JBP1_LEIBR
ID JBP1_LEIBR Reviewed; 813 AA.
AC A4H5X5;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 60.
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; ORFNames=LbrM09_V2.1540, LbrM_09_1540;
OS Leishmania braziliensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC Leishmania braziliensis species complex.
OX NCBI_TaxID=5660;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904;
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.-A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Sqaures R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
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; FR798983; CAM41892.1; -; Genomic_DNA.
DR RefSeq; XP_001562766.1; XM_001562716.1.
DR AlphaFoldDB; A4H5X5; -.
DR SMR; A4H5X5; -.
DR GeneID; 5413245; -.
DR KEGG; lbz:LBRM_09_1540; -.
DR VEuPathDB; TriTrypDB:LbrM.09.1540; -.
DR VEuPathDB; TriTrypDB:LBRM2903_090022000; -.
DR InParanoid; A4H5X5; -.
DR OMA; SFTYEHE; -.
DR Proteomes; UP000007258; Chromosome 9.
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..813
FT /note="Thymine dioxygenase JBP1"
FT /id="PRO_0000377551"
FT REGION 62..264
FT /note="Thymine dioxygenase"
FT /evidence="ECO:0000250|UniProtKB:Q9U6M1"
FT REGION 392..561
FT /note="DNA-binding JBP1 domain"
FT /evidence="ECO:0000250|UniProtKB:Q9U6M1"
FT BINDING 189
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 191
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 239
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 255
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT SITE 525
FT /note="Involved in J base recognition, conferring
FT specificity towards J-DNA"
FT /evidence="ECO:0000250|UniProtKB:Q9U6M1"
SQ SEQUENCE 813 AA; 92367 MW; D33B74E3EE76F940 CRC64;
MESSTKRIKM DIFNFPTIKE TRTPEEVAES YAEAVKLHPF YDNAHCVIDF YDSGTIKDGR
GEIIGVVLRK ALPKYATSMA SALLISAAVR TSLRSMIFGG ESPLSGIAGY FDYRGSPVEL
KSRKTSFTYE HEEAWSAVFP VVDYVSEIYR HVAPERWKAQ NNAIPDLVRI HGTPFSTLTI
NSRFRTASHT DVGDFDAGYS CIACIDGKFK GLALTFDDFR INVLMQPRDV MVFDSHHFHS
NTEVEVSCSE EDWKRLTCVF YYRTALGEPS SYAEYRRRLE KSKQDPSFTP VVSNVMMKEN
GTNLNRPSPV HPVPPSPFWL PMLAHCLQHC ASAAQSVHEA MTADGSQLAE IIFGEPLSTS
DGIPLRGDDE KLKANGDTGA KPLSRLGGFS ETDLMVSTAA EKRKYLDSEF LSHCISAQLL
DMWKQARARW LELVGKEWKH MLTLNPERKD FLWKNRSEMN SAFFDLCEVG KQVMLGLLDK
EAALPKEEQA FWTMYAVHLS AACAEELHMP HDAMSLRKLN VKLKDFNFGG TRYFKDMPPE
EQQRRMERKQ RIEEARRHGM TGAHEKRANW LTNDSFDYQT EDCVVDYAKH KWVLPERHAK
AVTKNVHTAW LPTREEVVRV LVVLPDLQIR VEGVDCKLEK PDTVEDSSEW VRLVSSPAVH
RLLAAAQRNL QLPDDVMHGN IHIRFVFHST LPTDMYDFVV LQHVLSRIPD DVLASSYITR
AAALCSGCLF VEETDVQCRQ YYTLKYSIRR NYDAVAPHFF QQLHQASYGT KMARVRTKGE
LEALIPTVCC ARYKLQGSPL NTTIHVVSPT APH
