ID A0A0J9BCC7_9GAMM Unreviewed; 303 AA.
AC A0A0J9BCC7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN ORFNames=AI28_01680 {ECO:0000313|EMBL:KMV70829.1};
OS bacteria symbiont BFo1 of Frankliniella occidentalis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae.
OX NCBI_TaxID=1628855 {ECO:0000313|EMBL:KMV70829.1, ECO:0000313|Proteomes:UP000037152};
RN [1] {ECO:0000313|EMBL:KMV70829.1, ECO:0000313|Proteomes:UP000037152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFo1 {ECO:0000313|EMBL:KMV70829.1,
RC ECO:0000313|Proteomes:UP000037152};
RA Facey P.D., Hitchings M.D., Hegarty M.J., Pachebat J.A., Morgan L.V.,
RA Hoeppner J.E., Whitten M.A., Dyson P.J., Del Sol R.;
RT "The draft genomes, genome evolution and classification of BFo1 and BFo2
RT two insect symbionts isolated from Western Flower Thrips (Frankliniella
RT occidentalis [Pergande]).";
RL Submitted (MAY-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMV70829.1}.
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DR EMBL; JMSO01000094; KMV70829.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J9BCC7; -.
DR STRING; 1628855.WB66_09585; -.
DR PATRIC; fig|1628855.3.peg.333; -.
DR Proteomes; UP000037152; Unassembled WGS sequence.
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; 3.30.2350.10; Pseudouridine synthase; 1.
DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
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 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 6..77
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 261..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 303 AA; 33898 MW; 5C722FE328D32A1B CRC64;
MSDKSEKLQK VLARAGHGSR REIETMISAG RVSVDGKLAT LGDRVEPSAS MKIRIDGHVV
PVSESITEVC RVLAYYKPEG ELCTRNDPEG RPTVFDRLPK LRGARWIAVG RLDVNTCGLL
LFTTDGELAN RLMHPSREVE REYAVRVFGA VDDDKIKQLS RGVQLEDGPA AFKTLKFTGG
EGINQWYNVT LTEGRNREVR RLWEAVGVQV SRLIRVRYGD IDLPKGLPRG GWTELELGPT
NYLRELVGLD AETVSKVAVE KDRRRTKANQ IRRAVKRHTT TAKASKPGSN RRPTKSSKRQ
QQG
//
