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Thymine dioxygenase JBP1 (EC 1.14.11.6) (J-binding protein 1) (Thymidine hydroxylase JBP1)

 JBP1_TRYB2              Reviewed;         839 AA.
P86938; Q382H3; Q9U6M3;
27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 1.
12-SEP-2018, entry version 26.
RecName: Full=Thymine dioxygenase JBP1;
EC=1.14.11.6;
AltName: Full=J-binding protein 1;
AltName: Full=Thymidine hydroxylase JBP1;
Name=JBP1; ORFNames=Tb11.01.5220;
Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma.
NCBI_TaxID=185431;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
PubMed=16020726; DOI=10.1126/science.1112642;
Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B.,
Bohme U., Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L.,
Wickstead B., Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J.,
Bringaud F., Brooks K., Carrington M., Cherevach I.,
Chillingworth T.J., Churcher C., Clark L.N., Corton C.H., Cronin A.,
Davies R.M., Doggett J., Djikeng A., Feldblyum T., Field M.C.,
Fraser A., Goodhead I., Hance Z., Harper D., Harris B.R., Hauser H.,
Hostetler J., Ivens A., Jagels K., Johnson D., Johnson J., Jones K.,
Kerhornou A.X., Koo H., Larke N., Landfear S., Larkin C., Leech V.,
Line A., Lord A., Macleod A., Mooney P.J., Moule S., Martin D.M.,
Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E.,
Rajandream M.A., Reitter C., Salzberg S.L., Sanders M., Schobel S.,
Sharp S., Simmonds M., Simpson A.J., Tallon L., Turner C.M., Tait A.,
Tivey A.R., Van Aken S., Walker D., Wanless D., Wang S., White B.,
White O., Whitehead S., Woodward J., Wortman J., Adams M.D.,
Embley T.M., Gull K., Ullu E., Barry J.D., Fairlamb A.H.,
Opperdoes F., Barrell B.G., Donelson J.E., Hall N., Fraser C.M.,
Melville S.E., El-Sayed N.M.A.;
"The genome of the African trypanosome Trypanosoma brucei.";
Science 309:416-422(2005).
[2]
DISRUPTION PHENOTYPE.
PubMed=12366829; DOI=10.1046/j.1365-2958.2002.03144.x;
Cross M., Kieft R., Sabatini R., Dirks-Mulder A., Chaves I., Borst P.;
"J-binding protein increases the level and retention of the unusual
base J in trypanosome DNA.";
Mol. Microbiol. 46:37-47(2002).
[3]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND DEVELOPMENTAL STAGE.
STRAIN=29-13, and 427;
PubMed=15694344; DOI=10.1016/j.molcel.2004.12.022;
DiPaolo C., Kieft R., Cross M., Sabatini R.;
"Regulation of trypanosome DNA glycosylation by a SWI2/SNF2-like
protein.";
Mol. Cell 17:441-451(2005).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-213 AND
ASP-215.
PubMed=17389644; DOI=10.1093/nar/gkm049;
Yu Z., Genest P.-A., ter Riet B., Sweeney K., DiPaolo C., Kieft R.,
Christodoulou E., Perrakis A., Simmons J.M., Hausinger R.P.,
van Luenen H.G.A.M., Rigden D.J., Sabatini R., Borst P.;
"The protein that binds to DNA base J in trypanosomatids has features
of a thymidine hydroxylase.";
Nucleic Acids Res. 35:2107-2115(2007).
[5]
DISRUPTION PHENOTYPE.
STRAIN=29-13, and 427;
PubMed=19136460; DOI=10.1093/nar/gkn1067;
Cliffe L.J., Kieft R., Southern T., Birkeland S.R., Marshall M.,
Sweeney K., Sabatini R.;
"JBP1 and JBP2 are two distinct thymidine hydroxylases involved in J
biosynthesis in genomic DNA of African trypanosomes.";
Nucleic Acids Res. 37:1452-1462(2009).
-!- FUNCTION: Dioxygenase that catalyzes the first step of DNA base J
(beta-d-glucosyl-HOMedU) biosynthesis by converting thymine to 5-
hydroxymethyluracil (HOMedU). DNA base J is a hypermodified
thymidine residue found in the genome of kinetoplastid parasites,
which is localized primarily to repetitive DNA, namely the
telomeres, and is implicated in the regulation of antigenic
variation. Also specifically binds to base J-containing DNA (J-
DNA). Involved in propagation and maintenance of DNA base J
synthesis initiated by JBP2 by specifically binding already
synthesized DNA base J and propagating J synthesis. Thymine
dioxygenase activity and J-DNA-binding are independent functions.
{ECO:0000269|PubMed:15694344, ECO:0000269|PubMed:17389644}.
-!- CATALYTIC ACTIVITY: Thymine + 2-oxoglutarate + O(2) = 5-
hydroxymethyluracil + succinate + CO(2).
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Note=Binds 1 Fe(2+) ion per subunit.;
-!- SUBUNIT: Monomer. Binds to DNA as a monomer (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15694344,
ECO:0000269|PubMed:17389644}.
