ID   JBP2_TRYCC              Reviewed;        1086 AA.
AC   Q4DCH3;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 74.
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:Q57X81};
DE   Includes:
DE     RecName: Full=Thymine dioxygenase JBP2;
DE              EC=1.14.11.6 {ECO:0000250|UniProtKB:Q57X81};
GN   Name=JBP2; ORFNames=Tc00.1047053508859.74;
OS   Trypanosoma cruzi (strain CL Brener).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=353153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL Brener;
RX   PubMed=16020725; DOI=10.1126/science.1112631;
RA   El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA   Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA   Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA   Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA   Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA   da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA   Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA   Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA   Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA   Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA   Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA   Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA   Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA   Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA   Andersson B.;
RT   "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT   disease.";
RL   Science 309:409-415(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 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 (By similarity). {ECO:0000250|UniProtKB:Q57X81}.
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:Q57X81};
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:0000250|UniProtKB:Q57X81};
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:0000250|UniProtKB:Q57X81}.
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; AAHK01000656; EAN90229.1; -; Genomic_DNA.
DR   RefSeq; XP_812080.1; XM_806987.1.
DR   AlphaFoldDB; Q4DCH3; -.
DR   SMR; Q4DCH3; -.
DR   STRING; 5693.XP_812080.1; -.
DR   PaxDb; Q4DCH3; -.
DR   PRIDE; Q4DCH3; -.
DR   EnsemblProtists; EAN90229; EAN90229; Tc00.1047053508859.74.
DR   GeneID; 3543167; -.
DR   KEGG; tcr:508859.74; -.
DR   eggNOG; KOG0390; Eukaryota.
DR   OMA; QDLIHRT; -.
DR   OrthoDB; 74004at2759; -.
DR   Proteomes; UP000002296; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
DR   GO; GO:0070580; P:base J metabolic process; IEA:UniProt.
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   3: Inferred from homology;
KW   ATP-binding; Dioxygenase; DNA-binding; Helicase; Hydrolase; Iron;
KW   Metal-binding; Nucleotide-binding; Nucleus; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..1086
FT                   /note="Bifunctional helicase and thymine dioxygenase JBP2"
FT                   /id="PRO_0000377563"
FT   DOMAIN          533..708
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          883..1041
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..518
FT                   /note="Thymine dioxygenase"
FT   REGION          187..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..1084
FT                   /note="DNA Helicase"
FT   MOTIF           659..662
FT                   /note="DEAH box"
FT   COMPBIAS        192..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         395
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         443
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         457
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         546..553
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1086 AA;  122630 MW;  ACDD7E746BDE89DE CRC64;
     MPVPSHVSVA TLQSVLQTVC STGEPAIIAP SSFLGELDTV VDEVKRHGMK LASIPHGGIT
     ILPPVPISGT ELFDFCAEYC KAQTHEERLA VRHKINNHNF LMQDPLLRMP CRQLYNPADY
     VLRIVHLCSE LVSASEEEYH GAYGVAPLLH INPVQDVCGK LRSMFQSGSL YVKPWILEEE
     EERREMDESN RGVLFNSDSF GNGRGGSSIS SSERSVDEND VADEDLTGEE VVDNATDTVV
     EYLSEKDFDV VTESGIFYDD SGERVHAIYL RGGIKKELCQ RAAIAIEEAA TTKNLRKAVN
     GGKTNPETGI VGYYDYLNNP TQRKCRETEF TRKNWSSVVD SCEPFLVALN KLYSECAPTH
     YKLQRIAIPH HYQLFNTVFS TMTVNRNFRT AVHTDRGDFR SGLAALCVID GVFEGCHLAI
     KKLGKAFRLE TGDVLFFDTS LEHGNTEVHN FDYCWKRVSV VCYLRNGLMS QICEMERRRW
     LQKQMLKQRL LDRSRQSVIN LNATDPNLPP IYLPGRLLEV LSPVQQAALG FVVDRLSKGN
     GCVIALTMGL GKTLLSLALC YSHMYDQNPR DVLILAPKIV LTHWTGEKQK WEKYGLVFSH
     FVVSDGTDSV SFEIALKRYK QQLNGELPRT SHVFVINPEY IRTVLKKLTG FRPSLIIVDE
     GHRVSSKGSK LKDWLEGLRC TARVILSGTP VQNNAEELYR LIGWINSDVH SVLPPRVFTD
     LAGTINRYIN GDDSALAAAV SAQRYIQEWM CSYVFSVMKT DLPPLNDYII ICGFSSIQRK
     MLEDHFGMEG IDGLTSIKAS EHRPYHLSTH PLCFLGFISG VYKSLNGNHK LTPEAEEELE
     SQEYASQLYS LTEDDIGLID ECLSLVNSGF LTEFVGLSGK MTVLISILHS IREKKEKAII
     FSQYVGSQDF ISRTLTSFDI VSSTIRGRDC HERRRRTIEK FREDEKITCL LLSTQIGAYG
     LDFTAANHVI LWDSWWNPQV ESQAIARAYR RNQTRAVIVY RLASEFEDTI VLKTQIRKLA
     LFRCIMNEEA SRAVPPEELL DCVDTEEDEG RRFLWRSLKK SYLEGGAPAV SKVFRHGDTV
     RSESWS