JBP1_CRIFA
ID JBP1_CRIFA Reviewed; 811 AA.
AC Q9U6M2;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 42.
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;
OS Crithidia fasciculata.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Crithidia.
OX NCBI_TaxID=5656;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DNA-BINDING.
RX PubMed=10562569; DOI=10.1093/emboj/18.22.6573;
RA Cross M., Kieft R., Sabatini R., Wilm M., de Kort M., van der Marel G.A.,
RA van Boom J.H., van Leeuwen F., Borst P.;
RT "The modified base J is the target for a novel DNA-binding protein in
RT kinetoplastid protozoans.";
RL EMBO J. 18:6573-6581(1999).
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}.
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; AF182400; AAF01742.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9U6M2; -.
DR SMR; Q9U6M2; -.
DR PRIDE; Q9U6M2; -.
DR VEuPathDB; TriTrypDB:CFAC1_050026200; -.
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 1: Evidence at protein level;
KW Dioxygenase; DNA-binding; Iron; Metal-binding; Nucleus; Oxidoreductase.
FT CHAIN 1..811
FT /note="Thymine dioxygenase JBP1"
FT /id="PRO_0000377550"
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 811 AA; 90444 MW; FFF1B8775E62260D CRC64;
MEPKSKKVKQ DIFNFPDGKD VPTTKEKAEA YVDALKAHPF YDNVHSVVDV YDSATLRDGK
GRVIGVMLRK ALPEHATTAA SGLLSAAAVR TSLRSSMFGG ESPLSGIAGY FDYRGSPVEL
KARKTAFTYE HEKKWPAVFP LVDYVSEIYK SVMPEHWAAQ DSAIPDIVRI HGTPFSTLTI
NSRFRTASHT DAGDFDGGYS CIACIDGDFK GLALGFDDFH VNVPMQPRDV LVFDSHYFHS
NSELEISCPT EEWRRLTCVF YYRSALGEPS SYAEYRRRLA AAQQDSTAQP VVSSVVEKPN
GKNLYKPSTV FPIDPTPFAV VAQLHRLHHC AAKGLCVHEL LAVPSSPLAV LLFGERLSCS
DGIPLRAAEQ KLKANADGAS RGVTSSGGFS ESDAVLTTAV EKSKYLERDH LSQCISAELL
AMWVEARKHW LRLVATEWAR MIATAPERTD FLWKNKSPMN TAFFDLCEVA KQVMLGLLDK
ETATPTEERH FWSVYAAHLH RACAERLMMP EEAMSLRKLN VKLKDFSFGG TRYFKDMPVE
EQERRVARKA SIEEARRRST AAKDGEQRSN WLTNDAFDYQ TEDCEVDYAG HGWAVPKQHA
KTVTANVHQE AVAATTEAVR VLVVLPRPPS GDRGDAAVDL PKEVTTSAEW VRLMSSPAVR
RVLAAKQRNL TLLPNCNVEA VSLNFAYHDS LPQKATFDFV VLQHVLSAMP EDAIATDYVS
RMRSICTGCL FVVETDVQCR QYFTLHYPLR VQYDAVAPAF FQLLHRCSYG TPLARTRTKA
EVEALFPFVC CARYKLQGSP MNTVVHLLAL E
