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Database: UniProt
Entry: A0A2S4N8F5_9FLAO
LinkDB: A0A2S4N8F5_9FLAO
Original site: A0A2S4N8F5_9FLAO 
ID   A0A2S4N8F5_9FLAO        Unreviewed;       345 AA.
AC   A0A2S4N8F5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN   ORFNames=Q361_10630 {ECO:0000313|EMBL:POS01968.1};
OS   Flavobacterium croceum DSM 17960.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1121886 {ECO:0000313|EMBL:POS01968.1, ECO:0000313|Proteomes:UP000237056};
RN   [1] {ECO:0000313|EMBL:POS01968.1, ECO:0000313|Proteomes:UP000237056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17960 {ECO:0000313|EMBL:POS01968.1,
RC   ECO:0000313|Proteomes:UP000237056};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase I: the one thousand microbial
RT   genomes (KMG-I) project.";
RL   Submitted (JAN-2018) 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}.
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:POS01968.1}.
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DR   EMBL; PQNY01000006; POS01968.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4N8F5; -.
DR   OrthoDB; 9807829at2; -.
DR   Proteomes; UP000237056; 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   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:UP000237056};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          29..88
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   ACT_SITE        152
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ   SEQUENCE   345 AA;  39477 MW;  A7D2A5B4595B82BF CRC64;
     MNSFIDTQDL EEELFEHHRF EVPKGQAMLR IDKYLMQVLP NTTRNKIQNA ASNGDVYVND
     TPVKSNYKVK PFDIVKILLA HPPYENRIDP ENIPLEIVYE DDELIVLNKP AGLVVHPGHG
     NYTGTLVNGL AFHFQNLPMN SSNRPGLVHR IDKNTSGLLV VAKTEYAMSF LAKQFEEKTT
     EREYIALVWG NVKEDSGTIT GNIARHVKDR MQMAVFPDGD VGKHAVTHYK VLERLGYVTL
     VSCKLETGRT HQIRVHMKYI GHTLFNDERY GGNLILKGTT FTKYKQFVEN CFKILPRQAL
     HARTLGFLHP TTGAFLKFEC DIPNDMLECI DKWRNYAKNI TVDEE
//
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