ID A0A0A7JM41_9PSED Unreviewed; 360 AA.
AC A0A0A7JM41;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN ORFNames=NJ69_11340 {ECO:0000313|EMBL:AIZ33537.1};
OS Pseudomonas parafulva.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=157782 {ECO:0000313|EMBL:AIZ33537.1, ECO:0000313|Proteomes:UP000030632};
RN [1] {ECO:0000313|EMBL:AIZ33537.1, ECO:0000313|Proteomes:UP000030632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRS01-1 {ECO:0000313|EMBL:AIZ33537.1,
RC ECO:0000313|Proteomes:UP000030632};
RA Liu Q.;
RT "Genome sequence of Pseudomonas parafulva CRS01-1, an antagonistic
RT bacterium isolated from rice field.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-2605
CC in 23S ribosomal RNA. {ECO:0000256|ARBA:ARBA00037383}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(2605) in 23S rRNA = pseudouridine(2605) in 23S rRNA;
CC Xref=Rhea:RHEA:42520, Rhea:RHEA-COMP:10095, Rhea:RHEA-COMP:10096,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.22;
CC Evidence={ECO:0000256|ARBA:ARBA00036944};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC {ECO:0000256|ARBA:ARBA00008348, ECO:0000256|RuleBase:RU003887}.
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DR EMBL; CP009747; AIZ33537.1; -; Genomic_DNA.
DR RefSeq; WP_039579097.1; NZ_CP009747.1.
DR AlphaFoldDB; A0A0A7JM41; -.
DR KEGG; ppv:NJ69_11340; -.
DR eggNOG; COG1187; Bacteria.
DR Proteomes; UP000030632; 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; cd02556; PseudoU_synth_RluB; 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:SF3; RIBOSOMAL LARGE SUBUNIT PSEUDOURIDINE SYNTHASE B; 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 RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 17..74
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 275..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 360 AA; 40505 MW; 403EACBFCE6C51E4 CRC64;
MSDKDLQETQ PTPPSGEKLQ KVLARIGVGS RRDVEAWISQ GRIKVNGVAA TLGQRVDLHD
AIAVDGKLIK REEAAEATRR VIMYNKPDGE ICTRDDPEGR PTVFDRLPRP KEGRWINIGR
LDINTTGLLL FTTDGELANR LMHPSYEMDR EYAVRVRGEV DDEMIDRLKA GVMLEDGPAK
FTDIQKAPGG EGFNHWYHCV VMEGRNREVR RLWESQGMVV SRLKRVRFGP VFLNSDLPMG
RWREMSQGEI DILAAEVGLQ PVALPTLNLK AKDKLERLQR KSTRPLGRGE RVRNLRPAQE
AGERQPREAA ERPARPVREE APRKGNRGSA VAERPSEMRK RATKPGADKP AGRGRGKPRG
//