UniProt: L0B353

Database: UniProt
Entry: L0B353_THEEQ

LinkDB:  L0B353_THEEQ 
Original site:  L0B353_THEEQ

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (29)   

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ID   L0B353_THEEQ            Unreviewed;      2293 AA.
AC   L0B353;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN   ORFNames=BEWA_010730 {ECO:0000313|EMBL:AFZ81656.1};
OS   Theileria equi strain WA.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=1537102 {ECO:0000313|EMBL:AFZ81656.1, ECO:0000313|Proteomes:UP000031512};
RN   [1] {ECO:0000313|EMBL:AFZ81656.1, ECO:0000313|Proteomes:UP000031512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA {ECO:0000313|EMBL:AFZ81656.1,
RC   ECO:0000313|Proteomes:UP000031512};
RX   PubMed=23137308; DOI=10.1186/1471-2164-13-603;
RA   Kappmeyer L.S., Thiagarajan M., Herndon D.R., Ramsay J.D., Caler E.,
RA   Djikeng A., Gillespie J.J., Lau A.O., Roalson E.H., Silva J.C., Silva M.G.,
RA   Suarez C.E., Ueti M.W., Nene V.M., Mealey R.H., Knowles D.P., Brayton K.A.;
RT   "Comparative genomic analysis and phylogenetic position of Theileria
RT   equi.";
RL   BMC Genomics 13:603-603(2012).
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}.
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DR   EMBL; CP001670; AFZ81656.1; -; Genomic_DNA.
DR   RefSeq; XP_004831322.1; XM_004831265.1.
DR   STRING; 1537102.L0B353; -.
DR   EnsemblProtists; AFZ81656; AFZ81656; BEWA_010730.
DR   GeneID; 15804747; -.
DR   KEGG; beq:BEWA_010730; -.
DR   VEuPathDB; PiroplasmaDB:BEWA_010730; -.
DR   eggNOG; KOG1798; Eukaryota.
DR   OrthoDB; 5475218at2759; -.
DR   Proteomes; UP000031512; Chromosome 3.
DR   GO; GO:0008622; C:epsilon 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:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000031512};
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          1580..1997
FT                   /note="DNA polymerase epsilon catalytic subunit A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01159"
SQ   SEQUENCE   2293 AA;  265495 MW;  B803344712F1A6F4 CRC64;
     MAGYSRSLSW NSNGKRQGFL YNVVPTTVKG SIELNRRVSS DNKPEEHLNL SNFGSSNEFG
     SGHLIGLKSA LSLYFVSDDG SEWHTSIIYA PYFYVSITDP GCVDVTLQFL YNKFKSHSIG
     PVLLEPCTKI DLSLPNHLEK IDPTDGTSKH NIGQLIRIYF STVDQLERGR DLIVGLKRQF
     EKEIALHTDL SSTLGYDPAN ESSVKSAFSE SFLYNDSENS LNLAYQDSWK YKNEHFEGKK
     YNTNPSISNI GDIYEYDIKY VNRVCIDLSI RCGTWYDVER NGYDVKLRQL SITSVAPLNV
