UniProt: A0A2J6LTJ2

Database: UniProt
Entry: A0A2J6LTJ2_LACSA

LinkDB:  A0A2J6LTJ2_LACSA 
Original site:  A0A2J6LTJ2_LACSA

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Ontology (12)   
   GO (12)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (30)   

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ID   A0A2J6LTJ2_LACSA        Unreviewed;      2178 AA.
AC   A0A2J6LTJ2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN   ORFNames=LSAT_6X39380 {ECO:0000313|EMBL:PLY90544.1};
OS   Lactuca sativa (Garden lettuce).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC   Lactucinae; Lactuca.
OX   NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY90544.1};
RN   [1] {ECO:0000313|EMBL:PLY90544.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28401891; DOI=10.1038/ncomms14953;
RA   Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA   Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA   Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT   "Genome assembly with in vitro proximity ligation data and whole-genome
RT   triplication in lettuce.";
RL   Nat. Commun. 8:14953-14953(2017).
CC   -!- FUNCTION: DNA polymerase II participates in chromosomal DNA
CC       replication. {ECO:0000256|RuleBase:RU365029}.
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:RU365029};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966,
CC         ECO:0000256|RuleBase:RU365029};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365029}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU365029}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PLY90544.1}.
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DR   EMBL; NBSK01002337; PLY90544.1; -; Genomic_DNA.
DR   STRING; 4236.A0A2J6LTJ2; -.
DR   EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_6X39380_mrna; cds-PLY90544.1; gene-LSAT_6X39380.
DR   Gramene; rna-gnl|WGS:NBSK|LSAT_6X39380_mrna; cds-PLY90544.1; gene-LSAT_6X39380.
DR   GO; GO:0008622; C:epsilon 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; IBA:GO_Central.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008310; F:single-stranded DNA 3'-5' DNA exonuclease activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006287; P:base-excision repair, gap-filling; IBA:GO_Central.
DR   GO; GO:0045004; P:DNA replication proofreading; IBA:GO_Central.
DR   GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
DR   CDD; cd05779; DNA_polB_epsilon_exo; 1.
DR   CDD; cd05535; POLBc_epsilon; 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; 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; 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; IPR013697; DNA_pol_e_suA_C.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR029703; POL2.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10670:SF0; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT 1; 1.
DR   PANTHER; PTHR10670; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   Pfam; PF08490; DUF1744; 1.
DR   SMART; SM01159; DUF1744; 1.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU365029};
KW   DNA replication {ECO:0000256|RuleBase:RU365029};
KW   DNA-binding {ECO:0000256|RuleBase:RU365029};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU365029};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU365029};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU365029};
