JBP2_LEITA
ID JBP2_LEITA Reviewed; 1098 AA.
AC B6EU02;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Bifunctional helicase and thymine dioxygenase JBP2;
DE AltName: Full=J-binding protein 2;
DE Short=LtJBP2;
DE Includes:
DE RecName: Full=Probable DNA helicase JBP2;
DE EC=3.6.4.12 {ECO:0000305|PubMed:19114062};
DE Includes:
DE RecName: Full=Thymine dioxygenase JBP2;
DE EC=1.14.11.6 {ECO:0000305|PubMed:19114062};
GN Name=JBP2;
OS Leishmania tarentolae (Sauroleishmania tarentolae).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC lizard Leishmania.
OX NCBI_TaxID=5689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-415; ASP-417; HIS-465;
RP ARG-479; VAL-483 AND LEU-548.
RX PubMed=19114062; DOI=10.1016/j.molbiopara.2008.12.001;
RA Vainio S., Genest P.-A., ter Riet B., van Luenen H.G.A.M., Borst P.;
RT "Evidence that J-binding protein 2 is a thymidine hydroxylase catalyzing
RT the first step in the biosynthesis of DNA base J.";
RL Mol. Biochem. Parasitol. 164:157-161(2009).
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. {ECO:0000269|PubMed:19114062}.
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:0000305|PubMed:19114062};
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:0000305|PubMed:19114062};
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:0000269|PubMed:19114062}.
CC -!- DISRUPTION PHENOTYPE: Does not lead to death. The genome contains
CC reduced level of DNA base J in the DNA. {ECO:0000269|PubMed:19114062}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FM242183; CAR82639.1; -; Genomic_DNA.
DR AlphaFoldDB; B6EU02; -.
DR SMR; B6EU02; -.
DR VEuPathDB; TriTrypDB:LtaPh_1400300; -.
DR BRENDA; 1.14.11.6; 2956.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; TAS:UniProtKB.
DR GO; GO:0070580; P:base J metabolic process; IMP:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; Dioxygenase; DNA-binding; Helicase; Hydrolase; Iron;
KW Metal-binding; Nucleotide-binding; Nucleus; Oxidoreductase.
FT CHAIN 1..1098
FT /note="Bifunctional helicase and thymine dioxygenase JBP2"
FT /id="PRO_0000377561"
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"
FT MUTAGEN 415
FT /note="H->A: Impairs DNA base J biosynthesis."
FT /evidence="ECO:0000269|PubMed:19114062"
FT MUTAGEN 417
FT /note="D->A: Impairs DNA base J biosynthesis."
FT /evidence="ECO:0000269|PubMed:19114062"
FT MUTAGEN 465
FT /note="H->A: Impairs DNA base J biosynthesis."
FT /evidence="ECO:0000269|PubMed:19114062"
FT MUTAGEN 479
FT /note="R->A: Impairs DNA base J biosynthesis."
FT /evidence="ECO:0000269|PubMed:19114062"
FT MUTAGEN 483
FT /note="V->A: No effect; when associated with Q-548."
FT /evidence="ECO:0000269|PubMed:19114062"
FT MUTAGEN 548
FT /note="L->Q: No effect; when associated with A-483."
FT /evidence="ECO:0000269|PubMed:19114062"
SQ SEQUENCE 1098 AA; 123938 MW; 387AE21C14849538 CRC64;
MLNGLTRVST SSELESILDI VQSSGEIAVV FISPSIGDLE TITSETQRRQ LRIAGIPRGG
YTILPAIPLY DDELLQMCER YTAANDYEKA QIRDSLFMRE YPLFAYSVRN HKALFHPADY
VSRILQFCSY YVQAPDADVL SLLDRSPFLH ISPIKEICTH IRLIARGTPL APEDSESPAP
EQLRFHAESD AEKLAAERAG AMSIATSSGG ASETEQLSLF SGVVPSALFQ KDAVEEVDKD
TEETMVDLTG EETVDAVHSF QAEYLTLDGL ELVTKAAIFY DREGEGQRIV AVYIPGGVPE
DTCRAAAAVL EPAATKKNLR ALTNGGLPPD TGLVGYYDYL TNPTRHKCRE TEFSRRNWGL
LAQSEPLLKH LDKLYSQLAP MHHHLQKVAI PSQYQLCGTV FSTITVNRNF RTAVHTDKGD
FRSGLGVLSV INGEFEGCHL AIKKLKKAFQ LKVGDVLLFD TSLEHGNTEV INPEIHWQRT
SIVCYLRTGL MSSVCEMERR KHLNRLILQQ LRNTEVLNTT VNINGADSSL PPLFVPTRLA
SHLAPVQLAA LGFIVERTEK QSGCVVAMTM GLGKTLVALT LCFSQLHLAP QADILILTPK
PIISHWVDEK NKWAMHGLHF PHFVASDGLN SLEFEQQLLE YERQKNNEKP KLGHVFVING
EYLAGFLRRF KRFTPLLIIV DEGHRVAAKG NKLTESLDRL RCNLRIVLSG TPLQNDASEL
YRLVGWVNKG VGRVLPPKRF QELANDINQF VEGDDGAFYN AVMAQEYIQD WMRGFVFREM
ENDLPPLHDY LLICGSSDVQ REYEEKLGLT ETTMTALKAT EHRPHHLSTH PACYLAFISD
SYQSMVSGWT VRAQANTSRM RVSQLEEIDT MRLEHYVQMV ENEQLDTFID LSGKMRVLVD
IVLRVQARKE KLIIFSLYVG SQDLIHRTLT ALRVCTFTVR GRDSQDRRRR AMQEFSENKD
LIVLVLSTKI AAYGLDFTAA NHVVLFDSWW NPQVDAQAIA RAYRRNQRKP VTVYRLISAT
ENKFVLSSQT RKIALFKCIL HERTSRQALP DELEDCAANE KDEERRSFWA KLKTTLLAGG
TRALLNVYRY QESVRESE
