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 05-DEC-2018, 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; DE Includes: DE RecName: Full=Thymine dioxygenase JBP2; DE EC=1.14.11.6; GN Name=JBP2; ORFNames=Tc00.1047053508859.74; OS Trypanosoma cruzi (strain CL Brener). OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma; OC 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., RA Aggarwal G., Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., RA Blandin G., Westenberger S.J., Caler E., Cerqueira G.C., Branche C., RA Haas B., Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., RA Bringaud F., Burton P., Cadag E., Campbell D.A., Carrington M., RA Crabtree J., Darban H., da Silveira J.F., de Jong P., Edwards K., RA Englund P.T., Fazelina G., Feldblyum T., Ferella M., Frasch A.C., RA Gull K., Horn D., Hou L., Huang Y., Kindlund E., Klingbeil M., RA Kluge S., Koo H., Lacerda D., Levin M.J., Lorenzi H., Louie T., RA Machado C.R., McCulloch R., McKenna A., Mizuno Y., Mottram J.C., RA Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M., Pentony M., RA Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L., RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., RA Simpson A.J., Sisk E., Tammi M.T., Tarleton R., Teixeira S., RA Van Aken S., Vogt C., Ward P.N., Wickstead B., Wortman J., White O., RA Fraser C.M., Stuart K.D., 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 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}. 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 -!- 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 -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. 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}. 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 ProteinModelPortal; Q4DCH3; -. DR SMR; Q4DCH3; -. DR STRING; 353153.XP_812080.1; -. DR PaxDb; Q4DCH3; -. DR PRIDE; Q4DCH3; -. DR EnsemblProtists; EAN90229; EAN90229; Tc00.1047053508859.74. DR GeneDB; TcCLB.508859.74:pep; -. DR GeneID; 3543167; -. DR KEGG; tcr:508859.74; -. DR eggNOG; KOG0387; Eukaryota. DR eggNOG; ENOG410XP4Z; LUCA. DR KO; K22407; -. 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:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050341; F:thymine dioxygenase activity; IEA:UniProtKB-EC. DR CDD; cd00079; HELICc; 1. 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 1086 Bifunctional helicase and thymine FT dioxygenase JBP2. FT /FTId=PRO_0000377563. FT DOMAIN 533 708 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 883 1041 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT NP_BIND 546 553 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT REGION 1 518 Thymine dioxygenase. FT REGION 519 1084 DNA Helicase. FT MOTIF 659 662 DEAH box. FT METAL 393 393 Iron; catalytic; for thymine dioxygenase FT activity. {ECO:0000250}. FT METAL 395 395 Iron; catalytic; for thymine dioxygenase FT activity. {ECO:0000250}. FT METAL 443 443 Iron; catalytic; for thymine dioxygenase FT activity. {ECO:0000250}. FT BINDING 457 457 2-oxoglutarate. {ECO:0000250}. 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 //