JBP2_LEIMA
ID JBP2_LEIMA Reviewed; 1098 AA.
AC Q4QFY1;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Bifunctional helicase and thymine dioxygenase JBP2;
DE AltName: Full=J-binding protein 2;
DE Includes:
DE RecName: Full=Probable DNA helicase JBP2;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:B6EU02};
DE Includes:
DE RecName: Full=Thymine dioxygenase JBP2;
DE EC=1.14.11.6 {ECO:0000250|UniProtKB:B6EU02};
GN Name=JBP2; ORFNames=LmjF14.0040, LmjF_14_0040;
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. Probably also acts
CC as a DNA helicase. Recognizes and binds specific regions of the genome,
CC hydrolyzes ATP and allows the DNA base J de novo synthesis. Involved in
CC initial synthesis of DNA base J, JBP1 being able to act via the basal
CC level of DNA base J and propagate further synthesis. In contrast to
CC JBP1, it does not specifically bind DNA base J, it however binds
CC chromatin (By similarity). {ECO:0000250|UniProtKB:B6EU02}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:B6EU02};
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:B6EU02};
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:B6EU02}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the SNF2/RAD54
CC helicase family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the TET family. JBP2
CC subfamily. {ECO:0000305}.
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DR EMBL; FR796410; CAJ02566.1; -; Genomic_DNA.
DR RefSeq; XP_001687603.1; XM_001687551.1.
DR AlphaFoldDB; Q4QFY1; -.
DR SMR; Q4QFY1; -.
DR STRING; 5664.LmjF.14.0040; -.
DR EnsemblProtists; CAJ02566; CAJ02566; LMJF_14_0040.
DR GeneID; 5650208; -.
DR KEGG; lma:LMJF_14_0040; -.
DR VEuPathDB; TriTrypDB:LmjF.14.0040; -.
DR VEuPathDB; TriTrypDB:LMJLV39_140005400; -.
DR VEuPathDB; TriTrypDB:LMJSD75_140005400; -.
DR eggNOG; KOG0387; Eukaryota.
DR InParanoid; Q4QFY1; -.
DR BRENDA; 1.14.11.6; 2950.
DR Proteomes; UP000000542; Chromosome 14.
DR GO; GO:0005634; C:nucleus; ISO:GeneDB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
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; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR024779; 2OGFeDO_noxygenase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF12851; Tet_JBP; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Dioxygenase; DNA-binding; Helicase; Hydrolase; Iron;
KW Metal-binding; Nucleotide-binding; Nucleus; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..1098
FT /note="Bifunctional helicase and thymine dioxygenase JBP2"
FT /id="PRO_0000377560"
FT DOMAIN 555..730
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 897..1057
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..540
FT /note="Thymine dioxygenase"
FT REGION 541..1098
FT /note="DNA Helicase"
FT MOTIF 681..684
FT /note="DEAH box"
FT BINDING 415
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic; for thymine dioxygenase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 417
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic; for thymine dioxygenase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 465
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic; for thymine dioxygenase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 479
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 568..575
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1098 AA; 124001 MW; 3D3884AE7DB05DAE CRC64;
MLNGLTRVST SSELESILDI VQSSGEIAVV FTSPSIGDLE TIASETQRRQ LRIAGIPRGG
YTILPAIPLY DDELLQMCER YTAANEYEKA EMRNSLYMRE YPLFAYSMRH QRALFHPADY
VSRILQFCSY YVQAPDADVL SLQDRSPFLH ISPIKEICTQ LRLIARGTPV AASDSESPVP
EQLRLHAESD VEKLAAERAT AMSIAASSGG ASETEQLSLF SGVAPSALFQ KDAVEEVNKD
AEDTMEDLTG EETVDAVHSF QAEYLTLDGF ELVTKASIFY DREGEGQCIV AVYIPGGVPE
DTCRAAAAVL EPAATKKNLR APTNGGLPPD TGIVGYYDYL TNPTQHKCRE TEFSRRNWGL
LAQSEPLLKH LDKLYSQLAP MHHHLQRVAI PSQYQLCGTV FSTITVNRNF RTAVHTDRGD
FRSGLGVLSV INGEFEGCHL AIKRLKKAFQ LKVGDVLLFD TSLEHGNTEV VNPEIHWQRT
SVVCYLRTGL MSSVCEMERR KHLNRLILEQ LLNTEVRNTT VNINGADSSL PPLFVPTRLA
SHLAPVQLAA LGFIVERTEK QSGCVVAMTM GLGKTLVALT LCFSQLYLAP QADILILTPK
PIISHWVDEK NKWGMHGLHF PHFVASDGLN SLEFEQQLLE YERQKNNEKP KSGHIFVING
EYLAGFLRRF KRFTPLVMIV DEGHRVAAKG NKLTESLDRL RCNLRIVLSG TPLQNDASEL
YRLVGWVNKG VSRVLPPKRF QELANDINQF VEGDDGAFYN AVVAQEYIQD WMRGFVFREM
ENDLPPLHDY LLICGSSDVQ REYEEKLGLT ETAMTALKAT EHRPHHLSTH PACYLAFISD
SYQSMVSGWT VRALSNTSRQ RVSQLEEIDT MRLEQYVQLV ENEQLDAFID LSGKMRVLVD
IVLRVQARKE KLIVFSLYVG SQDLIHRTLT ALRVCTFTVR GRDSQDRRRR AMQEFSENKD
LIVLVLSTKI AAYGLDFTAA NHVVLFDSWW NPQVDAQAIA RAYRRNQRKP VTVYRLISAT
ENKFVLRSQT RKIALFKCIL HERTSRQALP DELEDCAANE KDEERRNFWA KLKMTSLAGD
TRALLNVYRY QESVRESE
