ID   JBP1B_TRYCC             Reviewed;         831 AA.
AC   Q4DLX9;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   08-NOV-2023, entry version 50.
DE   RecName: Full=Thymine dioxygenase JBP1-B;
DE            EC=1.14.11.6 {ECO:0000250|UniProtKB:Q9U6M1};
DE   AltName: Full=J-binding protein 1B;
DE   AltName: Full=Thymidine hydroxylase JBP1-B;
GN   Name=JBP1B; ORFNames=Tc00.1047053506753.120;
OS   Trypanosoma cruzi (strain CL Brener).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=353153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL Brener;
RX   PubMed=16020725; DOI=10.1126/science.1112631;
RA   El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA   Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA   Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA   Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA   Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA   da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA   Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA   Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA   Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA   Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA   Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA   Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA   Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA   Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA   Andersson B.;
RT   "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT   disease.";
RL   Science 309:409-415(2005).
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 (By similarity). {ECO:0000250|UniProtKB:Q9U6M1}.
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:0000250|UniProtKB:Q9U6M1}.
CC   -!- DOMAIN: The DNA-binding JBP1 domain (DB-JBP1) is necessary and
CC       sufficient for binding to J-DNA. {ECO:0000250|UniProtKB:Q9U6M1}.
CC   -!- SIMILARITY: Belongs to the TET family. JBP1 subfamily. {ECO:0000305}.
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DR   EMBL; AAHK01000343; EAN93526.1; -; Genomic_DNA.
DR   RefSeq; XP_815377.1; XM_810284.1.
DR   AlphaFoldDB; Q4DLX9; -.
DR   SMR; Q4DLX9; -.
DR   PaxDb; 353153-Q4DLX9; -.
DR   EnsemblProtists; EAN93526; EAN93526; Tc00.1047053506753.120.
DR   GeneID; 3547091; -.
DR   KEGG; tcr:506753.120; -.
DR   eggNOG; ENOG502RTYX; Eukaryota.
DR   InParanoid; Q4DLX9; -.
DR   OrthoDB; 167469at2759; -.
DR   Proteomes; UP000002296; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050341; F:thymine dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070580; P:base J metabolic process; IEA:UniProt.
DR   Gene3D; 1.20.120.1440; JBP1, DNA-binding domain; 1.
DR   InterPro; IPR024779; 2OGFeDO_JBP1/TET_oxygenase_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   3: Inferred from homology;
KW   Dioxygenase; DNA-binding; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..831
FT                   /note="Thymine dioxygenase JBP1-B"
FT                   /id="PRO_0000377557"
FT   REGION          80..282
FT                   /note="Thymine dioxygenase"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U6M1"
FT   REGION          409..578
FT                   /note="DNA-binding JBP1 domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U6M1"
FT   BINDING         207
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         209
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         257
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         273
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   SITE            542
FT                   /note="Involved in J base recognition, conferring
FT                   specificity towards J-DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U6M1"
SQ   SEQUENCE   831 AA;  93540 MW;  8AC5FC67B4CE1595 CRC64;
     MKQKRGKQDV KMVESAPPQL LPKKGRLEIS ELAPQQRTIR TAEEIEMAYN EAVRKHPFYD
     NADHTIDFHD ATVFRDARGV VGGVLLPGAL PAFAATMAAD VLRPAAVRTS LRSNMFGGFA
     PLSGIAGYFD YRGSPVELKC RKTSFTYENV HSWPNVFPMI DYVSAIYKAV FPERWAAQDA
     AVPDIVRIHG SPFSTLTVNQ QFRTASHTDA GDFDMGYGLL AVLEGKFEGL SLALDDFGVC
     FRMQPRDVLI FNTHFFHSNT EPELNHPKDD WSRLTCVCYY RAALGEPACV AEYERRLARA
     KEIGASPPPA VDAILQKDNG NNFNKPAPTF TYSLTPFGGA ASICSLHCCT AKLLRLHELL
     LENPTLEVIL FGESLRTDDG LPRREKEQLI SVHLPVVVKM SPSGGFSELG GALKAAEEKQ
     YFFEEKYLAD ELGPDLMSMW TQSRAHWLRL VKEDWERLCR RDPERTKFTW NNSSAMNAAF
     FDLCEVAKQM MIGLLNKETP SSAENHSFWI LFAAHLNYAC TTENGMPRDA VGMHKLNVKL
     KDFHFGGTRY LKDMPPEEQE RRLERKKRIE EARRRGNAAR ETHTDNWLLN DTFDYQQEDR
     KVEFEENGWM TPEAYVKHLG LKPCGDVTAA ASPTEPIHVL VVLPRPAAAA PKDVKRDVPL
     ATSEESIRLL MNPAAQRVLT GKARNVTLPS PLSFGGVKIT VLFDGDDIDC IHPDFVVLQH
     LLAAIEEDEA AKARVKYWAH VARYCVFVVE TDVRDRRHFL LREEVRVAYE DVAEDCFRSL
     HAAAYSTKCN RLRTTPSLIA LSNSKNIGLR FKFRGSPLNT IALIVVGERL D
//