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Database: UniProt
Entry: Q87RM8_VIBPA
LinkDB: Q87RM8_VIBPA
Original site: Q87RM8_VIBPA 
ID   Q87RM8_VIBPA            Unreviewed;       371 AA.
AC   Q87RM8;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN   OrderedLocusNames=VP0750 {ECO:0000313|EMBL:BAC59013.1};
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC59013.1, ECO:0000313|Proteomes:UP000002493};
RN   [1] {ECO:0000313|EMBL:BAC59013.1, ECO:0000313|Proteomes:UP000002493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX   PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(2604) in 23S rRNA = pseudouridine(2604) in 23S rRNA;
CC         Xref=Rhea:RHEA:38875, Rhea:RHEA-COMP:10093, Rhea:RHEA-COMP:10094,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00036535};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(35) in tRNA(Tyr) = pseudouridine(35) in tRNA(Tyr);
CC         Xref=Rhea:RHEA:60556, Rhea:RHEA-COMP:15607, Rhea:RHEA-COMP:15608,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC         Evidence={ECO:0000256|ARBA:ARBA00036390};
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC       {ECO:0000256|ARBA:ARBA00008348, ECO:0000256|RuleBase:RU003887}.
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DR   EMBL; BA000031; BAC59013.1; -; Genomic_DNA.
DR   RefSeq; NP_797129.1; NC_004603.1.
DR   RefSeq; WP_005481361.1; NC_004603.1.
DR   AlphaFoldDB; Q87RM8; -.
DR   GeneID; 1188245; -.
DR   KEGG; vpa:VP0750; -.
DR   PATRIC; fig|223926.6.peg.717; -.
DR   eggNOG; COG1187; Bacteria.
DR   HOGENOM; CLU_024979_6_0_6; -.
DR   Proteomes; UP000002493; Chromosome 1.
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; cd02554; PseudoU_synth_RluF; 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:UP000002493};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT   DOMAIN          7..65
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   REGION          238..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..371
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   371 AA;  41830 MW;  1CF961FD3F0A50F2 CRC64;
     MSQDNAKRLN KFISETGFCS RRAADKLIEE GRVTINGKQP EMGTKVLPGD DVCVDGKPVA
     SKEKPIYIAL NKPTGITCTT ERDIPGNIVD FIGHKKRIFP IGRLDKPSDG LIFLTNDGDI
     VNKILRAGNN HEKEYVVRVD KPITDEFLKQ MSSGVRILDT VTLPCKVTKE TKFSFRIVLT
     QGLNRQIRRM CEALGYEVFK LRRVRIMNIS LDGIPNGKWR YLTDDEVAEI LAMCDGSVGT
     EEASKTDSRG RNIRKATDAK LFDSREENQG STARRNQKTR TFRGNNADEF RHAPNSKKGQ
     QKRRQRDDES SRPAKEHYKA KTQGEHAKPQ GEHGRPQNKP QTPSKPKQHY VNPNTTSKPA
     KRTSGTLSLK K
//
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