JBP1_LEIIN
ID JBP1_LEIIN Reviewed; 814 AA.
AC A4HU70;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 59.
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=LinJ09.1540, LinJ_09_1560;
OS Leishmania infantum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5;
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; FR796441; CAM65977.1; -; Genomic_DNA.
DR RefSeq; XP_001463611.1; XM_001463574.1.
DR AlphaFoldDB; A4HU70; -.
DR SMR; A4HU70; -.
DR GeneID; 5066971; -.
DR KEGG; lif:LINJ_09_1560; -.
DR VEuPathDB; TriTrypDB:LINF_090022400; -.
DR eggNOG; ENOG502RTYX; Eukaryota.
DR InParanoid; A4HU70; -.
DR OMA; SFTYEHE; -.
DR Proteomes; UP000008153; 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..814
FT /note="Thymine dioxygenase JBP1"
FT /id="PRO_0000377552"
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 814 AA; 91928 MW; 1B2CA6E4D92279CB CRC64;
MEPDPKKVKL DIFDFPTARE TRTPEEVAES YAEAVKSHPF YDNVHSAIDF YDSGTIKDGR
GQIIGVVLRE ALPKYAASMA SELLASAAVR TSLRSMMFGG ESPLSGIAGY FDYRGSPVEL
KSRKTSFTYE HEAAWPAVFP VVDYVSELYR HVAPERWKAQ NDAIPDVVRI HGTPFSTLTI
NSRFRTASHT DVGDFDGGYS CIACLDGQFK GLALAFDDFG INVLMQPRDV MIFDSHHFHS
NTEVELSFSG EDWKRLTCVF YYRAALGEPA SYAEYRRRLE KSKQDTSFTP VVSNVRVKEN
GTNLNRPSPV YPIFLSPFWV PMVAHCLQHC ASEAQCVHDA MTADGSRLAE VMFGEPLSTS
DGIPLRGEEE KLKANSDSAS RPLSRLGGFS ETNLMVSTAV EKKKYLNSEF LSHFISAQLL
DMWKQARGKW LELVGREWTH MLALNPERKD FLWRNQSEMN SAFFDLCEVG KQVMLGLLGK
EAALPKEEQA FWTMYAVHLN AACAEELNMP HVAMSLRKLN VKLKDFNFGG TRYFKDMPPE
EQKRRMERKQ RIEEARRHGM SSGAHEKRAN WLTNDSFDYQ TEDCVFDYAQ HKWVPPALHA
KEITKNVRSG ELPTREGVVR VLVVLPDPQS KVDCVDCKLE VSETVRCSCE WERLMSSPAV
HRVLAAAQRN LQLPDSVTHD NIEIRFAFHS RLPTDMCDFV VLQHVLSCIP DDVLASAYIR
RSAALCSGCV FVVETDVQCR QYYTLKCSVR CDYDAVAPLF FQQLHRVSYG TKAARVRTKG
ELESLIPTVC CARYKLQGSP LNTTVHVVAP APPR
