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Database: UniProt
Entry: W9XNX1_9EURO
LinkDB: W9XNX1_9EURO
Original site: W9XNX1_9EURO 
ID   W9XNX1_9EURO            Unreviewed;      1731 AA.
AC   W9XNX1;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   05-JUN-2019, entry version 27.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=A1O1_07958 {ECO:0000313|EMBL:EXJ81893.1};
OS   Capronia coronata CBS 617.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ81893.1, ECO:0000313|Proteomes:UP000019484};
RN   [1] {ECO:0000313|EMBL:EXJ81893.1, ECO:0000313|Proteomes:UP000019484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ81893.1,
RC   ECO:0000313|Proteomes:UP000019484};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Capronia coronata CBS 617.96.";
RL   Submitted (MAR-2013) 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}.
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:EXJ81893.1}.
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DR   EMBL; AMWN01000007; EXJ81893.1; -; Genomic_DNA.
DR   RefSeq; XP_007727014.1; XM_007728824.1.
DR   STRING; 43229.XP_007727014.1; -.
DR   EnsemblFungi; EXJ81893; EXJ81893; A1O1_07958.
DR   GeneID; 19162813; -.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000019484; 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:UP000019484};
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:UP000019484};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN       50    244       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      834   1032       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN     1098   1545       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1599   1689       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION      424    452       Disordered. {ECO:0000256|MobiDB-lite:
FT                                W9XNX1}.
FT   REGION      522    579       Disordered. {ECO:0000256|MobiDB-lite:
FT                                W9XNX1}.
FT   REGION      596    659       Disordered. {ECO:0000256|MobiDB-lite:
FT                                W9XNX1}.
FT   REGION      809    829       Disordered. {ECO:0000256|MobiDB-lite:
FT                                W9XNX1}.
FT   REGION     1711   1731       Disordered. {ECO:0000256|MobiDB-lite:
FT                                W9XNX1}.
FT   COMPBIAS    553    579       Polar. {ECO:0000256|MobiDB-lite:W9XNX1}.
FT   COMPBIAS    596    653       Polar. {ECO:0000256|MobiDB-lite:W9XNX1}.
SQ   SEQUENCE   1731 AA;  195638 MW;  144B0AB7EFDFE816 CRC64;
     MDPFRVRLNC IDHYQAVPLD EFDPPVPQGL VHENAKERPR ISVIRVFGAT ETGQKVLMHI
     HGALQYTYIE YSGSLVPEDV DVAIRTLQLS IDHALAVSYR KNIYEGKHRY VAHISLVKGV
     PFYGFHVGYR FYLKIYLLNP LHMTRLADLL REGAVMKRVL QPYESHMQYL AQWMCDYNLY
     GCGYIECDKV KFRGPIPKYF DMTSAMHQWH DHSIPPEYIS DEAALPKQSN CSLEVDVHVK
     DILNRRDVHA RDLHHDFIER VHLLSADAKL VQSMAGLWKD ETRRRKIRMG LKDNNSSPFP
     PEVLISMSAD PRDTSAGGWI HEEEYREKVE QIVTEEHAKG DAAKVSFDNF VKPVSLESTV
     KTALESVEDL YPHNMREPGF GSRNHRPSTP NQENVAHETV IDGAQAENVI GGLDHSLSDA
     VASNEGSFSM SKSSDDSSAK DTHDNGRVLT PISSSEYEKY GIRRAGDTAR LAEDVFEVPE
     EYLGQDPVPP NKAKRARFAV APSFKPRKRR KQLMDDDNVF PEVSFSGSED DPDFVTDAEG
     MDPAAEPTSE EMRSVRLSGT NQHQLPFSTQ AARSKDTSVE GPNALLLSQQ STLSFSAVKN
     PNDPTTILRL SQKSGTSPKS SQTASVKPPT SPVIQKTPAE SVLTSSQPTL RPPMSAESVK
     PTAPVDIIIS GLSSGRTGAC WHTYQIRPPS FHEVETTLRQ HGLPDVIYQE AFYSNEDDVP
     DQAREYAGRE FKLESATVPY LPDFDSSGAS PATYGRKPAA LVDVTGESVR DNQRRKRCTI
     SNWVISESPP RKADVVSWLK EEHAAKEHDT SFRMKSRRPL SQIDGPTQKN KYGFKYSQKQ
     ASTSVHHETQ YMSIMSLEVH VNTRGSLAPN PEEDAVACIF WCIQTDDDEV ETNGSKDGMH
     VGVIAVADEP HMGKNIGRIL PYDVEEEATE LDVLTRLVDI VRHYDPDILT GYEVHNSSWG
     YLIERARVKY DLNYCDELSR MKSQSHGRFG KDDDRWGFNH TSTIRVTGRH TINIWRAMRG
     ELNLLQYTME NVVYQLLHQR TPHYTFADLT RWYRSKNPRD LAKAVEYFCS RVQMDIEILD
     ANELVPRTSE QARLLGVDWF SVISRGSQFK VESLMFRIAK PENFMLVSPS RRQVGGQNAL
     ECLPLVMEPR SDFYTSPMLV LDFQSLYPSV MIAYNYCYST FLGRVVSWRG TNKMGFTDYR
     REPRLLELLK DHINIAPNGI MYAKPHIRKS LLAKMLSEIL ETRVMVKSGM KVDKDDKTLQ
     RLLNNRQLAL KLIANVTYGY TSASFSGRMP CSEIADSIVQ TGRETLEKAI ALIHSVERWG
     AEVVYGDTDS LFVYLKGRTR DQAFDIGEEI AAAVTNMNPR PVKLKFEKVY HPCVLLAKKR
     YVGFKYESRN QTTPDFDAKG IETVRRDGTP AEQKVEETAL KLLFRTADLS QVKRFFQAQC
     SKIMRGNVSV QDFCFAREVK LGTYSDKGPP PPGALISARR MLQDPRLEPQ YGERVPYVVV
     TGGPGARLID RCVAPEVLLN DPHAELDAEY YISKNLIPPL ERIFNLVGAN VRQWYDEMPK
     YQRIRRVEGV GVGGDLNLHQ HQNQKKKATL ESYMKSSTCL VCRELLDTST TTTAATTSTT
     AAAALSANLG LCSNCIRNSA RSILTLRTRL TKTERRVNQL AKVCRSCSGL AWNEEVKCDS
     KDCPVFYSRT RYNVSWGNER AQLGPVLESL ERHDDDDGNE HVKVNESGLE W
//
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