JBP2_LEIBR
ID JBP2_LEIBR Reviewed; 1098 AA.
AC A4H7G5;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=LbrM14_V2.0040, LbrM_14_0040;
OS Leishmania braziliensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC Leishmania braziliensis species complex.
OX NCBI_TaxID=5660;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904;
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}.
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DR EMBL; FR798988; CAM37473.1; -; Genomic_DNA.
DR RefSeq; XP_001562198.1; XM_001562148.1.
DR AlphaFoldDB; A4H7G5; -.
DR SMR; A4H7G5; -.
DR STRING; 5660.A4H7G5; -.
DR GeneID; 5413800; -.
DR KEGG; lbz:LBRM_14_0040; -.
DR VEuPathDB; TriTrypDB:LbrM.14.0040; -.
DR VEuPathDB; TriTrypDB:LBRM2903_140005300; -.
DR InParanoid; A4H7G5; -.
DR OMA; QDLIHRT; -.
DR Proteomes; UP000007258; 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_0000377558"
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; 124231 MW; 4F7CCE69153FA927 CRC64;
MPSGLMRANT STELESILDI VQSSGEIAVV FTSPSIGDLE TITSETQRRQ LRIAGIPRGG
YTILPAIPLY DDELLQMCER YTAASEHEKV EIRNSLYMRE YPLFAYSMRN QRALFHPADY
VSRILQFCFH YVQVPDEDVL SLQDRSPFLH ISPVKEICVH LRLIVRGTPA APDESESPVP
EQLHFHAESD AEKLAAERAR ALSIAASSGG ASETEPLSLF TGVAPSALFQ KGAVEEVDLD
TEETIEDLTG EETVDAVHSF HSEYLTLSGF ELVTKASIFY DHEGEGQRVV AVYIPGGVPK
ETCRAAAAVL ELAVTKKNLR AATNGGLPPD TGIVGYYDYL TNPTQHKCRE TEFSRRNWGL
FSQSESLLKH LDKLYSQLAP THHHLQRVAI PSQYQLCGTV FSTITVNRNF RTAVHTDKGD
FRSGLGVLSV INGEFEGCHL AIKSLKKAFQ LKVGDVLLFD TSLEHGNTEV VHPENHWQRT
SIVCYLRTGL MSSVCEMERR KHLNRLILQQ LLNTEIRHTT VNINEADSSL PPLFVPTRLA
SQLAPVQLAA LGFIVERTNK QSGCVVAMTM GLGKTLVALT LCFSHLHLAP QADILILTPK
PIISHWVDEK NKWGMYGLHF PHFVASDGLN SLEFEQQLLE YERQKNNEKP KAGHVFVINS
EYLAGFLRRF RRFTPFLIIV DEGHRVAAKG NKLTESLDRL RCNLRVVLSG TPLQNDASEL
YRLVGWVNKG VSKVLPPKRF QELANSINQF VEGDDGAFYN AVMAQEYIQD WMRGFVFREM
ENDLPPLHDY LLVCGSSNVQ REYEEKLGLT ETAMTALRAT EHRPHHLSTH PACYLAFISN
CYQSMVSGWT VRAQSNTSRL RTTQLEEIDA MRLEQYAQMI ENEQLDAFIN VSGKMRVLVD
IVLRVQARKE KLIIFSLYVG SQDLIHRTLT ALRVCTFTVR GRDSQDRRRR AMHEFSENKD
LTVLVLSTKI AAYGLEFTAA NHVVLFDSWW NPQADAQAIA RAYRRNQRKP VTVYRLISAT
ENKFVLRSQT RKIALFKCIF HKRTTRQALP SELEDCSANE TDNERRDFWA KLKATHLVGD
TRALLNVYRY QESVRESQ
