ID G0UPJ0_TRYCI Unreviewed; 618 AA. AC G0UPJ0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-DEC-2022, entry version 30. DE SubName: Full=Putative pseudouridylate synthase I {ECO:0000313|EMBL:CCC91301.1}; GN ORFNames=TCIL3000_7_1020 {ECO:0000313|EMBL:CCC91301.1}; OS Trypanosoma congolense (strain IL3000). OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas. OX NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCC91301.1}; RN [1] {ECO:0000313|EMBL:CCC91301.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IL3000 {ECO:0000313|EMBL:CCC91301.1}; RX PubMed=22331916; DOI=10.1073/pnas.1117313109; RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P., RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J., RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A., RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D., RA Hertz-Fowler C., Berriman M.; RT "Antigenic diversity is generated by distinct evolutionary mechanisms in RT African trypanosome species."; RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012). CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family. CC {ECO:0000256|ARBA:ARBA00009375}. 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; HE575320; CCC91301.1; -; Genomic_DNA. DR AlphaFoldDB; G0UPJ0; -. DR VEuPathDB; TriTrypDB:TcIL3000_7_1020; -. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt. DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:InterPro. DR CDD; cd02568; PseudoU_synth_PUS1_PUS2; 1. DR Gene3D; 3.30.70.580; -; 1. DR Gene3D; 3.30.70.660; -; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf. DR InterPro; IPR001406; PsdUridine_synth_TruA. DR InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom. DR InterPro; IPR020095; PsdUridine_synth_TruA_C. DR InterPro; IPR041708; PUS1/PUS2-like. DR InterPro; IPR020094; TruA/RsuA/RluB/E/F_N. DR PANTHER; PTHR11142; PSEUDOURIDYLATE SYNTHASE; 1. DR Pfam; PF01416; PseudoU_synth_1; 1. DR SUPFAM; SSF55120; Pseudouridine synthase; 1. PE 3: Inferred from homology; KW Isomerase {ECO:0000256|ARBA:ARBA00023235}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}. FT DOMAIN 218..347 FT /note="PseudoU_synth_1" FT /evidence="ECO:0000259|Pfam:PF01416" FT REGION 497..560 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 497..516 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 517..552 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 618 AA; 68869 MW; F3B8CB98AB2E9D06 CRC64; MGRWKPFNTR RACLRKAPEN HTLIGLCVMY CGTSYRGLQL QTHAPTHHTV EGVLIQALKD AGIVDGLHRG RVSGDAHRFA RSCRTDRGVH AVRNLICLFV DNGRLESAGG CRCLPQKLNA LLPSTIRVAH ATQLMGDFVP RFCCDRRVYR YMIPAYALMS PCTSWEEFYT KFPGSNELLQ HRALGSDFVD FCPGREEAGT FLSVLGDVVS RGNDLLLRHI VGTHFFHNFS VSINERAGGG GGWNKKVILP DDNTAVRSVI RCEIATRLFL LKQGEVGPTI KEYEAFLETA ESGSGTAAET RTLGKLHFDG APLPFVVFQI EGRSFLFNMI RKIVGLTLAV LRGARETLFE EVLSREWQAN CPLAPSPYLL LFQSFYGSYD RKARLRASDR FRPLEDEWSG EVVQKAGLFT FANIAADIVD LDLNRVPALG TMLSARDAQR RITRPSCVEE DSHLGEMKEF HPAVLEPHPV CSEMTLFLRS LRVHNWGLLS VKKPVKSNLS TSSATKNSCT STAEKLGVKR QRSEDGEMDE IPAKMSHKEE EGDGRNEDAD STEFVRGAPA SKEVDDGWLY VASTPEEECR LRSDYQRRVQ MLQSNKRVSS ARFACETLLQ SGDGGGSE //