GenomeNet

Database: UniProt
Entry: Q57X81
LinkDB: Q57X81
Original site: Q57X81 
ID   JBP2_TRYB2              Reviewed;        1077 AA.
AC   Q57X81;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   16-OCT-2019, entry version 72.
DE   RecName: Full=Bifunctional helicase and thymine dioxygenase JBP2;
DE   AltName: Full=J-binding protein 2;
DE            Short=TbJBP2;
DE   Includes:
DE     RecName: Full=Probable DNA helicase JBP2;
DE              EC=3.6.4.12 {ECO:0000305|PubMed:15694344, ECO:0000305|PubMed:19136460};
DE   Includes:
DE     RecName: Full=Thymine dioxygenase JBP2;
DE              EC=1.14.11.6 {ECO:0000305|PubMed:15694344, ECO:0000305|PubMed:19136460};
GN   Name=JBP2; ORFNames=Tb927.7.4650;
OS   Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=185431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
RX   PubMed=16020726; DOI=10.1126/science.1112642;
RA   Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA   Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B.,
RA   Bohme U., Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L.,
RA   Wickstead B., Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J.,
RA   Bringaud F., Brooks K., Carrington M., Cherevach I.,
RA   Chillingworth T.J., Churcher C., Clark L.N., Corton C.H., Cronin A.,
RA   Davies R.M., Doggett J., Djikeng A., Feldblyum T., Field M.C.,
RA   Fraser A., Goodhead I., Hance Z., Harper D., Harris B.R., Hauser H.,
RA   Hostetler J., Ivens A., Jagels K., Johnson D., Johnson J., Jones K.,
RA   Kerhornou A.X., Koo H., Larke N., Landfear S., Larkin C., Leech V.,
RA   Line A., Lord A., Macleod A., Mooney P.J., Moule S., Martin D.M.,
RA   Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA   Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E.,
RA   Rajandream M.A., Reitter C., Salzberg S.L., Sanders M., Schobel S.,
RA   Sharp S., Simmonds M., Simpson A.J., Tallon L., Turner C.M., Tait A.,
RA   Tivey A.R., Van Aken S., Walker D., Wanless D., Wang S., White B.,
RA   White O., Whitehead S., Woodward J., Wortman J., Adams M.D.,
RA   Embley T.M., Gull K., Ullu E., Barry J.D., Fairlamb A.H.,
RA   Opperdoes F., Barrell B.G., Donelson J.E., Hall N., Fraser C.M.,
RA   Melville S.E., El-Sayed N.M.A.;
RT   "The genome of the African trypanosome Trypanosoma brucei.";
RL   Science 309:416-422(2005).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS
RP   OF LYS-550 AND 657-ASP-GLU-658.
RX   PubMed=15694344; DOI=10.1016/j.molcel.2004.12.022;
RA   DiPaolo C., Kieft R., Cross M., Sabatini R.;
RT   "Regulation of trypanosome DNA glycosylation by a SWI2/SNF2-like
RT   protein.";
RL   Mol. Cell 17:441-451(2005).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17706299; DOI=10.1016/j.molbiopara.2007.06.010;
RA   Kieft R., Brand V., Ekanayake D.K., Sweeney K., DiPaolo C.,
RA   Reznikoff W.S., Sabatini R.;
RT   "JBP2, a SWI2/SNF2-like protein, regulates de novo telomeric DNA
RT   glycosylation in bloodstream form Trypanosoma brucei.";
RL   Mol. Biochem. Parasitol. 156:24-31(2007).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-391; ASP-393;
RP   HIS-441; ARG-455 AND VAL-459.
RX   PubMed=19136460; DOI=10.1093/nar/gkn1067;
RA   Cliffe L.J., Kieft R., Southern T., Birkeland S.R., Marshall M.,
RA   Sweeney K., Sabatini R.;
RT   "JBP1 and JBP2 are two distinct thymidine hydroxylases involved in J
RT   biosynthesis in genomic DNA of African trypanosomes.";
RL   Nucleic Acids Res. 37:1452-1462(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
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.
CC       {ECO:0000269|PubMed:15694344, ECO:0000269|PubMed:19136460}.
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:15694344,
CC         ECO:0000305|PubMed:19136460};
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:0000305|PubMed:15694344,
CC         ECO:0000305|PubMed:19136460};
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:0000269|PubMed:15694344,
CC       ECO:0000269|PubMed:19136460}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in bloodstream form.
CC       {ECO:0000269|PubMed:15694344}.
CC   -!- DISRUPTION PHENOTYPE: The genome contains reduced level of DNA
CC       base J in the DNA. Cells lacking both JBP1 and JBP2 show a
CC       complete absence of base J. {ECO:0000269|PubMed:17706299}.
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; AC159421; AAX69788.1; -; Genomic_DNA.
DR   RefSeq; XP_846088.1; XM_840995.1.
DR   SMR; Q57X81; -.
DR   STRING; 5691.AAZ12529; -.
DR   PaxDb; Q57X81; -.
DR   PRIDE; Q57X81; -.
DR   GeneDB; Tb927.7.4650:pep; -.
DR   GeneID; 3658676; -.
DR   KEGG; tbr:Tb927.7.4650; -.
DR   EuPathDB; TriTrypDB:Tb927.7.4650; -.
DR   InParanoid; Q57X81; -.
