JBP1A_TRYCC
ID JBP1A_TRYCC Reviewed; 832 AA.
AC Q4DBW3;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Thymine dioxygenase JBP1-A;
DE EC=1.14.11.6 {ECO:0000250|UniProtKB:Q9U6M1};
DE AltName: Full=J-binding protein 1A;
DE AltName: Full=Thymidine hydroxylase JBP1-A;
GN Name=JBP1A; ORFNames=Tc00.1047053510357.10;
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; AAHK01000683; EAN90000.1; -; Genomic_DNA.
DR RefSeq; XP_811851.1; XM_806758.1.
DR AlphaFoldDB; Q4DBW3; -.
DR SMR; Q4DBW3; -.
DR PaxDb; Q4DBW3; -.
DR PRIDE; Q4DBW3; -.
DR EnsemblProtists; EAN90000; EAN90000; Tc00.1047053510357.10.
DR GeneID; 3542898; -.
DR KEGG; tcr:510357.10; -.
DR eggNOG; ENOG502RTYX; Eukaryota.
DR OMA; SFTYEHE; -.
DR OrthoDB; 157110at2759; -.
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; -; 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 3: Inferred from homology;
KW Dioxygenase; DNA-binding; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..832
FT /note="Thymine dioxygenase JBP1-A"
FT /id="PRO_0000377556"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 832 AA; 93816 MW; 78C00B8F2ABF54FA CRC64;
MKQKRGKQDV KMLESAPPQL LPKKGRLEIS ELAPQQRTIR TAEEIETAYN EAVRKHPFYD
NADHTIDFHD ATVFRDARGV VGGVFLPGAL PAFAATMAAD VLRPAAVRTS LRSNMFGGFA
PLSGIAGYFD YRGSPVELKC RKTSFTYENV HSWPNVFPMI DYVSAIYKAV FPEQWAAQDA
AVPDIVRIHG SPFSTLTVNQ QFRTASHTDA GDFDMGYGLL AVLEGKFEGL SLALDDFGVC
FRMQPRDILI FNTHFFHSNT EPELNHPRDD WSRLTCVCYY RAALGEPACV AEYERRLARA
KEIGASPPPA VDAILQKDNG NNFNKPAPTF PYLLTPFGGA ASVCSLHCCT AKLLRLHELL
LENPTLEVIL FGESLRTDDG LPRREKEQLI SVHLPVVVKM SPSGGFSELG GALKAAEEKQ
YFFEEKYLAD ELGPDLMSMW TQSRAHWLRL VKEDWERLCR RDPERTKFTW NNSSAMNAAF
FDLCEVAKQM MIGLLNKETP SSAENHSFWI LFAAHLNYAC TTENGMPRDA VGMHKLNVKL
KDFHFGGTRY LKDMPPEEQE RRLERKKRIE EARRRGSSAH ETHTDNWLLN DTFDYQQEDR
KVEFEENGWM TPEAYVKHLG LKPCGDVTAA ASPTEPIHVL VVLPRPAAAA TAKDAKRDVP
LATSEESIRL LMNPAAQRVL RGKARNVALP SPLSFGGVKI TVLFDGDDID CIHPDFVILQ
HLLATIEEDE AAKARVKYWA RVARYCVFVV ETDVRDRRHF LLREEVRVAY EDVAEDCFRS
LHAAAYSTKY NRLRTTPSLI ALCNRKNIGL RFKFRGSPLN TIALVVVGER LD
