UniProt: A0A251NYS6

Database: UniProt
Entry: A0A251NYS6_PRUPE

LinkDB:  A0A251NYS6_PRUPE 
Original site:  A0A251NYS6_PRUPE

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Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (28)   

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ID   A0A251NYS6_PRUPE        Unreviewed;      1821 AA.
AC   A0A251NYS6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=PRUPE_6G324000 {ECO:0000313|EMBL:ONI04488.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI04488.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONI04488.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=23525075; DOI=10.1038/ng.2586;
RA   Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA   Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA   Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA   Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA   Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA   Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA   Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA   Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA   Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA   Rokhsar D.S.;
RT   "The high-quality draft genome of peach (Prunus persica) identifies unique
RT   patterns of genetic diversity, domestication and genome evolution.";
RL   Nat. Genet. 45:487-494(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; 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|ARBA:ARBA00001966,
CC         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|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; CM007656; ONI04488.1; -; Genomic_DNA.
DR   EnsemblPlants; ONI04488; ONI04488; PRUPE_6G324000.
DR   Gramene; ONI04488; ONI04488; PRUPE_6G324000.
DR   Proteomes; UP000006882; Chromosome g6.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IEA:InterPro.
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:0019985; P:translesion synthesis; IEA:InterPro.
DR   CDD; cd05778; DNA_polB_zeta_exo; 1.
DR   CDD; cd05534; POLBc_zeta; 1.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR   Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR   Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
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; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR45812:SF1; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 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; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU000442};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU000442};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000442};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU000442};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442}; Nucleus {ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          102..221
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          960..1085
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          1226..1674
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1720..1793
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
FT   REGION          512..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          922..944
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..582
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        922..940
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1821 AA;  202592 MW;  1663E0E374C310FE CRC64;
     MAASDAFSVR IVSVDYYMAP PIPGVDISYS SFQGGKVNEV PVIRIFGSTP AGQKTCLHIH
     RALPYLYVPC ADIPIQLHEK GDSYTHDMSL LIEKALKLKG NAGSKRQHVH SCSLVQARKL
     YGYHSSEEVF VKIYLYSPHD VSRAANLLLG SSVLDKCLQP HESHIPFILQ FLVDYNLYGM
     GHLHVSKIKF RHPIPDAFCP RKSVHNGQPS QDIDKSTCMP ADFQADIHGH LSLGSPVWIS
     STIPVDWTWN SPGEFDASSN PDMNCIKRQS ICELEGDATV DEILNQQLKI YTSFSQTRSD
     VKMVQSLIPI WEEYERTGIH EAAIPPDPAK PLPEDTLKTL AGGLEFNNKL IKVHGEAESS
     LCRTQLRKDV RSVEQMTSPK DEGNFVQLQT DNLTDGDIIR SPSTQDFTEE RVSNAKLSLN
     KELPASQVIE TINMKAADNE ALGLLRWLAT SQAADDINSD DELVCETILS PLLPATTIDK
     VLEKANVDYE TESQKECQDI LDSVGDLIDF EGGKEKASYP SDRNHSSKRS SEYVIPRVDG
     CGDDAISTPC DGSSGSFSEI EGKSEFRTSD HQVQDDSSSF NHKHKRKKSL WGSLPLSATQ
     KMKTEGELIK LYRETNKPVG TSSSSEDQVG KRAGIGACDL KESSMLARCS VRDLMRRKRS
     YRIEPPECGS QGIKEVLLGR EENEDTLLCA KRLDFQMSCA DATTFEGLSS KGGVCEMPFE
     NPVGVNAITV ATFLNNEGSG GQKLGVDSVL CGLRNSPFGV IPSDDKGLIE MSFCRKPPVA
     DWNYGESKNA SSLYDDCQDE REIQNKCVRS ESSSHQESVM GVPIHYQTDG SYLYLLTPAT
     TPPSAKNVCR WLSSDEKGSS RNLTGLQSYL PNDWEKSSPE CGSIDDVLPI LHQGSQENHG
     NHETERTEIV QREGDAVKVQ TCSEYSQDSS QISGPDGRSK PTPLSQIGFR DPASVGGGQQ
     LTLLSVEVQA ESRGDLRPDP RFDAINLISL AIQNDSDSIV EIFVLLHSKA ESSQRILDGI
     SGCKVLVFYE EKYLFDHFIK TVCSLDPDVL MGWDIQGGSL GFLAERASLF GIGLLNKISR
     VPSETKMEAE DLEIPEKAIQ EKMIHEAVIA DPVVLDPIVE DEWGRTHASG VHVGGRIVLN
     VWRLMRGEVK LNIYTVEAVA QAVLRRKVPY ILNKVLTKWF LSGPGRARYR CIEYLNERAK
     LSLEIMNQLD MINRTSELAR VFGIDFFSVL SRGSQYRVES MFLRLAHAQN YVAISPGPKQ
     VASQPAMECL PLVMEPESGF YADPVVVLDF QSLYPSMIIA YNLCYSTCLG KVVPSEANTL
     GVSSFSPDPH DLHNLKDQIL LTPNGVMYVP EKVRKGVLPR LLEEILSTRI MVKQAMKKLS
     SSEQVLHRIF NARQLALKLI SNVTYGYTAA GFSGRMPCAE IADSIVQCGR STLEKAISYV
     NAHGKWNARV IYGDTDSMFV LLKGRSIEDS FQIGHEIASE ITAMNPNPIA LKMEKVYSSC
     FLLTKKRYVG YSYESPEQTE PIFDAKGIET VRRDTCGAVA KTMEQSLRLF FEHQDMYEVR
     AYLQRQWKRI LSGRVSLQDF VFAKEVRLGT YRASAFSSLP PAAIVATKAM RTDPRAEPRY
     AERVPYVVIH GEPGARLVDL VVDPLILLAI DSPYRLNDLY YIHKQIIPAL QRVFGLLGAD
     LSQWFSDMPR PAREAFGKRL FYASNPHRTR IDYYYLSRHC ILCGELVQAS AHLCNQCCEN
     KSFAAVAVTG RTSKLEREMQ QLAGICRHCG GGDWVVESGI KCTSLACSVF YERRKVQKEL
     QGLASVAAET GFYPKCMVEW F
//

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