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Database: UniProt
Entry: A0A1R3RGN4_ASPC5
LinkDB: A0A1R3RGN4_ASPC5
Original site: A0A1R3RGN4_ASPC5 
ID   A0A1R3RGN4_ASPC5        Unreviewed;      1098 AA.
AC   A0A1R3RGN4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   05-JUN-2019, entry version 15.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=ASPCADRAFT_508741 {ECO:0000313|EMBL:OOF93645.1};
OS   Aspergillus carbonarius (strain ITEM 5010).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=602072 {ECO:0000313|EMBL:OOF93645.1, ECO:0000313|Proteomes:UP000188318};
RN   [1] {ECO:0000313|Proteomes:UP000188318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ITEM 5010 {ECO:0000313|Proteomes:UP000188318};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K.,
RA   Battaglia E., Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C.,
RA   Canovas D., Cerqueira G.C., Chen F., Chen W., Choi C., Clum A.,
RA   Dos Santos R.A., Damasio A.R., Diallinas G., Emri T., Fekete E.,
RA   Flipphi M., Freyberg S., Gallo A., Gournas C., Habgood R., Hainaut M.,
RA   Harispe M.L., Henrissat B., Hilden K.S., Hope R., Hossain A.,
RA   Karabika E., Karaffa L., Karanyi Z., Krasevec N., Kuo A., Kusch H.,
RA   LaButti K., Lagendijk E.L., Lapidus A., Levasseur A., Lindquist E.,
RA   Lipzen A., Logrieco A.F., MacCabe A., Maekelae M.R., Malavazi I.,
RA   Melin P., Meyer V., Mielnichuk N., Miskei M., Molnar A.P., Mule G.,
RA   Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P., Overkamp K.M.,
RA   Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F., Ramon A.,
RA   Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E.,
RA   Sanguinetti M., Schuetze T., Sepcic K., Shelest E., Sherlock G.,
RA   Sophianopoulou V., Squina F.M., Sun H., Susca A., Todd R.B., Tsang A.,
RA   Unkles S.E., van de Wiele N., van Rossen-Uffink D., Oliveira J.V.,
RA   Vesth T.C., Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B.,
RA   Baker S.E., Benoit I., Brakhage A.A., Braus G.H., Fischer R.,
RA   Frisvad J.C., Goldman G.H., Houbraken J., Oakley B., Pocsi I.,
RA   Scazzocchio C., Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S.,
RA   Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(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}.
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DR   EMBL; KV907504; OOF93645.1; -; Genomic_DNA.
DR   EnsemblFungi; OOF93645; OOF93645; ASPCADRAFT_508741.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000188318; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000188318};
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:UP000188318};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN      123    468       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      532    962       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1000   1074       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION        1     92       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1R3RGN4}.
FT   COILED     1074   1094       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS     41     57       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1R3RGN4}.
FT   COMPBIAS     58     92       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1R3RGN4}.
SQ   SEQUENCE   1098 AA;  124572 MW;  BEEEBAAD8FB22F42 CRC64;
     MPEAVATPQK RVLGDATNNT PRGVTKDPNA LKKRKLDNPT TSSQRRVPGS GQPQKSQFEE
     EVLEKLTQDI NGLKDSNSEK DQQWERPPLG EFDPAKENIC FQQIDAEEGL IMGKTAVRLF
     GVTEAGQSVL LHVTGFQHYL YIAAPVNFTK EDCDPYRTFL ESRLGNFQPM IHSVQITMRE
     NIYGFQGNQK SYYLKITVTD PKYISKVRNA LESGGAQSLN YKGLWNNSDP GILTFDIIQY
     LLRFMIDTDI SGMSWIEAKA GKYRLLHNQE KVSNCQIEAC IDYRDLISHA PNGEWAKMAP
     LRILSFDIEC AGRKGIFPEP NQDPVIQIAN VVTRYGESKP FIRNVFVLDT CSLIVNTQIL
     EFKDESKMLM AWRDFVEKVD PDVIIGYNIA NFDFPYLLDR AKHLKCTNFP YWTRLKGMVS
     QSKETNFSSK QMGNRDTKST NTNGRIQLDM LQLVQRDYHL RSYTLNSVSY EFLGEQKEDV
     HHTMITELYN GTPDSRRRLA VYCLKDAYLP QRLMDKLMCL VNYTEMARVT GVPFNFLLSR
     GQQVKFISQL FRKALEQQLV IPNMKSSDEQ DYEGATVIEP IRGYYGVPIA TLDFASLYPS
     IIQAHNLCYT TLLNKNSVER LKLKKDEDYI VTPNGDMFCT ANVRKGLLSQ ILEELLGARK
     RAKKELAVEK DPFKKAVLNG RQLALKISAN SVYGLTGATV GKLPCLPIAS STTSYGRQMI
     EKTKQEVEAR YTIANGYSHD AKVIYGDTDS VMVKFGVTDL EEAMKLGQEA SEYVSSKFLK
     PIKLEFEKVY FPYLLINKKR YAGLYWTNPK KYDKMDTKGI ETVRRDNCLL VQNVIETVLQ
     RILIDRDIDG AQDYVKDTIS DLLQNKIDMS KLVITKALSK EAYTAKQAHV ELAERMRKRD
     AGSAPTLGDR VAYVIVKGAG GSKNYERSED PIYVLENNIP IDTKYYLDNQ LANPLGRIFE
     PILGEKKASQ LLTGEHTRSI SVASPTMGGL MKFAKKTQTC LGCKKPLSGK EESEGAVCAY
     CRPRLGELYT KSLTKVSDLE VRFGRLWTQC QRCQGSLHCE VICSSRDCPI FYMRMKAKKD
     VEDAQKELSR FDSDAGAW
//
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