFQLES NTIHYLPDFD PTAEGPAMFG EQIPATHDRD QQGKVDQQLR EKCTARVWEF
     APVPPSRSEV IQWCEELKAS REPNQKAAQT IPAQTKSDLL SQIEGPTQKN AHGFKYSQHG
     VSTSVEHQAQ HMSTMSLEVH VNTRGTLMAN PEEDEITSLF WCIQSEDEDL EVNSHLPGVH
     VGMVYHGEGE RPEAKLSKAL TIDIECEPTE LDLINRLIDI VRYHDPDIIT GYEVHSASWG
     YVIERARKKY DFDICEELSR TKSQSNGRFA KETDQWGHNH SSSVRITGRH VFNIWRAMKG
     ELNLLQYTME NVVFHVLHRR IPHYSPKDLT KWHQSGKPRN LLKVVEYFTS RVQMNLEILE
     ANELAPRTSE QARLLGIDFA SVISRGSQFK VESLMFRIAK PENFLLVSPS RKQVGQQNAL
     ECLPLVMEPQ SDFYTSPLLV LDFQSLYPSV MIAYNYCYST FLGRAMHWRG RDKMGFMDYK
     RQPRLLELLQ DKINIAPNGM MYVKQEARQS LLAKMLSEIL ETRVMVKNGM KADKDDKVLQ
     RLLNNRQLAL KLIANVTYGY TSASFSGRMP CSEIADSIVQ TGRETLEKAI AFIHSIDRWG
     AEVVYGDTDS LFVYLKGRTR DQAFDIGEEI AQAVTDLNPR PIKLKFEKVY HPCILLAKKR
     YVGFKYEHRQ QKEPEFDAKG IETVRRDGTP AEQKIEEKAL KTLFRTADLS QVKSYFQRQC
     AKIMQGRISI QDFCFAREVR LGTYSERNLP AGAVISTKRM MEDPRSEPQT GERVPYVVVT
     GAPGSKLVDR CVSPETLLHD AQLEIDVEYY ITKNIIPPLE RIFNLVGANV RQWYDEMPKV
     QRIRRVEGSA VARPSSRAGA VGRKTLESYM RSSSCVVCRS RLSDAAVPVC GDCLQKPHLT
     LLDVVSRLQR AEKRVVDLEA ICRSCMGVSP GDEVSCDSLD CSIFYSRTRD AANWRHSRAV
     LEPVVELLER KGDEGLDW
//
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