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 //