JBP2_TRYB2
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 03-AUG-2022, entry version 85.
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; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; 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., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., 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 OF
RP 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 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., Reznikoff W.S.,
RA 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 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: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, ECO:0000305|PubMed:19136460};
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:15694344, 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. {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 base J
CC in the DNA. Cells lacking both JBP1 and JBP2 show a complete absence of
CC 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. JBP2
CC subfamily. {ECO:0000305}.
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DR EMBL; AC159421; AAX69788.1; -; Genomic_DNA.
DR RefSeq; XP_846088.1; XM_840995.1.
DR AlphaFoldDB; Q57X81; -.
DR SMR; Q57X81; -.
DR STRING; 5691.AAZ12529; -.
DR PaxDb; Q57X81; -.
DR GeneID; 3658676; -.
DR KEGG; tbr:Tb927.7.4650; -.
DR VEuPathDB; TriTrypDB:Tb11.v5.0150; -.
DR VEuPathDB; TriTrypDB:Tb927.7.4650; -.
DR eggNOG; KOG1015; Eukaryota.
DR InParanoid; Q57X81; -.
DR OMA; QDLIHRT; -.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
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: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:0006283; P:transcription-coupled nucleotide-excision repair; IBA:GO_Central.
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;
KW Reference proteome.
FT CHAIN 1..1077
FT /note="Bifunctional helicase and thymine dioxygenase JBP2"
FT /id="PRO_0000377562"
FT DOMAIN 531..706
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 871..1032
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..516
FT /note="Thymine dioxygenase"
FT REGION 517..1075
FT /note="DNA Helicase"
FT MOTIF 657..660
FT /note="DEAH box"
FT BINDING 391
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 393
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 441
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 455
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 544..551
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 391
FT /note="H->A: Impairs DNA base J biosynthesis."
FT /evidence="ECO:0000269|PubMed:19136460"
FT MUTAGEN 393
FT /note="D->A: Induces a slight reduction in DNA base J
FT biosynthesis."
FT /evidence="ECO:0000269|PubMed:19136460"
FT MUTAGEN 441
FT /note="H->A: Impairs DNA base J biosynthesis."
FT /evidence="ECO:0000269|PubMed:19136460"
FT MUTAGEN 455
FT /note="R->A: Impairs DNA base J biosynthesis."
FT /evidence="ECO:0000269|PubMed:19136460"
FT MUTAGEN 459
FT /note="V->A: No effect."
FT /evidence="ECO:0000269|PubMed:19136460"
FT MUTAGEN 550
FT /note="K->A: Impairs DNA base J biosynthesis."
FT /evidence="ECO:0000269|PubMed:15694344"
FT MUTAGEN 657..658
FT /note="DE->AA: Impairs DNA base J biosynthesis."
FT /evidence="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
