ID A0A2J9DZ53_9GAMM Unreviewed; 234 AA.
AC A0A2J9DZ53;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN ORFNames=A6J60_007955 {ECO:0000313|EMBL:PNK60817.1};
OS Psychrobacter sp. FDAARGOS_221.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1975705 {ECO:0000313|EMBL:PNK60817.1, ECO:0000313|Proteomes:UP000217719};
RN [1] {ECO:0000313|Proteomes:UP000217719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_221 {ECO:0000313|Proteomes:UP000217719};
RA Hoffmann M., Allard M., Evans P., Brown E., Tallon L., Sadzewicz L.,
RA Sengamalay N., Ott S., Godinez A., Nagaraj S., Vavikolanu K.,
RA Aluvathingal J., Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-516 in
CC 16S ribosomal RNA. {ECO:0000256|ARBA:ARBA00037590}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(516) in 16S rRNA = pseudouridine(516) in 16S rRNA;
CC Xref=Rhea:RHEA:38867, Rhea:RHEA-COMP:10089, Rhea:RHEA-COMP:10090,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.19;
CC Evidence={ECO:0000256|ARBA:ARBA00036749};
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:PNK60817.1}.
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DR EMBL; NWFK02000001; PNK60817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J9DZ53; -.
DR OrthoDB; 9807213at2; -.
DR Proteomes; UP000217719; 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; cd02553; PseudoU_synth_RsuA; 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:SF4; PSEUDOURIDINE SYNTHASE; 1.
DR PANTHER; PTHR47683; PSEUDOURIDINE SYNTHASE FAMILY PROTEIN-RELATED; 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 1..65
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
SQ SEQUENCE 234 AA; 26168 MW; ABE4984ABF4D686D CRC64;
MRLDKFISKA TELSRKEAKK VLHASEITVN DKVVKDGSLH VDVLNDEVMW AGEPLSVAAG
SRYLLLYKPE GFECTLKPKE YPIVTELIAV PELDSLRIAG RLDVDTTGAL ILSDDGRWLH
RVTSPKHLHE KVYELTLADP MSEEEQAHAV KKVGQGILLD GDFEPTKPAT LEFIDDTHAR
LILTEGKYHQ VKRMMGYFGN KVTELHRASI GGITLEGLEK GESRFLTEEE VASF
//
