ID   JBP1_TRYBB              Reviewed;         839 AA.
AC   P86937; Q382H3; Q9U6M3;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Thymine dioxygenase JBP1;
DE            EC=1.14.11.6 {ECO:0000250|UniProtKB:Q9U6M1};
DE   AltName: Full=J-binding protein 1;
DE   AltName: Full=Thymidine hydroxylase JBP1;
GN   Name=JBP1;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DNA-BINDING.
RC   STRAIN=427;
RX   PubMed=10562569; DOI=10.1093/emboj/18.22.6573;
RA   Cross M., Kieft R., Sabatini R., Wilm M., de Kort M., van der Marel G.A.,
RA   van Boom J.H., van Leeuwen F., Borst P.;
RT   "The modified base J is the target for a novel DNA-binding protein in
RT   kinetoplastid protozoans.";
RL   EMBO J. 18:6573-6581(1999).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND DEVELOPMENTAL STAGE.
RC   STRAIN=29-13, and 427;
RX   PubMed=15694344; DOI=10.1016/j.molcel.2004.12.022;
RA   DiPaolo C., Kieft R., Cross M., Sabatini R.;
RT   "Regulation of trypanosome DNA glycosylation by a SWI2/SNF2-like protein.";
RL   Mol. Cell 17:441-451(2005).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=29-13, and 427;
RX   PubMed=19136460; DOI=10.1093/nar/gkn1067;
RA   Cliffe L.J., Kieft R., Southern T., Birkeland S.R., Marshall M.,
RA   Sweeney K., Sabatini R.;
RT   "JBP1 and JBP2 are two distinct thymidine hydroxylases involved in J
RT   biosynthesis in genomic DNA of African trypanosomes.";
RL   Nucleic Acids Res. 37:1452-1462(2009).
CC   -!- FUNCTION: Dioxygenase that catalyzes the first step of DNA base J
CC       (beta-d-glucosyl-HOMedU) biosynthesis by converting thymine to 5-
CC       hydroxymethyluracil (HOMedU). DNA base J is a hypermodified thymidine
CC       residue found in the genome of kinetoplastid parasites, which is
CC       localized primarily to repetitive DNA, namely the telomeres, and is
CC       implicated in the regulation of antigenic variation. Also specifically
CC       binds to base J-containing DNA (J-DNA). Involved in propagation and
CC       maintenance of DNA base J synthesis initiated by JBP2 by specifically
CC       binding already synthesized DNA base J and propagating J synthesis.
CC       Thymine dioxygenase activity and J-DNA-binding are independent
CC       functions. {ECO:0000269|PubMed:15694344}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + O2 + thymine = 5-hydroxymethyluracil + CO2 +
CC         succinate; Xref=Rhea:RHEA:10316, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16964,
CC         ChEBI:CHEBI:17821, ChEBI:CHEBI:30031; EC=1.14.11.6;
CC         Evidence={ECO:0000250|UniProtKB:Q9U6M1};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q6N021};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6N021};
CC   -!- SUBUNIT: Monomer. Binds to DNA as a monomer (By similarity).
CC       {ECO:0000250|UniProtKB:Q9U6M1}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15694344}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in bloodstream form and significantly
CC       less in procyclic form. {ECO:0000269|PubMed:15694344}.
CC   -!- DOMAIN: The DNA-binding JBP1 domain (DB-JBP1) is necessary and
CC       sufficient for binding to J-DNA. {ECO:0000250|UniProtKB:Q9U6M1}.
CC   -!- DISRUPTION PHENOTYPE: Does not affect growth, gene expression or the
CC       stability of some repetitive DNA sequences. The genome contains only
CC       about 5% of the wild-type level of J in their DNA. Cells lacking both
CC       JBP1 and JBP2 show a complete absence of base J.
CC       {ECO:0000269|PubMed:19136460}.
CC   -!- SIMILARITY: Belongs to the TET family. JBP1 subfamily. {ECO:0000305}.
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DR   EMBL; AF182399; AAF01741.1; -; Genomic_DNA.
DR   AlphaFoldDB; P86937; -.
DR   SMR; P86937; -.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050341; F:thymine dioxygenase activity; TAS:UniProtKB.
DR   GO; GO:0070580; P:base J metabolic process; IMP:UniProtKB.
DR   Gene3D; 1.20.120.1440; -; 1.
DR   InterPro; IPR024779; 2OGFeDO_noxygenase_dom.
DR   InterPro; IPR041241; DB_JBP1.
DR   InterPro; IPR043111; DB_JBP1_sf.
DR   Pfam; PF18526; DB_JBP1; 1.
DR   Pfam; PF12851; Tet_JBP; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; DNA-binding; Iron; Metal-binding; Nucleus; Oxidoreductase.
FT   CHAIN           1..839
FT                   /note="Thymine dioxygenase JBP1"
FT                   /id="PRO_0000412184"
FT   REGION          86..288
FT                   /note="Thymine dioxygenase"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U6M1"
FT   REGION          415..583
FT                   /note="DNA-binding JBP1 domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U6M1"
FT   BINDING         213
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         215
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         263
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         279
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   SITE            548
FT                   /note="Involved in J base recognition, conferring
FT                   specificity towards J-DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U6M1"
SQ   SEQUENCE   839 AA;  95230 MW;  72CEC5A3E3EEB342 CRC64;
     MRRQVKKVLR EKADDSMKPG WDVYQPSNDV VYAFNHYMQG SQIDAEAREK AEKAFQEAVK
     KHPFHNNADH AVDFHGTTVF 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 PAPVYPVPLT PFSCAASAWA LRGCAAAMLT
     RLHGLVRENA SLMTELFGEP VEVADGLPRR APEEIIPVHK HTNVQMHYLG GFSEKGDILN
     EAMNKRHYLD KENLQKMFGE EFVNIWTQSR THWLQLVKKE WEHQKETNPT RTRFSWNNTS
     AMNFAFFDLC DVAKQLMCGA FGDREVNKKE EQSFWGMFAA HLDNACINEI GMLQGSMGMH
     KLNVKLKDYN FGGTRYLKDM PPEEQERRRR RRLEIEQARR RAPICNSESG 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