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Database: UniProt
Entry: A4H7G5
LinkDB: A4H7G5
Original site: A4H7G5 
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   16-OCT-2019, entry version 58.
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; Euglenozoa; Kinetoplastida; Trypanosomatidae;
OC   Leishmaniinae; Leishmania; 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.,
RA   Chillingworth T., Hance Z., Jagels K., Moule S., Ormond D., Rutter S.,
RA   Sqaures R., Whitehead S., Rabbinowitsch E., Arrowsmith C., White B.,
RA   Thurston S., Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D.,
RA   Depledge D.P., Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O.,
RA   Barrell B., Cruz A.K., 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
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; FR798988; CAM37473.1; -; Genomic_DNA.
DR   RefSeq; XP_001562198.1; XM_001562148.1.
DR   PRIDE; A4H7G5; -.
DR   GeneDB; LbrM.14.0040:pep; -.
DR   GeneID; 5413800; -.
DR   KEGG; lbz:LBRM_14_0040; -.
DR   EuPathDB; TriTrypDB:LbrM.14.0040; -.
DR   eggNOG; KOG0387; Eukaryota.
DR   eggNOG; ENOG410XP4Z; LUCA.
DR   InParanoid; A4H7G5; -.
DR   KO; K22407; -.
DR   OMA; EMENDLP; -.
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: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   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_0000377558.
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;  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
//
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