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Database: UniProt
Entry: A0A285CLT3_9RHOB
LinkDB: A0A285CLT3_9RHOB
Original site: A0A285CLT3_9RHOB 
ID   A0A285CLT3_9RHOB        Unreviewed;       345 AA.
AC   A0A285CLT3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN   ORFNames=SAMN05878503_102160 {ECO:0000313|EMBL:SNX68510.1};
OS   Cereibacter ovatus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=439529 {ECO:0000313|EMBL:SNX68510.1, ECO:0000313|Proteomes:UP000219467};
RN   [1] {ECO:0000313|Proteomes:UP000219467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA234 {ECO:0000313|Proteomes:UP000219467};
RA   Varghese N., Submissions S.;
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil at
CC       positions 955, 2504 and 2580 in 23S ribosomal RNA.
CC       {ECO:0000256|ARBA:ARBA00002876}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a uridine in RNA = a pseudouridine in RNA;
CC         Xref=Rhea:RHEA:48348, Rhea:RHEA-COMP:12068, Rhea:RHEA-COMP:12069,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC         Evidence={ECO:0000256|RuleBase:RU362028};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(955/2504/2580) in 23S rRNA =
CC         pseudouridine(955/2504/2580) in 23S rRNA; Xref=Rhea:RHEA:42528,
CC         Rhea:RHEA-COMP:10099, Rhea:RHEA-COMP:10100, ChEBI:CHEBI:65314,
CC         ChEBI:CHEBI:65315; EC=5.4.99.24;
CC         Evidence={ECO:0000256|ARBA:ARBA00000381};
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC       {ECO:0000256|ARBA:ARBA00010876, ECO:0000256|RuleBase:RU362028}.
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DR   EMBL; OAOQ01000002; SNX68510.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285CLT3; -.
DR   OrthoDB; 9807829at2; -.
DR   Proteomes; UP000219467; 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; cd02869; PseudoU_synth_RluA_like; 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; IPR006224; PsdUridine_synth_RluA-like_CS.
DR   InterPro; IPR006225; PsdUridine_synth_RluC/D.
DR   InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   NCBIfam; TIGR00005; rluA_subfam; 1.
DR   PANTHER; PTHR21600; MITOCHONDRIAL RNA PSEUDOURIDINE SYNTHASE; 1.
DR   PANTHER; PTHR21600:SF93; PSEUDOURIDYLATE SYNTHASE RPUSD4, MITOCHONDRIAL; 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; PS01129; PSI_RLU; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|RuleBase:RU362028};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219467};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          15..72
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   ACT_SITE        142
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ   SEQUENCE   345 AA;  38300 MW;  3F509E552C3122FD CRC64;
     MSVQLLKVTA DEGEQRLDRW FKRRFPHLTQ GAVEKMCRTG QVRVDGARAK ASDRVAEGME
     IRVPPLPDPD APRPDAPRIT KSDEQMIQDC VIYKDNDIIV LNKPAGLPSQ GGSGQGERHV
     DGLTEALKFG YKERPKLVHR LDKDTSGVLV LARTDRVARA LSESFRHRNT RKIYWALVAG
     VPTPKQGSIK YALMKAPGHG RGGEGEKMLC IHPAKVADYP EAKRAQTDFF TLWFLGTRCA
     WMALSPITGR THQLRAHMAE LGHPIVGDGK YGGSGQENLG DGWGANLGGE ISRKLHLHAR
     SLTVEHPIRK EPVTFTAPLP PHMVKTWKLL DWKEGDVPED PFGGR
//
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