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Database: UniProt
Entry: Q4QFY1
LinkDB: Q4QFY1
Original site: Q4QFY1 
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   16-OCT-2019, entry version 72.
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; Euglenozoa; Kinetoplastida; Trypanosomatidae;
OC   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.,
RA   Cadag E., Ciarloni L., Clayton C., Coulson R.M.R., Cronin A.,
RA   Cruz A.K., Davies R.M., De Gaudenzi J., Dobson D.E., Duesterhoeft A.,
RA   Fazelina G., Fosker N., Frasch A.C., Fraser A., Fuchs M., Gabel C.,
RA   Goble A., Goffeau A., Harris D., Hertz-Fowler C., Hilbert H., Horn D.,
RA   Huang Y., Klages S., Knights A., Kube M., Larke N., Litvin L.,
RA   Lord A., Louie T., Marra M., Masuy D., Matthews K., Michaeli S.,
RA   Mottram J.C., Mueller-Auer S., Munden H., Nelson S., Norbertczak H.,
RA   Oliver K., O'neil S., Pentony M., Pohl T.M., Price C., Purnelle B.,
RA   Quail M.A., Rabbinowitsch E., Reinhardt R., Rieger M., Rinta J.,
RA   Robben J., Robertson L., Ruiz J.C., Rutter S., Saunders D.,
RA   Schaefer M., Schein J., Schwartz D.C., Seeger K., Seyler A., Sharp S.,
RA   Shin H., Sivam D., Squares R., Squares S., Tosato V., Vogt C.,
RA   Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J., Zhou S.,
RA   Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D., Barrell B.G.,
RA   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
CC       thymidine residue found in the genome of kinetoplastid parasites,
CC       which is localized primarily to repetitive DNA, namely the
CC       telomeres, and is implicated in the regulation of antigenic
CC       variation. Probably also acts as a DNA helicase. Recognizes and
CC       binds specific regions of the genome, hydrolyzes ATP and allows
CC       the DNA base J de novo synthesis. Involved in initial synthesis of
CC       DNA base J, JBP1 being able to act via the basal level of DNA base
CC       J and propagate further synthesis. In contrast to JBP1, it does
CC       not specifically bind DNA base J, it however binds chromatin (By
CC       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 +
CC         CO2 + 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.
CC       {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.
CC       JBP2 subfamily. {ECO:0000305}.
DR   EMBL; FR796410; CAJ02566.1; -; Genomic_DNA.
DR   RefSeq; XP_001687603.1; XM_001687551.1.
DR   STRING; 5664.LmjF.14.0040; -.
DR   PRIDE; Q4QFY1; -.
DR   EnsemblProtists; CAJ02566; CAJ02566; LMJF_14_0040.
DR   GeneDB; LmjF.14.0040:pep; -.
DR   GeneID; 5650208; -.
DR   KEGG; lma:LMJF_14_0040; -.
DR   EuPathDB; TriTrypDB:LmjF.14.0040; -.
DR   eggNOG; KOG0387; Eukaryota.
DR   eggNOG; ENOG410XP4Z; LUCA.
DR   HOGENOM; HOG000113126; -.
DR   InParanoid; Q4QFY1; -.
DR   KO; K22407; -.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015616; F:DNA translocase activity; IBA:GO_Central.
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:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR   Gene3D; 3.40.50.10810; -; 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_N; 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; Complete proteome; Dioxygenase; DNA-binding; Helicase;
KW   Hydrolase; Iron; Metal-binding; Nucleotide-binding; Nucleus;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN         1   1098       Bifunctional helicase and thymine
FT                                dioxygenase JBP2.
FT                                /FTId=PRO_0000377560.
FT   DOMAIN      555    730       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      897   1057       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     568    575       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION        1    540       Thymine dioxygenase.
FT   REGION      541   1098       DNA Helicase.
FT   MOTIF       681    684       DEAH box.
FT   METAL       415    415       Iron; catalytic; for thymine dioxygenase
FT                                activity. {ECO:0000250|UniProtKB:Q6N021}.
FT   METAL       417    417       Iron; catalytic; for thymine dioxygenase
FT                                activity. {ECO:0000250|UniProtKB:Q6N021}.
FT   METAL       465    465       Iron; catalytic; for thymine dioxygenase
FT                                activity. {ECO:0000250|UniProtKB:Q6N021}.
FT   BINDING     479    479       2-oxoglutarate.
FT                                {ECO:0000250|UniProtKB:Q6N021}.
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
//
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