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Database: UniProt
Entry: J4D675_THEOR
LinkDB: J4D675_THEOR
Original site: J4D675_THEOR 
ID   J4D675_THEOR            Unreviewed;      1072 AA.
AC   J4D675;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   03-JUL-2019, entry version 36.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=TOT_010000846 {ECO:0000313|EMBL:BAM39390.1};
OS   Theileria orientalis strain Shintoku.
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM39390.1, ECO:0000313|Proteomes:UP000003786};
RN   [1] {ECO:0000313|EMBL:BAM39390.1, ECO:0000313|Proteomes:UP000003786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shintoku {ECO:0000313|EMBL:BAM39390.1,
RC   ECO:0000313|Proteomes:UP000003786};
RX   PubMed=22951932;
RA   Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA   Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA   Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA   Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA   Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT   "Comparative genome analysis of three eukaryotic parasites with
RT   differing abilities to transform leukocytes reveals key mediators of
RT   Theileria-induced leukocyte transformation.";
RL   MBio 3:e00204-e00212(2012).
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; AP011946; BAM39390.1; -; Genomic_DNA.
DR   RefSeq; XP_009689691.1; XM_009691396.1.
DR   STRING; 68886.XP_009689691.1; -.
DR   EnsemblProtists; BAM39390; BAM39390; TOT_010000846.
DR   GeneID; 20713713; -.
DR   KEGG; tot:TOT_010000846; -.
DR   EuPathDB; PiroplasmaDB:TOT_010000846; -.
DR   KO; K02327; -.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000003786; Chromosome 1.
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   Complete proteome {ECO:0000313|Proteomes:UP000003786};
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:UP000003786};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN       78    445       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      510    941       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN      979   1049       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
SQ   SEQUENCE   1072 AA;  122934 MW;  8EF22E48CE457D83 CRC64;
     MIEIEPENTS FGQYSNFYGT KNDYGTLFRS LKRPDVDYIF FLTDADYTFK NVKYDANGGS
     ERSDQGTEVP IIRLYGVTKQ EQSVLVSLQN FNPYFYIEKP AALLDRHFDD LKELFTRHLS
     EQNQFKRSLR YVLDIQKVRL TSLMLYDENS EKDFLKITVS VPRMVSNLRT FIESGIYLKV
     YDQDRNEVRV AFSRQTYEAN LPYTLRFLLD CNIVSGSWLK IPKGQYTLVE QPSCYKVHPS
     KNGWDRSSTC SIEVVAEYDA VISLPLEGEY EEIGPIKILS FDIECIKLTG TGFPNANYDP
     VIQISSVIYT HGKDINETRN FVFTLKDCDQ LSNAAVLSFE TEDQLLLAWS DFLVQVDPDF
     LTGYNIIVFD LPYLLTRSTV LNIERFKKIT RIRSTSSNFK DAIVSNNMMG TYENKDINIE
     GRIMFDVYDL VRRDHKLKSY TLNYVSFEFL GQQKEDVHYS TISKLQQGTS SDRRRIASYC
     LKDAILPLLL INKLLLVFNY VEMARVTSTP IKFLITRGQQ IRVTMQIYRQ CRKMKYVIPV
     ISSAGRHGSN ENNYEGATVL DPQKGYHTNP IAVLDFQSLY PSIMIAYNLC YSTLVPQNKI
     LNHPEEDVTR IPGYIDLCFV KATKRKGILP IIVENLIEAR RKAKKMMASC QDPMLKKVYD
     GRQLALKVTT NSVYGYTGAA SGGFLPCVDV ATAITSFGRN IILNTKNIIE DHFTVKNGYK
     NDAKVVYGDT DSVMINFGTE DIQEAIDLGN EAASKITSVS VKPITLLFEK VYRPLLLLNK
     KRYAGLYYNN SKTYEKIDCK GIETVRRDFC MLVQQMMERV LYLLLVELNL PAAIEFVKNK
     VSELLRNEID ISLLVVTKSL GKLEYEQRLP HVELAKKLRK RDPGKAPGVG DRISYIIVKG
     TKGEAQYDRA EEPLYVTENN LPIDTNHYLE SIKTTLLRIF DVVMPNPQSL FSGEHTRVIN
     ISSNTGGLMN KFLKKVNRCL SCNTVIQTST FCDNCNQSKK QQVLLDKLKI CRMKEETYFK
     LWTHCQRCQG NLHSAVVCDN RDCPIFYRRV KTSKDLSNLV NTLNTLQIGY ED
//
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