     LAWDIECYKA PLKFPDMETD EIILISVVFN GQGYLIVNRS VVAKDILEFS YQPSEDMIGT
     ASFKIFNEAN ELDLLQRFFN LILALKPHIV VTYNGDNFDF PYVSRRSEIN GIPIGKVLGF
     FHSSSGLFTN SAILNMDCYK WVERDSYLPF GSRTLKQVCK LMLKYNPVEI DPEDMVHFAR
     SAPQKLAVYS VSDAVATYFL FIKFIHNFIF ALCSIVPLPP NDTLRQGTGT LCENLLMAEA
     YSNNILFPNK HTQKSIRYYT NPDTDKQHLI YENSYIGGRV ESLRCGIFRD DQAEQFKLNS
     ASYQMLIDTI EETLLYWAKN NIDGDIETLI CDEDVSSSNI DFAPSEKLCR IFSKFENFNE
     VYRDLYTRLC TLRDNPMIKT FPRIYHLDVG AMYPNIIISQ RLQPTAIVTE DFCRKCSYYK
     ESLLCQKKMN WKQRLEISPI DKSQILILAQ DLKGRAYKST NIQYNNTIKD EDTESEEDEI
     ETISKSTNRT WYQLNERERG AELQKAVKLY SQKIFKKSKI NREIDVESII CQRENPFYVQ
     TVSTFRDRRY TYKHLKKEGE NELKQLLREL NPDSVKIKQA REKILINDSL QLAYKCILNS
     FYGYVKRAGS RWYSMEMGAI VTFAGASIID SARKLIENVG IPIELDTDGI WCMLPDIFPA
     VLDLKFGSGE SAGKIKELEY MTTVLNMLIA KKWTNDQYLE LEEIGKYRTT RRNEIAFELD
     GPWHAMFLPA SEKSEELLKK RYVVYNHQNK IVELKGFEIK RRGEMRMIQL FQEDIFPQYL
     LGKTKDDAYK NAAKVALCYR QILDSRAAGL VEDDMFDLLV AKKTVKKPVN QQPALKCFGT
     TSAKRLAELF KNDTYLNDGN LSMSFLLASH PEDAPRTSRA IPIQTFKVDS AVRSQFLSKW
     LKIQLSKANV SSARDILDWD YYKEKLDTQI LKLICLPAIM QGVTNPIPHI DMPKWIKKKQ
     SLAENKQRQI SSFFAKGEIS NQKTSKIDLL KVEHPKKINI NWIQNLKFKW LKTSQNFKRN
     RKKTQYINFQ LHKELKELLP EIRTRTIDFD DLYALFSETW HVYNFSVDEK NPGIINCYLS
     VHNKPLFINV RIEAWRKFYI NNKKKWDVVP NENVIVREIN DQYLLPRGAV QAHLIELEMK
     ENYFLDYIKN SLNSIFHKTV LGVYETQIPI FFDFLTRMGN MVKTGSEDVN TVMNNNMEFQ
     SNKLSPITTM HSGDLKYFSD VEILYVHIFH GTDYETKRHN KFFASIYSKE ENMVNKVFIG
     GSMLLKKYAD EAFTNISEPI LSKHRAKWIE HKSIKHDDYV NPAIFPDCFG AIYDAEFDIS
     DIPITSFRNS LRKLDKFLYN LRPAVSKRKY VVYVYSTLQT SELGDWSKGL YYPVHFEVSN
     SHQIISNTFL KQCFDSSIDL LYQHLCLIEE KLAISQISSI PFGFILSLNK PNMFKCVFDV
     MYARVLRSSS VILWGTRDLS SDLGVPHFSN KTHSDFDIIT NENLNFTVPG IYRGYGVNIT
     FNQSLMYNAI VLESKLDGNI QFNNPNTLKS DEYKCYDEVQ LDSNSHLSLF HPLAFRALGA
     TLENLMKLTN LVFQKVDYGT FQNIVNICSF LKPWLSDAGA ILYDPSLYAM AVMSTQKYLK
     KLIYHFSSVH KLRVIYVTST SIVVDTNTTS ITKGRNKIYE ALEDLSSAHS KFRNIPFHVE
     EEFVAMAQLD NTYYIRYKDY IDASKSNCSE NLKVLEYLPC AVEMFIRYFI KTIALDPLWQ
     SLKKFYMNET TDDKQIGQQE PLELINTDSL DIQEQIEKHI IHDWHQPGTH FSKLYDILSD
     NDSFLRMFDR SGSHSQLNFP ALPGSIFEGK DCWKLETVKL LIYIIQIDRA LDWKNNILNT
     SFEEKIHQLF MLTGESEYVS KNWNPPMRKM EINSITCEKC FMVSDIDVVS GLTYIDDNDG
     NISYQWPCQI CSDPLNSKQI EVKIIQYLEN IFHAQQAQDS ICPDCKTVKT VYRRRGCKCG
     KKYVPRLSKS HWM
//

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