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Database: UniProt
Entry: A0A1L9VX28_ASPGL
LinkDB: A0A1L9VX28_ASPGL
Original site: A0A1L9VX28_ASPGL 
ID   A0A1L9VX28_ASPGL        Unreviewed;      1101 AA.
AC   A0A1L9VX28;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   05-JUN-2019, entry version 14.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=ASPGLDRAFT_117318 {ECO:0000313|EMBL:OJJ88473.1};
OS   Aspergillus glaucus CBS 516.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ88473.1, ECO:0000313|Proteomes:UP000184300};
RN   [1] {ECO:0000313|Proteomes:UP000184300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
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; KV878889; OJJ88473.1; -; Genomic_DNA.
DR   EnsemblFungi; OJJ88473; OJJ88473; ASPGLDRAFT_117318.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000184300; 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:UP000184300};
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:UP000184300};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN      127    471       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      535    965       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1003   1077       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION        1     27       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1L9VX28}.
FT   REGION       39     98       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1L9VX28}.
FT   COMPBIAS     39     60       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1L9VX28}.
FT   COMPBIAS     61     95       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1L9VX28}.
SQ   SEQUENCE   1101 AA;  124547 MW;  03E1169E3D475CA6 CRC64;
     MPEAVKRVLG EATNNLRSPL NTPAAMKKRK LEADAIVKVN SPSQNGQRKA FGSSQPQKSQ
     FEEEVLEKLT QDISGLKDSN SEKDQQWERP PLGKFDPTKE NICFQQIDAE EGTIMGGKTA
     IRLFGVTEVG QSVLLHVTGF QHYLYIAAPV NFTKEDCDPY RAFLETKTGL FQNAIQSVQI
     TMRENIYGFQ GNQKSYYLKI TVTEPRYITK VRSALENGGS SMNYKGLWSS SDSGILTFDN
     IQYLLRFMID TDIAGMAWVE AKAGKYHLFP PNEKLSTCQI EASVDYRDLI SHPPNGEWAK
     MAPLRVLSFD IECAGRKGIF PEPNQDPVIQ IANVVTRYGE SKPFVRNVFV LDTCSLIVNT
     QVLEFDKEEK MLMAWRDFVD KVDPDVIIGY NIANFDFPYL LDRAKHLKCA GFPYWTRLRG
     IQSQARETNF SSKQMGNRDT KSTNTNGRIQ LDLLQLVQRD YHLRSYTLNS VSYEFLGEQK
     EDVHHTMITE LFNGTPDSRR RLAVYCLKDA YLPQRLMDKL MCLVNYTEMA RVTGVPFNFL
     LSRGQQVKFI SQLFRKALEQ QLVIPNAKST DEQDYEGATV IEPVRGYYGV PIATLDFASL
     YPSIIQAHNL CYTTLLNKTS VEKLGLKKDE DYIVTPNGDM FCTIKVRKGL LSQILEELLT
     ARKRAKKELG VETDPFKQAV LNGRQLALKV SANSVYGLTG ATVGKLPCLP IASSTTSYGR
     QMIEKTKQEV EAKYTIANGY SHDAKVIYGD TDSVMVKFGV TELEDAMKLG QEASEYVSSK
     FIKPIKLEFE KVYFPYLLIN KKRYAGLYWT NPKKFDKMDT KGIETVRRDN CLLVQNVIEM
     VLNKILIDRN LDAAQEYVKD TISDLLQNKV DMSKLVITKA LSKSDYTAKQ AHVELAERMR
     KRDAGSAPTL GDRVAYVIVK GAGGSKNYEK SEDPIFVLEN NIPIDTKYYL DNQLANPLGR
     IFEPILGEKK ANQLLTGEHT RSISVAAPTL GGLMKFAKKT QTCMGCKKPL SGKEEMAGAV
     CEHCRPRLGE LYTKTLTKTS DLEVRFGRLW TQCQRCQGSL HCEVICSSRD CPIFYMRMKA
     KKDVEDSQKE LSRFDFDPGA W
//
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