DR   KO; K22407; -.
DR   OMA; EMENDLP; -.
DR   BRENDA; 1.14.11.6; 6519.
DR   Proteomes; UP000008524; Chromosome 7.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IMP:UniProtKB.
DR   GO; GO:0070580; P:base J metabolic process; IMP:UniProtKB.
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   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Dioxygenase; DNA-binding; Helicase;
KW   Hydrolase; Iron; Metal-binding; Nucleotide-binding; Nucleus;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN         1   1077       Bifunctional helicase and thymine
FT                                dioxygenase JBP2.
FT                                /FTId=PRO_0000377562.
FT   DOMAIN      531    706       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      871   1032       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     544    551       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION        1    516       Thymine dioxygenase.
FT   REGION      517   1075       DNA Helicase.
FT   MOTIF       657    660       DEAH box.
FT   METAL       391    391       Iron; catalytic; for thymine dioxygenase
FT                                activity. {ECO:0000250|UniProtKB:Q6N021}.
FT   METAL       393    393       Iron; catalytic; for thymine dioxygenase
FT                                activity. {ECO:0000250|UniProtKB:Q6N021}.
FT   METAL       441    441       Iron; catalytic; for thymine dioxygenase
FT                                activity. {ECO:0000250|UniProtKB:Q6N021}.
FT   BINDING     455    455       2-oxoglutarate.
FT                                {ECO:0000250|UniProtKB:Q6N021}.
FT   MUTAGEN     391    391       H->A: Impairs DNA base J biosynthesis.
FT                                {ECO:0000269|PubMed:19136460}.
FT   MUTAGEN     393    393       D->A: Induces a slight reduction in DNA
FT                                base J biosynthesis.
FT                                {ECO:0000269|PubMed:19136460}.
FT   MUTAGEN     441    441       H->A: Impairs DNA base J biosynthesis.
FT                                {ECO:0000269|PubMed:19136460}.
FT   MUTAGEN     455    455       R->A: Impairs DNA base J biosynthesis.
FT                                {ECO:0000269|PubMed:19136460}.
FT   MUTAGEN     459    459       V->A: No effect.
FT                                {ECO:0000269|PubMed:19136460}.
FT   MUTAGEN     550    550       K->A: Impairs DNA base J biosynthesis.
FT                                {ECO:0000269|PubMed:15694344}.
FT   MUTAGEN     657    658       DE->AA: Impairs DNA base J biosynthesis.
FT                                {ECO:0000269|PubMed:15694344}.
SQ   SEQUENCE   1077 AA;  121447 MW;  F668A0CC55E144ED CRC64;
     MPMFMDGASQ VLQQVLQTVL VTSEPAIVIP GSFLGELDVI VDEAKNHGMK LVSIPKGGIT
     ILPPIPMSES SLTRLCKDYY GLKTDAERLA LFSNLEETFP TAPGVSLPCR LLYHPRDYIC
     RIVHLCAELV TASDEEYQKA YDIVPLLHIR PVQNVCEELR RQFRAGALTQ RLPLGQRVDV
     QFKRTVVHLD GSMDPFPRNA AEAAVNIAPV ALDAVDDIYE GFDVTGTEVV DIPTGKVSEY
     LSEKDFELVT EDSVLLDPTG KRVQAIFIRG GIDKDICRRA AADVEGVATK QNMRRLTNGG
     VRNPDTGILG YYDYLNNPTK RKCRMTEFTR RNWGKIIGPC GELLQLLDQL YKENAPDHYE
     LQRRVIPPEY MLFNTVFSTV SVNKNFRTAV HRDKGDFRGG LTALCVLDGN YEGCYLALKS
     ARKAFCLQVG DVLFFDSSLE HGNTEVHNRE GSWRRISIVC YLRCGLMSHT CETERSMRLR
     NQIMSDRLHA DSADSVVNLN GVTGHLPPLC IPFKIAKTLS LTQHAALRFV SRRIKEGDGC
     VLALTMGLGK TLVSLTICYS YIYNNGPCDI LIVAPKTLLQ HWMQEAKKWK DYGLVFPGFI
     VLNNVDSSSF EDDLSNYEQQ GTTTNPKKSY VFVINPGYIK SFLSRVKGFR PALIVVDEGH
     CISSKESKLR EVLDSLYCSA RVVLTGTPVQ NNAEELYRLV GWVDDKVHST LPQRDFNEFS
     NSINRYVNGD DSAFCDALFA QRYIHEWMSP YVFTVMKVDL PPLHDYIIIC NFSAVQQKMF
     EERIKVDATD NLLCLKASEH RPYHLSTHPL CFLGFLTGIW RTGQVDIEEE PGEFEELGTY
     RLSRDDDALA KDCSSLLENG KLADFVALSG KLTALISILH SIFEKMEKAV IFSQYIGSQD
     FIARTLTAYK ISVVTIRGKD CQQRRRRVVE MFRDDKNVLC LVVSTQIGAY GLDLTAANHV
     ILWDTWWNPQ VESQAIARCY RQNQSKAVIA YKLASGFEDA TVLKAQARKR ALFKCLINEE
     TSQVVPGHDL VDYTSSEEDD DRRHLWETLK TCTLEGGKPA VTKIIRNIDT VKSERWI
//
DBGET integrated database retrieval system