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Database: UniProt
Entry: A0A1J7ITM7_9PEZI
LinkDB: A0A1J7ITM7_9PEZI
Original site: A0A1J7ITM7_9PEZI 
ID   A0A1J7ITM7_9PEZI        Unreviewed;      1751 AA.
AC   A0A1J7ITM7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-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=CONLIGDRAFT_630624 {ECO:0000313|EMBL:OIW30669.1};
OS   Coniochaeta ligniaria NRRL 30616.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Coniochaetales; Coniochaetaceae;
OC   Coniochaeta.
OX   NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW30669.1, ECO:0000313|Proteomes:UP000182658};
RN   [1] {ECO:0000313|EMBL:OIW30669.1, ECO:0000313|Proteomes:UP000182658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW30669.1,
RC   ECO:0000313|Proteomes:UP000182658};
RG   DOE Joint Genome Institute;
RA   Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA   Van Elsas J.D., Nichols N.N.;
RT   "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT   lignocellulolytic fungus for bioabatement of inhibitors in plant
RT   biomass hydrolysates.";
RL   Submitted (OCT-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; KV875096; OIW30669.1; -; Genomic_DNA.
DR   EnsemblFungi; OIW30669; OIW30669; CONLIGDRAFT_630624.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000182658; 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:UP000182658};
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:UP000182658};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN       50    242       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      965   1081       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN     1149   1594       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1644   1718       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION      424    476       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1J7ITM7}.
FT   REGION      533    554       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1J7ITM7}.
FT   REGION      573    682       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1J7ITM7}.
FT   REGION      857    883       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1J7ITM7}.
FT   COMPBIAS    424    450       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1J7ITM7}.
FT   COMPBIAS    453    468       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1J7ITM7}.
FT   COMPBIAS    535    554       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1J7ITM7}.
FT   COMPBIAS    616    677       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1J7ITM7}.
SQ   SEQUENCE   1751 AA;  198058 MW;  BEA3FD1AD8C14C4E CRC64;
     MDQVFRVRLN CIDYYRVSPT KYDPVLRKHV RNSQLSKEPE VPVIRVFGST ETGQKVCAHI
     HGAFPYMFVE YTGSLAPEVV GAYIYQLHLS IDHALAASYR RTNSAKPPKF VARVTLVKAV
     PFYGFHVGYR FYLKIYMLNP LVMTRLADML HQGLIMNRKF QPYESHLQFL LQFMVDYNLY
     GCGYIETKNV AFRAPVPRYD AEEVMPHNWH SQSVRPESIT EDIQLPRVSH CSIEVDICVQ
     DILNRSAIHE RPLHHDFVER LHPQPADVKL VHSMAGLWND EAKRRKRRMA GKDAKSSPFA
     PEALVSMSAD LRHSQSPGWI HEEEYREQIN ELIKQEAGVT GEEPSFEGFV QRPPGEDSVK
     TVLQSVEDLY PENLLPQLGL DVQYPNLEQH PDSSIVVDEQ GILDFEGDGD DSDVFPYDFE
     EELVGKAKIP GDQEESSEES LGDEKLVKLG ESGESSGASN STKATEGIRR TSGPDFDGDD
     LALDAVDCLA AGVYSSGLRT GRPPHVPIST ELAAEIMRDG LVSKITQNGQ KETFADKPLL
     KRRQKAHDDQ PSLKKLKSIH GLDLDSLAMH HHDKSALTTP DEITKGPVTI EEQIRKPSSS
     QRKTAPAEGD HRKGRGNQTL SFNVVKDPND PNTRLRLSQL SAASQRGEDS LLKRQPSFNP
     TATLVGNSSS ETGLHEESLS KPSVPLASLP EWTSTATKIC NPGLVWDARR TMYCLSVSPP
     SADEVLKSMQ EYGLPDVIYQ DPYYSDEKDV PPRTREYAGR EFRLEGSTLP FLPDFDPTGR
     SPATFGVRAE LGFTERRKAD AAIYERQRAH CSLRSWEIAE SPPAFDEVAG WWQARLQKQD
     ETAQKKQSAE AILATQRKSN QYQSQVEGPT PKNKHGFKYS QKRKSTSVQH EAQYMSTMSL
     EVHVNTRGKL VANPEEDEVK CIFWCVKSDE DFSLTSQSAD NNNNNNNMLS GVVVLSEDGT
     LAQRIRSMTS LEVFEEASEW DMMVRMVELV RTYDPDVLTG YEVHGGSWGY LIERARFKYE
     YDLCDEFSRM KSLSHGRIGK DADKWGFNTT STIRVTGRHM INIWRAMRGE LNLLQYTMEN
     VVWHLLHRRI PHYSYKDLTE WYSSGRVADL DKVLKYHLIR TRLDIEILET NELIPRTSEQ
     ARLLGVDFFS VFSRGSQFKV ESIMFRIAKP ENFLLVSPSR KQVGGQNALE CLPLVMEPQS
     AFYNSPLLVL DFQSLYPSVM IAYNYCYSTF LGRIVNWRGT NKMGFAEYKR REGLLKLLKE
     HINIAPNGMM YTKAEIRKSL LARMLTEILE TRVMVKSGMK QDKDDRTLQQ LLNHRQLALK
     LLANVTYGYT SASFSGRMPC SEIADSIVQT GRETLERAIA YIHSVDCWDA EVVYGDTDSL
     FVHLKGRTRE QAFKLGDEIA KAITDLNPRP IKLKFEKVYH PCVLLAKKRY VGYKYEHPDQ
     AQPEFDAKGI ETVRRDGTPA EQKIEEKALK LLFGTADLSE VKAYFQAQCT KIMHGNVSVQ
     DFCFAREVKL GTYSDKGPPP PGALISTKRM LEDARAEPQY GERVPYVVVS GGPGARLIDR
     CVAPEDLLHD PHASLDAEYY ISKNLIPPLE RIFNLVGANV RQWYDEMPKV QRIRRVDASS
     LAGPATGAAW KKKTLEAYLK SASCAVCGVK MHKESVGTVC SRCKRDTAAS MVKVQRRLNA
     DEVRLRDAVK VCQTCAGLPP VDVDVRCDSK DCPVFYSRTK LASRVRTERS IVESVLSELE
     DPEAGRRELE W
//
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