JBP2_LEIIN
ID JBP2_LEIIN Reviewed; 1098 AA.
AC A4HVU6;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 67.
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:Q9U6M1};
GN Name=JBP2; ORFNames=LinJ14.0040, LinJ_14_0040;
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. 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM66564.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FR796446; CAM66564.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001464187.1; XM_001464150.1.
DR AlphaFoldDB; A4HVU6; -.
DR SMR; A4HVU6; -.
DR STRING; 5671.XP_001464187.1; -.
DR GeneID; 5067670; -.
DR KEGG; lif:LINJ_14_0040; -.
DR VEuPathDB; TriTrypDB:LINF_140005300; -.
DR eggNOG; KOG0387; Eukaryota.
DR InParanoid; A4HVU6; -.
DR Proteomes; UP000008153; Chromosome 14.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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: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; 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_0000377559"
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; 124115 MW; 3DB2F947B322DBAE CRC64;
MLNGLTRVST SSELESILDI VQSSGEIAVV FTSPSIGDLE TITSETQRRQ LRIAGIPRGG
YTILPAIPLY DDELLQMCER YTSANEYEKA EMRNSLYMRE YPLFTYSIRH QRALFHPADY
VSRILQFCSY YVQAPDADVL PLQDKSPFLH ISPIKEICKH LRLIARGTPV APDDSESPVP
EQLRLHAESD AEKLAAERAT AMSIATSSGG ASETEQPSLF SGVAPSALFQ KGAVEEVDKD
AEDTMEDLTG EETVDAVHSF QAEYLTLDGF ELVTKASIYY DREGEGQRVV AVYIPGGVPE
DTCRAAAAVL EPAATKKNLR APTNGGLPPD TGIVGYYDYL TNPTQHKCRE TEYSRRNWGL
LAQSEPLLKH LDKLYSQLAP MHHHLQRVAI PSQYQLCGTV FSTITVNRNF RTAVHTDKGD
FRSGLGVLSV INGEFEGCHL AIKRLKKAFQ LKVGDVLLFD TSLEHGNTEV VNPEIHWQRT
SVVCYLRTGL MSSVCEMERR KHLNRLILLQ LLNTEVRNTT VNINGADSSL PPLFVPTRLA
SHLAPVQLAA LGFIVERTEK QSGCVVAMTM GLGKTLVALT LCFSQLHLAP QADILILTPK
PIISHWVDEK NKWGMHGLHF PHFVASDGLN SLEFEQQLLE YERQRNNEKP KLGHIFVING
EYLAGFLRRF KRFTPLLMIV DEGHRVAAKG NKLTESLDRL RCNLRIVLSG TPLQNDASEL
YRLVGWVNKG VSRVLPPKRF QELANDINQF VEGDDGAFYN AVMAQEYIQD WMRGFVFREM
ENDLPPLHDY LLICGSSDVQ REYEEKLGLT ETAMTALKAT EHRPHHLSTH PACYLAFISD
SYQSMVSGWT VRAQSNTSRP RVSQLEEIDT MRLEQYVQLV ENEQLDAFID LSGKMRVLVD
IVLRVQARKE KLIIFSLYVG SQDLIHRTLT ALRVCTFTVR GRDSQDRRRR AMQEFSENKD
LIVLVLSTKI AAYGLDFTAA NHVVLFDSWW NPQVDAQAIA RAYRRNQRKP VTVYRLISAT
ENKFVLRSQT RKIALFKCIL HERTSRQALP DELEDCAANE KDEERRIFWA KLKTTSLAGD
SRALLNVYRY QESVRESE
