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Database: UniProt
Entry: A0A0D1E3V2_USTMA
LinkDB: A0A0D1E3V2_USTMA
Original site: A0A0D1E3V2_USTMA 
ID   A0A0D1E3V2_USTMA        Unreviewed;      1678 AA.
AC   A0A0D1E3V2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   05-JUN-2019, entry version 30.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=UMAG_01931 {ECO:0000313|EMBL:KIS70779.1};
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS70779.1, ECO:0000313|Proteomes:UP000000561};
RN   [1] {ECO:0000313|EMBL:KIS70779.1, ECO:0000313|Proteomes:UP000000561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H.,
RA   Wosten H.A., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbrugge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C.,
RA   Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Munch K.,
RA   Rossel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U.,
RA   Sandrock B., Meng S., Ho E.C., Cahill M.J., Boyce K.J., Klose J.,
RA   Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W.,
RA   Sanchez-Alonso P., Schreier P.H., Hauser-Hahn I., Vaupel M.,
RA   Koopmann E., Friedrich G., Voss H., Schluter T., Margolis J.,
RA   Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G.,
RA   Guldener U., Munsterkotter M., Haase D., Oesterheld M., Mewes H.W.,
RA   Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S., Jaffe D.B.,
RA   Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen
RT   Ustilago maydis.";
RL   Nature 444:97-101(2006).
RN   [2] {ECO:0000313|Proteomes:UP000000561}
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G.,
RA   Kahmann R.;
RL   Submitted (SEP-2014) 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; CM003142; KIS70779.1; -; Genomic_DNA.
DR   RefSeq; XP_011387851.1; XM_011389549.1.
DR   STRING; 5270.UM01931P0; -.
DR   EnsemblFungi; KIS70779; KIS70779; UMAG_01931.
DR   GeneID; 23562797; -.
DR   KEGG; uma:UMAG_01931; -.
DR   EuPathDB; FungiDB:UMAG_01931; -.
DR   KO; K02350; -.
DR   OMA; AHIHGAF; -.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000000561; Chromosome 3.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IBA:GO_Central.
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:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000561};
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:UP000000561};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN       79    217       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      781    977       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN     1044   1490       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1563   1632       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION        1     29       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0D1E3V2}.
FT   REGION      321    347       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0D1E3V2}.
FT   REGION      434    455       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0D1E3V2}.
FT   REGION      476    607       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0D1E3V2}.
FT   REGION      620    641       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0D1E3V2}.
FT   COILED      755    775       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS      1     28       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0D1E3V2}.
FT   COMPBIAS    321    340       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0D1E3V2}.
FT   COMPBIAS    434    450       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0D1E3V2}.
FT   COMPBIAS    519    541       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0D1E3V2}.
FT   COMPBIAS    568    588       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0D1E3V2}.
FT   COMPBIAS    589    607       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0D1E3V2}.
FT   COMPBIAS    624    641       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0D1E3V2}.
SQ   SEQUENCE   1678 AA;  189539 MW;  0C10E55B7C0EB1A7 CRC64;
     MTSLESAEQS DPSAQQTAQQ TEKIDSASAS SDPFFRVRLI NIDHILTVPT PFDRTSCAFN
     AEGQPLRKVP VLRLFGATPA GQRVCLYIHN VYPYCYIQYK GSLDPDNVLR YIHRLGRGLN
     AAMAASLRRN LHDTDANQFI AAIHLCKGVN FYGYHVGYSY YLKISFVDPA HNYRIAAILE
     SGGVMKTVFQ PFEIHIRYQL QFMLDYNIFG CDYVDLDDIR FRLPIPEGNL VANDDLSPLD
     SRSKIWNRNS IPYAHVQAPD VHRGSYCELE ADASAPWIIN RRRFKQRDIH SNFDETSTTP
     SDQDILVPSL SGLWEDEMKR RKAAGLPPSI PREDPARDPR LYASGDSPTW MSEERMRLLL
     EKRLIEEKQK TLPRERNASH FTDRPGLDEY IMTTFDAVEV FHPYQDQIHA ADPYSQRTGP
     SASSRLYDLQ HAISQTQQSP PDQMEPTQLT QQLKEEEDDF DDEFFQSQDF NHRLQSAEKE
     AMSANQDPPS DQEDDANDAD QVEPAWAQPD GPGTPCKWHR TESSHSNSNT ASSSTFSKSP
     SSTPKRRHHA DVLGSDKTTS TASPSSKPSK EVHEDSVRRF KKAKHEHSTA STNATSGSRS
     GHAINSVRST KVRFVEAGSS APAARLRQQE TSSLQHSSAS RTRFLTFHES APSLRDVVGT
     FPLFSIARQI HPEPFFSNPS DLPARPREYA GRMFHFQSHS LPYLRSFDHW DQKSEHVAST
     QKDKPPKRLY WQFGPPPPTL LEARAWRQKE KVIERQRSKR RRARLLSQIE RLTQANDFGF
     KISQHKATAL VKRDKQHMTT LAVEVMTTTR DSLFPDPALD AIQSIVYSFQ NEDENLQDTG
     SRPDLRTGLI IVSGDEINFD RLGLSHLAVE VVEDELELFN TLIDLVRAFD PEILVGWEIH
     SSSWGYIVER ASKEYDYDLV PQIGRAIIHN TGRAGGKSDN YAYTQSSALR FTGRHTLNLW
     RLMKGELTLN LYTLENVCYH LLHRRIPKYS HQTLTQWYKS GRAELIRRAL LYYVDMVELE
     LEIIAESEFV LRTAEFARIY GIDFFSVISR GSQFKVESIM LRIAKPENFV LISPSRAQVG
     KQNAAECLPL IMEPQSAFYK GPLIVLDFQS LYPSIMIAYN LCYSTCLGRV AGFKGTSKFG
     VTEYAPPKGL LSLLQDDVNI SSNGLLFVKP SVRKSLLAKM LSEILDTRVM VKSSMKATKS
     DKSFQRIQNA RQISLKLLAN VTYGYTSASF SGRMPCVEIA DAIVQTGRET LEKAMDLING
     TEEWGAQVVY GDTDSLFVYL PGRTKEEAFT LGNVIADKVT SLNPRPVKLK FEKVYLPSVL
     LAKKRYVGFK YETLDEREPG FDAKGIETVR RDFHPAIQRM LEACIRILFR SRDLSLVKSY
     LQRQWRKILE GRVSAQDFIF AKEVRLGSYS DKVAPPPGAA VASRRMLADP RSEPQYGERV
     PYIISQGEPR AKLNQQAVSP EAFLKDPQLQ INALYYITRT IIPPLARVFN LLGADVEAWF
     HHMPKPNNAY WNKRPTAALL SALLAQQDPS SSTHEIGSDS AASKATSSTA IATLNSHYAT
     ETCLLCSSRT EALVCLDCRQ SPLESIHATS SKLHKLEAQV AAIDSICSTC AHMERPGPVD
     CVSFDCPYTY QKTKVHKSLQ DTALVHTYIS RLFDSEPQRQ AVVDDAWTGT KNLNDGIS
//
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