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Database: UniProt
Entry: A0A1E3PEB0_9ASCO
LinkDB: A0A1E3PEB0_9ASCO
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ID   A0A1E3PEB0_9ASCO        Unreviewed;      1046 AA.
AC   A0A1E3PEB0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   08-MAY-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=NADFUDRAFT_62083 {ECO:0000313|EMBL:ODQ63544.1};
OS   Nadsonia fulvescens var. elongata DSM 6958.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetales incertae sedis;
OC   Nadsonia.
OX   NCBI_TaxID=857566 {ECO:0000313|EMBL:ODQ63544.1, ECO:0000313|Proteomes:UP000095009};
RN   [1] {ECO:0000313|EMBL:ODQ63544.1, ECO:0000313|Proteomes:UP000095009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6958 {ECO:0000313|EMBL:ODQ63544.1,
RC   ECO:0000313|Proteomes:UP000095009};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T.,
RA   Goker M., Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H.,
RA   Aerts A.L., Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S.,
RA   Douglass A.P., Hanson S.J., Klenk H.P., LaButti K.M., Lapidus A.,
RA   Lindquist E.A., Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A.,
RA   Otillar R.P., Pangilinan J.L., Peng Y., Rokas A., Rosa C.A.,
RA   Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B., Sun H.,
RA   Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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; KV454414; ODQ63544.1; -; Genomic_DNA.
DR   EnsemblFungi; ODQ63544; ODQ63544; NADFUDRAFT_62083.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000095009; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   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; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
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:UP000095009};
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:UP000095009};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN       80    416       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      480    913       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN      951   1024       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
SQ   SEQUENCE   1046 AA;  118878 MW;  CBAC2D583B16FA56 CRC64;
     MTAKSGSLKA EKPSEFEQDL TLLTQEIKSS QGLLSSHDQV WPRLPVKDFD HSTTDITFQQ
     IEVEETSFRG QPVLRLFGVT ENGQSVCCNI TGFNHYFYVA APIGFGIHHT DNLAQYLNNR
     LEQHIVKNIE IVTKENLWGY KGDQKVPFLK IIVSQPDRIA KVRGFFERGL IDFDCFFPMQ
     VTTYDNISYD LRLMVDCKIS GMSWVTLPAG KYLPLDHDLV SRCQYEVSIP YESLIAHPID
     GEWSKIAPLR VLSFDIECAG RKGVFPDPNI DSVIQIANVV SKYGEARPFV RNVFTLNTCS
     PIIGTEVYEN KTEQEMLIKW RDFVREVDPD VIIGYNTANF DFPYLLDRAK ALKVNDFPYF
     GRLVNNRQEV KSSTFSSKAY GTRESKVVNI DGRLQLDLLQ FIQREYKLRS YTLNSVSAHF
     LGEQKEDVHH SQITELQNGT AESRRRLAVY CLKDAYLPIR LMEKLMCLVN YTEMARVTGV
     PFSYLLSRGQ QIKVVSQLFR KALSFDLVVP NMRRDGGGSD EQYEGATVIE PIRGYYDMPI
     ATLDFSSLYP SIMMAHNLCY TTLLDKETIK RLNLQKDLDY TLTPNGDCFI KTTKRKGLLP
     VILEELLGAR KRAKADLKKE TDPFKKAVLD GRQLALKISA NSVYGFTGAT VGKLPCLEIS
     SSVTAFGREM IEKTKNEVED FYSIKNGYEY DAQVIYGDTD SVMVKFGSGD LGTCMKLGEE
     AAAHVSTKFI TPIKLEFEKV YFPYLLINKK RYAGLYWTNT KKFDKMDTKG IETVRRDNCR
     LVQNVIETIL RKILMDRDVE GAQTYVKGII SDLLQNNVDL SQLVITKQLS RADYTAKQAH
     VELAERMRKR DAGSAPAIGD RVAYVIIKGS IGGKNYEKSE DPLYVLENNV PIDTKYYLEN
     QLSKPLGRIF EPILGEKKFQ QLITGAHTRT VSIAAPTTGG LMKFAVKTEL CKGCKAPLRG
     KFAKSALCEK CLPRAGELYS KELNKMNDLE TKFGKLWTEC QRCQGSLHQD VLCVSKDCPI
     FYMRKKVQKD MNISVEELKK FDSTDW
//
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