JBP1_LEIMA
ID JBP1_LEIMA Reviewed; 814 AA.
AC Q4QHM7;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=LmjF09.1480, LmjF_09_1480;
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin;
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B.G., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(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; FR796405; CAJ03108.1; -; Genomic_DNA.
DR RefSeq; XP_001681321.1; XM_001681269.1.
DR AlphaFoldDB; Q4QHM7; -.
DR SMR; Q4QHM7; -.
DR EnsemblProtists; CAJ03108; CAJ03108; LMJF_09_1480.
DR GeneID; 5649588; -.
DR KEGG; lma:LMJF_09_1480; -.
DR VEuPathDB; TriTrypDB:LmjF.09.1480; -.
DR VEuPathDB; TriTrypDB:LMJLV39_090022400; -.
DR VEuPathDB; TriTrypDB:LMJSD75_090022100; -.
DR eggNOG; ENOG502RTYX; Eukaryota.
DR InParanoid; Q4QHM7; -.
DR OMA; SFTYEHE; -.
DR BRENDA; 1.14.11.6; 2950.
DR Proteomes; UP000000542; Chromosome 9.
DR GO; GO:0005634; C:nucleus; ISO:GeneDB.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008198; F:ferrous iron binding; ISO:GeneDB.
DR GO; GO:0050341; F:thymine dioxygenase activity; ISO:GeneDB.
DR GO; GO:0070580; P:base J metabolic process; ISO:GeneDB.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IBA:GO_Central.
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_0000377553"
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; 91826 MW; 1AFAFC544A964F3D CRC64;
MEPDPKKIKL DIFNFPTARE TRTPEEVAES YAEAVKSHPF YDNVHSVIDF YDSGTIKDGR
GQIIGVVLRE ALPKYAVSMA SELLASAAVR TSLRSMMFGG ESPLSGIAGY FDYRGSPVEL
KSRKTSFTYE HEAAWPAVFP VVDYVSELYR HVAPERWKAQ NDAIPDVVRI HGTPFSTLTI
NSRFRTASHT DVGDFDGGYS CIACLDGHFK GLALAFDDFG INVLMQPRDV MIFDSHHFHS
NTEVELSFSG EDWKRLTCVF YYRAALGEPA SYAEYQRRLE KSKQDNSFTP VVSNVRVKEN
GTNLNRPSPV YPICPSPFWV PMVAHCLQHC ASEAQCVHDA MTADGSRLAE VMFGEPLSTS
DGIPLRGEDK KLKANSDSAS RPLSRLGGFS ETNLMVSTAV EKKKYLNSEF LSHFISAQLL
DMWKQARGKW LELVGREWTH MLALNPERKD FLWKNQSEMN SAFFDLCEVG KQVMLGLLGK
EVALPKEEQA FWTMYAVHLN AACAEELHMP HVAMSLRKLN VKLKDFNFGG TRYFKDMPPE
EQKRRMERKQ RIEEARRHGM SSGAHEKRAN WLTNDSFDYQ TEDCVVDYAQ HKWPPPALHA
KEITKNVRTG ELPTREGVVR VLVVLPDPQS KLECVDCKLE VPETVRCSCE WERLMSSLAV
RRVLAAAQRN LQLPGSVTHG NIEIRFAFHS RLPTDMCDFV VLQHVLSCIP DDVLASAYIR
RAAALCTGCV YVVETDVQCR QYYTLKCAAR CDYDAVASLF FQQLHRVSYG TKAARVRTKG
ELESLIPTVC CARYKLQGSP LNTTVHVVSP APSR
