ID A0A494SW09_9NOCA Unreviewed; 374 AA.
AC A0A494SW09;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN ORFNames=D8W71_17965 {ECO:0000313|EMBL:AYJ49869.1};
OS Rhodococcus sp. P1Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1302308 {ECO:0000313|EMBL:AYJ49869.1, ECO:0000313|Proteomes:UP000277147};
RN [1] {ECO:0000313|Proteomes:UP000277147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1Y {ECO:0000313|Proteomes:UP000277147};
RA Belimov A., Safronova V.I., Ismailov T.;
RT "Complete genome sequence of the abscisic acid utilizing strain Rhodococcus
RT sp. P1Y.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000277147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1Y {ECO:0000313|Proteomes:UP000277147};
RA Nikolaichik Y.A., Gogoleva N.E., Khlopko Y.A., Gogolev Y.V.;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC {ECO:0000256|ARBA:ARBA00008348, ECO:0000256|RuleBase:RU003887}.
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DR EMBL; CP032762; AYJ49869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494SW09; -.
DR KEGG; rhop:D8W71_17965; -.
DR OrthoDB; 9807213at2; -.
DR Proteomes; UP000277147; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0120159; F:rRNA pseudouridine synthase activity; IEA:UniProt.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IEA:UniProt.
DR CDD; cd02870; PseudoU_synth_RsuA_like; 1.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.30.70.1560; Alpha-L RNA-binding motif; 1.
DR Gene3D; 3.30.70.580; Pseudouridine synthase I, catalytic domain, N-terminal subdomain; 1.
DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR InterPro; IPR042092; PsdUridine_s_RsuA/RluB/E/F_cat.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR InterPro; IPR000748; PsdUridine_synth_RsuA/RluB/E/F.
DR InterPro; IPR018496; PsdUridine_synth_RsuA/RluB_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR NCBIfam; TIGR00093; pseudouridine synthase; 1.
DR PANTHER; PTHR47683; PSEUDOURIDINE SYNTHASE FAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR47683:SF2; S4 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00849; PseudoU_synth_2; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM00363; S4; 1.
DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR PROSITE; PS01149; PSI_RSU; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU003887};
KW Reference proteome {ECO:0000313|Proteomes:UP000277147};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 134..195
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 41143 MW; 2B56A7CE6258120F CRC64;
MNKPARRDGT PDRNKRQAPG RKPTAGRSED PRENRRGKDA PRGARAESPR GGRRAAAPRK
GADQRKPFED KPVDSGINDR SNDAVPRKKP SRPKPPKPQK KQTPSTTISN AKPAKHQYAE
PDSKRRHVPR GEGVRLQKVL AQAGVASRRA AEELIADGRV EVDGRIVTEQ GIRIDPDVAI
VRVDGTRIVV KEELVHLAMN KPRGWQCTMS DDLGRPCVGD IVSERVQAGQ RLFHVGRLDA
DTEGLLLFTN DGDLAHRLMH PSYEVSKTYL ATLFGAIPRD LGKKLRDGIT LDDGPVKVDG
FSLLDISNGL SLVKITLHEG RKHIVRRLFD QVGFPVGRLV RTDVGNIALG DQRPGTLRVL
GRGEIGKLYE SVGL
//
