ID A0A1P8R040_9GAMM Unreviewed; 285 AA.
AC A0A1P8R040;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN ORFNames=BWR19_03135 {ECO:0000313|EMBL:APX92019.1};
OS Halomonas sp. 1513.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1883416 {ECO:0000313|EMBL:APX92019.1, ECO:0000313|Proteomes:UP000187327};
RN [1] {ECO:0000313|Proteomes:UP000187327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1513 {ECO:0000313|Proteomes:UP000187327};
RA Shuang W.;
RT "Complete genome sequence of Haloterrigena daqingensis type strain
RT (JX313T).";
RL Submitted (JAN-2017) 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; CP019326; APX92019.1; -; Genomic_DNA.
DR RefSeq; WP_076746455.1; NZ_CP019326.1.
DR AlphaFoldDB; A0A1P8R040; -.
DR STRING; 1883416.BWR19_03135; -.
DR KEGG; halo:BWR19_03135; -.
DR OrthoDB; 9807213at2; -.
DR Proteomes; UP000187327; 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 Reference proteome {ECO:0000313|Proteomes:UP000187327};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 6..64
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 250..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..285
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 285 AA; 32551 MW; CC32E076325938C0 CRC64;
MTTTTEKLQK VLARAGLGSR REMETAISAG RVKVNGKLAT LGDRIEIRDK VTFDDRPVTL
RGAEETPRRV IMYNKPEGEL CTRKDPEGRR TVFERLPRLK GERWIAIGRL DINTSGLLLF
TTDGELANKL MHPSTEVERE YAVRVMGEVR REHVVAMVEG VMLDDGPARF SDVQEFGGEG
INTWFHVVIL EGRNREVRRL WESQGLTVSR LKRVRYGNIF LDKRAKAGEW TELTQDEVDD
LASLAGLASR KVPELTPDEK NRWSRDKNKR RPVQAMRKPK GTRKS
//