KW   Metal-binding {ECO:0000256|RuleBase:RU365029};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU365029};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365029};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365029};
KW   Zinc {ECO:0000256|RuleBase:RU365029};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU365029}.
FT   DOMAIN          1484..1869
FT                   /note="DNA polymerase epsilon catalytic subunit A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01159"
FT   REGION          1139..1203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1140..1168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1170..1190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2178 AA;  250220 MW;  5C7F9B7C71E1A935 CRC64;
     MNGDNRRRAD RKDTRISKKQ KLILSTEEKL ETKLGFDLFT EGEKRLGWLL TFSTSSWEDQ
     DTQREYSCVD LYFVCQDGST FKAKYKFRPY FYAATKDKME MDVDAYLRRR YEGKIADIQI
     VEKEDLDLKN HLSGLRKTYL KISFDTVQQL MDVKRDLMHV VERNQEKFNA SEAYESIMSG
     KSKERIQDFI DCISDLREYD VPYHVRFAID NDVRSGLWYD VSVSSDGIKL ERRHDLLQRA
     EVHVCAFDIE TTKLPLKFPD AEYDLVMMIS YMVDGKGYLI INRECVGEDI EDLEYTPKAE
     FEGYFKVTNV KNEEELIKSW FAHMAEVKPG IYVTYNGDFF DWPFMERRAA HHGLIMKDEL
     GFQCDTVQGE CRAKFACHLD CFAWVKRDSY LPQGSHGLKA VTKAKLGYDP LEVNPEDMVR
     FAMEKPQMMA SYSVSDAVST YYLYMTYVHP FIFSLATIIP MPPDEVLRKG SGTLCEMLLM
     VEAYVANVVC PNKHQSEAEK FHNGRLLESE TYIGGHVECL ETGVFRSDLP TSFKLDSSAF
     TQLIENLDRD LQYAIKVEGK MDIETVSNYD EVKDAITEKL ASLRDEPTRE ECPLIYHLDV
     AAMYPNIILT NRLQPPSIVT DEVCTACDFN RPGKTCLRKL EWKWRGETYT AKRSDYYHLK
     RQIESEVVAV DGFKSKSFLE LPKVDQQLKL KDRLKKYCQK AYKRVLEKPT TETREAGICM
     RENAFYVDTL SEAKASGNPI KIQEAQDMVV LYDSLQLAHK CILNSFYGYV MRKGARWYSM
     EMAGVVTYTG AKIIQNAHEL VKKIGKPLEL DTDGIWCVLP GSFPENFTFK FRDSKKKFTI
     SYPCVMLNVD VARNNTNDQY QTLKDPINRT YTTHSECSIE FEVDGPYKAM ILPASKEENK
     LIKKRYAVFN DDGTLAELKG FEIKRRGELK LIKVFQAELF DKFLHGSTLE ECYSAVASVA
     NRWLDLLDNQ GNDIADSELL DYISESSTMS KSLVDYGVQK SCAVTTAKRL ADFLGDTMVK
     DKGLRCQYVV ACEPKGTPVS ERAVPVAIFE TDPEIMKFYV KKWCKISSDI GIRSIIDWEY
     YKQRLSSAIQ KTITIPAAMQ KVSNPVPRVV HPPWLHKKVR EKDDKMRQRK LNVMFSSMKK
     ANEEEVRNDT NGKEHVLQEQ EVVDLEDFGS KGKSSNSTPR PVVRSYENNG KTSSSKEKVD
     HGQSMNPVVD IPVEDNIDSH VDYQGWLNQR KRKWKQVREK KKKQKLDSLD KNTQRNGVTE
     IRSGVSNKKQ AQGRTGVNSY FERHELALTR SHWQIIQLVP SSELGQFFAW AVVDGMMHKI
     GIKVPRVFYL NSKAPVTEDF PGRRVNKILP HGHHSHNLIE VIVDEDQFKT ESRKLAAHLA
     DPEVEGIYET KVGLDFSSIL QIGCVCKVDK SAKKRNAKEG WNLSELHMKT TTECSYLESP
     IPFFYLYHSI SEVRGIYVVY FPSSSVIHAV IVNPFQNKEL TPNILDKQFR EACQALSVES
     SMSRGSSNFK VEYVGTPKDA ERIFQRTISE FRDEVHGPAI GVIECPDVKL MKLSIRALDD
     FPCVSIPSNA RDCHYPTLAW QSFAAKIGMQ RCAASPRWLN ERISLSRYSH IPLGNFELDW
     LMHTADIFFA RALRDHQQIL WVSDNGIPDL GGDTEEETCY SDEVNQPVLI YPGAYRKVTV
     ELKIHHLAVN ALLKSNQINE MEGGTLFGFD HDLTSGSHLP NEQLGLDEAT SCSSAFRVLK
     QLIQRCLADA VSSGNIFADA MLQHLYRWLC SPRSALHDPA LHRMLHKVMQ KVFALLLSEF
     RKLGATIIFA NFSKVILDTG KSDLFAAQAY CDSLLKALQE RDLFEWIELE PMQFWHSLLF
     MDQYNYGGLQ AKLDQTDDNT YDEPQVELVS SWNIAENLPK ETQDHFVFIV TEFMHLPWKF
     TQDETMKRAA IRNSDSCTPS ITAAAAESFE SCITEHLREQ VNSYFTDRLL KIVRDLVLHT
     KGKGKSKEDE DNVYKGDPAL EFIKHVCAVL VLDQNVQHDI LIMRKNLLRY VRVREFAPEA
     QFQDCSFSFT LPNVICSYCN DCRDLDLCRD RGLLTQEWRC GVPQCGQPYN REVMENALLQ
     IVRQRERLYH LQDLVCLKCK QIKAAHLAEY CGCAGSFCLK EEVTVFMKKM EVFLNIGIHQ
     KFELLVECVS WILELKQV
//

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