ID   G0UPJ0_TRYCI            Unreviewed;       618 AA.
AC   G0UPJ0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-NOV-2024, entry version 37.
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).
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DR   EMBL; HE575320; CCC91301.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0UPJ0; -.
DR   VEuPathDB; TriTrypDB:TcIL3000_7_1020; -.
DR   OrthoDB; 129900at2759; -.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:1990481; P:mRNA pseudouridine synthesis; IEA:TreeGrafter.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:InterPro.
DR   CDD; cd02568; PseudoU_synth_PUS1_PUS2; 1.
DR   Gene3D; 3.30.70.660; Pseudouridine synthase I, catalytic domain, C-terminal subdomain; 1.
DR   Gene3D; 3.30.70.580; Pseudouridine synthase I, catalytic domain, N-terminal subdomain; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR001406; PsdUridine_synth_TruA.
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   PANTHER; PTHR11142:SF4; PSEUDOURIDYLATE SYNTHASE 1 HOMOLOG; 1.
DR   SUPFAM; SSF55120; Pseudouridine synthase; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235}.
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"
FT   ACT_SITE        86
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR641708-1"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR641708-2"
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
//