-!- DEVELOPMENTAL STAGE: Expressed in bloodstream form and
significantly less in procyclic form.
{ECO:0000269|PubMed:15694344}.
-!- DOMAIN: The DNA-binding JBP1 domain (DB-JBP1) is necessary and
sufficient for binding to J-DNA. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Does not affect growth, gene expression or
the stability of some repetitive DNA sequences. The genome
contains only about 5% of the wild-type level of J in their DNA.
Cells lacking both JBP1 and JBP2 show a complete absence of base
J. {ECO:0000269|PubMed:12366829, ECO:0000269|PubMed:19136460}.
-!- SIMILARITY: Belongs to the TET family. JBP1 subfamily.
{ECO:0000305}.
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EMBL; CH464491; EAN80308.1; -; Genomic_DNA.
RefSeq; XP_829420.1; XM_824327.1.
SMR; P86938; -.
STRING; 5691.EAN80308; -.
PaxDb; P86938; -.
PRIDE; P86938; -.
GeneDB; Tb927.11.13640:pep; -.
GeneID; 3665128; -.
KEGG; tbr:Tb11.01.5220; -.
EuPathDB; TriTrypDB:Tb927.11.13640; -.
HOGENOM; HOG000113125; -.
InParanoid; P86938; -.
KO; K22406; -.
Proteomes; UP000008524; Chromosome 11 Scaffold 1.
GO; GO:0005634; C:nucleus; IDA:GeneDB.
GO; GO:0003677; F:DNA binding; IDA:GeneDB.
GO; GO:0008198; F:ferrous iron binding; IMP:GeneDB.
GO; GO:0050341; F:thymine dioxygenase activity; ISO:GeneDB.
GO; GO:0070580; P:base J metabolic process; IMP:GeneDB.
GO; GO:0016458; P:gene silencing; TAS:GeneDB.
InterPro; IPR024779; 2OGFeDO_noxygenase_dom.
Pfam; PF12851; Tet_JBP; 1.
1: Evidence at protein level;
Complete proteome; Dioxygenase; DNA-binding; Iron; Metal-binding;
Nucleus; Oxidoreductase; Reference proteome.
CHAIN 1 839 Thymine dioxygenase JBP1.
/FTId=PRO_0000377555.
REGION 86 288 Thymine dioxygenase. {ECO:0000250}.
REGION 415 583 DNA-binding JBP1 domain. {ECO:0000250}.
METAL 213 213 Iron; catalytic.
METAL 215 215 Iron; catalytic.
METAL 263 263 Iron; catalytic. {ECO:0000250}.
BINDING 279 279 2-oxoglutarate. {ECO:0000250}.
SITE 548 548 Involved in J base recognition,
conferring specificity towards J-DNA.
{ECO:0000250}.
MUTAGEN 213 213 H->S: Impairs DNA base J biosynthesis.
{ECO:0000269|PubMed:17389644}.
MUTAGEN 215 215 D->S: Impairs DNA base J biosynthesis.
{ECO:0000269|PubMed:17389644}.
SEQUENCE 839 AA; 95251 MW; B3BEECD851CC0FE7 CRC64;
MRRQVKKVLR EKADDSMKPG WDVYQPSNDV VYAFNHYMQG SQIDAEAREK AEKAFQEAVK
KHPFHNNADH TVDFHGTTVF RNAKGKVCGV LIPKALPSFA TSMAADVLEC AVARTSLRSA
LFGGVSPNSG IAGYFDYRGT PVELKCRKTS FTYEHTKEWR SVFPMIDYTS AIYKAALPDH
WKAQDAAVPD VVRIHGSPFS TLTVNERFRT ASHTDNGDFD NGYGVLAVLK GEYSGLSLAL
DDYGVCFNMQ PTDVLLFDTH LFHSNTELEA KEANATWNRL SCVFYYRAAL GEQPCVEEYR
RRLKKAKEEK STSLSFNHIE QKDNGENTNK PAPVYPVSLT PFSCAASAWA LRGCAAAMLT
RLHGLVRENA SLMTELFGEP VEVADGLPRR APEEIIPVHK HTNVQMHYLG GFSEKGDILN
EAMNKRHYLD KENLQKMFGE EFVNIWTQSR THWLQLVKKE WEHQKETNPT RTRFSWNNTS
AMNFAFFDLC DVAKQLMCGA FGDREVNKKE EQSFWGMFAA HLDNACINEI GMLQGSMGMH
KLNVKLKDYN FGGTRYLKDM PPEEQERRRR RRLEIEQARR RAPICDSESG DWLRNEAFDY
QTEDVAVNYE REQWITPENN AKRFGFPERG VYGAEGAATG TISVLIVLPK PTNHRQKTCE
LPTSREADRI MKNPAAQRLL CAKPCNIGLS TSSNKSRTVL CGNIRIDKVF DGGSVGGKMY
DFVIMRHLLA ATTGEREPLE CLVRWTSLAR YCTFVVEVDL LDRHHYILKS EIGEEYSAVS
EICFSALYSA TYARDKVNLR TTPCLLSFID KSGNMLESRF KFNGSPLNTV AFVVRRREK


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