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Database: UniProt
Entry: B2B7A7_PODAN
LinkDB: B2B7A7_PODAN
Original site: B2B7A7_PODAN 
ID   B2B7A7_PODAN            Unreviewed;      1108 AA.
AC   B2B7A7;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   05-JUN-2019, entry version 78.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=PODANS_2_10460 {ECO:0000313|EMBL:CAP73685.1};
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Lasiosphaeriaceae;
OC   Podospora.
OX   NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP73685.1};
RN   [1] {ECO:0000313|EMBL:CAP73685.1, ECO:0000313|Proteomes:UP000001197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC   {ECO:0000313|EMBL:CAP73685.1};
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O.,
RA   Porcel B.M., Couloux A., Aury J.-M., Segurens B., Poulain J.,
RA   Anthouard V., Grossetete S., Khalili H., Coppin E.,
RA   Dequard-Chablat M., Picard M., Contamine V., Arnaise S., Bourdais A.,
RA   Berteaux-Lecellier V., Gautheret D., de Vries R.P., Battaglia E.,
RA   Coutinho P.M., Danchin E.G.J., Henrissat B., El Khoury R.,
RA   Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora
RT   anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2] {ECO:0000313|EMBL:CAP73685.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP73685.1};
RA   Genoscope - CEA;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000001197}
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197};
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E.,
RA   Benkhali J.A., Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and
RT   its role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
RN   [4] {ECO:0000313|EMBL:CDP26087.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:CDP26087.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA   Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and
RT   its role in heterokaryosis in Podospora anserina.";
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; CU640366; CAP73685.1; -; Genomic_DNA.
DR   EMBL; FO904937; CDP26087.1; -; Genomic_DNA.
DR   RefSeq; XP_001911857.1; XM_001911822.1.
DR   STRING; 5145.XP_001911857.1; -.
DR   EnsemblFungi; CAP73685; CAP73685; PODANS_2_10460.
DR   GeneID; 6196216; -.
DR   KEGG; pan:PODANSg8902; -.
DR   eggNOG; KOG0969; Eukaryota.
DR   eggNOG; COG0417; LUCA.
DR   KO; K02327; -.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000001197; Chromosome 2.
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:UP000001197};
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:UP000001197};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN      134    476       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      540    971       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1009   1083       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION        1     67       Disordered. {ECO:0000256|MobiDB-lite:
FT                                B2B7A7}.
FT   COILED       72     92       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS      1     30       Polar. {ECO:0000256|MobiDB-lite:B2B7A7}.
FT   COMPBIAS     42     67       Polar. {ECO:0000256|MobiDB-lite:B2B7A7}.
SQ   SEQUENCE   1108 AA;  125632 MW;  F8BC325719B031D8 CRC64;
     MPSATLPQKR AFGEASSTRR NIAATPSTAT TKKRRIDEPT SSPAQRFKSS QNDSKGRMAS
     SQQKSVFESE VLERLNQDIS DLKQNNSEKD QAWERPPIPN DFDPSKQSLC FQAIEAEEGT
     IGGGQPAVKL FGVTENGNSV LLHVKDFKHY LYVAAPVSFV VEDCLAFKAY LESQMSQNHQ
     YQQVIHNVSL TMRENIYGFQ GNVQNPYIKV TVTDPKHINK VRTMIERGEA NWKGMWKHDG
     GIMTYDSIQY LLRFMVDCSI AGMSWVEAPA GAYDLIHMNK QSNCQFEAVI SYRELISHKP
     SGEWSKMAPL RILSFDIECA GRKGIFPEAQ HDSVIQIANI VTKYGDKKPF VRNVFCLDTT
     SPIVATQILE FKDEGKMLAA WRDFLEKVDP DIIIGYNIAN FDFPYLLDRA KHLKVHNFEY
     WSRTHVKSVA KETNFSSKQM GNRDTKATNT NGRLQLDLLQ LVQRDHQLRS YTLNSVCAHF
     LGEQKEDVHH SMITELFEGT PESRRRLALY CLKDAYLPQR LMDKLSCLEN YTEMARVTGV
     PFNFLLARGQ QVKFLSQLFR KALEQKLVIP NMRSESSEEQ YEGATVIEPT RGYYDVPIAT
     LDFASLYPSI IQAHNLCYTT LIKKKDIERW SLVKDEDYIV TPNGDMFVTT KKRKGLLAQI
     LEELLSARKE AKRELAAETD PFKKAVLNGR QLALKISANS VYGLTGATNG KLPCLEIASS
     TTAFGRQMIE RTKHEVEERY CIKNGYSHDA QVIYGDTDSV MVKFGTKELA EAMKLGEDAA
     NYVSSKFIKP IKLEFEKVYF PYLLINKKRY AGLYWTKPEK YDKMDTKGIE TVRRDNCLLV
     QTVIEKVLRM ILIDRDVPGA QEYVKDTIAD LLQNRVDMSK LVITKALTKD DYAAKQAHVE
     LAHRMKKRDA GSAPALGDRV AYVMVKGATG SKNFERSEDP IYVLEHNVPI DTKYYLDNQL
     AKPLGRIFEP ILGETKAKSL LTGDHTRAIS VAAPKVGGLM KFAKKTQTCM GCKKPLTGKE
     ESRGAVCADD APRVGELYKK TLDKVSDLEV RFGRLWTQCQ RCQGSMHCEV ICSSKDCPIF
     YMRMKAKKDL EDANGELARF DFDQAAIW
//
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