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Database: UniProt
Entry: A0A1I4QPU7_9ACTN
LinkDB: A0A1I4QPU7_9ACTN
Original site: A0A1I4QPU7_9ACTN 
ID   A0A1I4QPU7_9ACTN        Unreviewed;       322 AA.
AC   A0A1I4QPU7;
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=SAMN04487980_1001156 {ECO:0000313|EMBL:SFM41723.1};
OS   Streptomyces sp. cf124.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1761903 {ECO:0000313|EMBL:SFM41723.1, ECO:0000313|Proteomes:UP000198530};
RN   [1] {ECO:0000313|EMBL:SFM41723.1, ECO:0000313|Proteomes:UP000198530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF124 {ECO:0000313|EMBL:SFM41723.1,
RC   ECO:0000313|Proteomes:UP000198530};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil.
CC       {ECO:0000256|RuleBase:RU362028}.
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   -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC       {ECO:0000256|ARBA:ARBA00010876, ECO:0000256|RuleBase:RU362028}.
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DR   EMBL; FOUV01000001; SFM41723.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4QPU7; -.
DR   Proteomes; UP000198530; 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:SF44; PSEUDOU_SYNTH_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00849; PseudoU_synth_2; 1.
DR   Pfam; PF01479; 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   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          27..70
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|Pfam:PF01479"
FT   DOMAIN          101..255
FT                   /note="Pseudouridine synthase RsuA/RluA-like"
FT                   /evidence="ECO:0000259|Pfam:PF00849"
FT   ACT_SITE        151
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ   SEQUENCE   322 AA;  34937 MW;  4F565F94AC1CBC87 CRC64;
     MAVRHTRRVS TIPEIRTLPV PDGLEGERVD AAISRMFGFS RTKAAELAAA GKVTVDGSVV
     GKSERVHGGA WLEVEMPQAP APVQVVAEPV EGMEIVHDDD DVVVIVKPVG VAAHPSPGWS
     GPTVIGGLAA AGYRISTSGA AERQGIVHRL DVGTSGLMVV AKSEYAYTSL KRQFKERTVD
     KRYHALVQGH PDPTSGTIDA PIGRHPNHDY KWAVTAEGKP SVTHYDLIEA FRAASLLDIK
     LETGRTHQIR VHMSAHRHPC VGDLTYGADP TLAKRLGITR QWLQAVRLGF EHPGDGSWVE
     FESDYPADLQ TALDKVREET YA
//
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