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Database: UniProt
Entry: A0A178ENE2_9PLEO
LinkDB: A0A178ENE2_9PLEO
Original site: A0A178ENE2_9PLEO 
ID   A0A178ENE2_9PLEO        Unreviewed;      1714 AA.
AC   A0A178ENE2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   05-JUN-2019, entry version 17.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=IQ07DRAFT_15180 {ECO:0000313|EMBL:OAL56699.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Cucurbitariaceae; Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL56699.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL56699.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL56699.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L.,
RA   Chaput D.L., Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-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; KV441636; OAL56699.1; -; Genomic_DNA.
DR   EnsemblFungi; OAL56699; OAL56699; IQ07DRAFT_15180.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000077535; 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:UP000077535};
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:UP000077535};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN       49    190       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      831   1008       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN     1076   1521       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1578   1663       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION      408    433       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A178ENE2}.
FT   REGION      445    502       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A178ENE2}.
FT   REGION      525    554       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A178ENE2}.
FT   REGION      579    615       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A178ENE2}.
FT   REGION      772    797       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A178ENE2}.
FT   REGION     1688   1714       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A178ENE2}.
FT   COMPBIAS    468    502       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A178ENE2}.
FT   COMPBIAS    536    554       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A178ENE2}.
SQ   SEQUENCE   1714 AA;  194023 MW;  3FBB1B17C86FC0F6 CRC64;
     MDTFRFRLNC IDNYQATPTE LDPVLRRSTG PSQRQGVPYV PVIRAFGATE TGQKVCAHIH
     GALPYLYLDY SGSLDKDTVN AYLVALRASI DHALAATYRR NPYDGKSVYV GHISLVKGVP
     FYGYSVGYKV FLKVYLLNPM HMTRFADLLY QGAILNRIFQ PYESHMQYLL QWMCDYNLYG
     CSYIDCAKVK FRGPVPDSDE TDVTIHKWHD ASIPEEMISD EGQFPRQSHC TLEVDVCVQD
     ILNRHELQYR PIHHDFLERS SQMPRNPDDK YVPSMAGLWR DETRRRKRRM GLSNPSSSPF
     PAEVLVSMSA DSRNTDKGGW IHEDEYRDLI ADLIKEEKKQ KDHVHFETFV KPVQGLDSIK
     TAVEGIEDLY PENLAKEELP AETEEEAVQP IDMYAGTTVP DVRPEDLQLQ DDKPVTKGQG
     DEEVGANNQS DIEEEQSLDP LTASLLQNYG NGSSEHDLMD EGVDLSSPKD DTSINGPQDI
     PTSRKRASPQ THEQSFKRQR IPLVSQGTPK RVSFQNIARG DSEHLAHASQ RPVDDALLPP
     SQSSQASIKA QGIGGPTTLS FPVVKNPGAP ETLLRLSQSG YSNSQESPKT PKTPWAKHNA
     SKVSQPTPEG IWSHQKTSSV VRSTGSPGTP PETLKLIEQL GTSFDHKAST LYYGCLPPSP
     EVIESTIMHA GLPPVIYQDA FYSDETDVPD RAREYAGREF KLQSNSLPYL PPFDPTGTSE
     ANFGEYPPVL VDKTKEAAVN QARSHRCSLR NWEIAMPPPS YKEVNDWLRR ETKSQNMDKS
     TPKKTLKQEV KPRKTKTLNH LSQIEGPTQR NKHGFKFSQK KRSTSVKHDT QYMSIMSLEV
     HANSRGSLVP DPAEDEIQCI FWSIEGEENA KTDRPHVGIL CLSDENGIAE RIAKSVSVEV
     EYEEDELDLI NRMVDIVRQF DPDILTGYEV HNGSWGYLIE RARMHFEYDL CDEISRMKSQ
     SHGRFGKEAD RWGFTHTSTI RITGRHMINI WRAMRGELNL LQYTMENVAF HLLHKRIPHY
     QHADLTDWYK SSRPRDLSKV LDYFLTRVQL NLDILEANEI VPRTSEQARL LGVDFFSVIS
     RGSQFKVEST MFRIAKPENF ILVSPSRKQV GKQNALECLP LVMEPQSDFY SSPLLVLDFQ
     SLYPSVMIAY NYCYSTCLGR IVGWRGRNKM GFMDFKREPQ LLELVKDHIN IAPNGMMYVK
     PEMRKSLLAK MLGEILETRV MVKSGMKQDK DDKTLQQLLN NRQLALKLLA NVTYGYTSAS
     FSGRMPCSEI ADSIVQTGRE TLEKAIALIH ATEKWGAEVV YGDTDSLFVY LKGRTRDQAF
     TIGEEIAAAI TAANPRPVKL KFEKVYHPCV LLAKKRYVGF KYESRNQVEP EFDAKGIETV
     RRDGTPAEQK IEERALKLLF RTSDLSQVKR YFQDQCAKIM QGRISIQDFL FAKEVKLGSY
     SDRGPPPPGA LIATKRMLAD PRTEPQYGER VPYVVITGAP GARLIDRCVS PETLLQSDHL
     ELDAEYYISK NLIPPLERIF NLVGANVRQW FDEMPKVQRI RSIALPINTK QDPGNMQTMG
     GNASLKKTLE SYMKSSACLV CRTKLPPTPT HLPGVDVDAF AVLPLCANCL RRPARSLLAL
     KDRIWESEVH VKNVDMVCRS CSSLAWGEEI RCDSRDCPVF YTRIRERSKL SGLKESIGPV
     IEVLETSNDN EETEGLVGME SEENSRQGSE DLAW
//
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