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Database: UniProt
Entry: D7E339_NOSA0
LinkDB: D7E339_NOSA0
Original site: D7E339_NOSA0 
ID   D7E339_NOSA0            Unreviewed;       329 AA.
AC   D7E339;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN   OrderedLocusNames=Aazo_3490 {ECO:0000313|EMBL:ADI65107.1};
OS   Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI65107.1, ECO:0000313|Proteomes:UP000001511};
RN   [1] {ECO:0000313|EMBL:ADI65107.1, ECO:0000313|Proteomes:UP000001511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0708 {ECO:0000313|EMBL:ADI65107.1,
RC   ECO:0000313|Proteomes:UP000001511};
RX   PubMed=20628610; DOI=10.1371/journal.pone.0011486;
RA   Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K.,
RA   Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.;
RT   "Genome erosion in a nitrogen-fixing vertically transmitted endosymbiotic
RT   multicellular cyanobacterium.";
RL   PLoS ONE 5:E11486-E11486(2010).
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; CP002059; ADI65107.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7E339; -.
DR   STRING; 551115.Aazo_3490; -.
DR   KEGG; naz:Aazo_3490; -.
DR   eggNOG; COG0564; Bacteria.
DR   HOGENOM; CLU_016902_4_4_3; -.
DR   Proteomes; UP000001511; 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; 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; 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; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|RuleBase:RU362028};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001511};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          33..98
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   ACT_SITE        157
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ   SEQUENCE   329 AA;  36519 MW;  0D08AA814AC96760 CRC64;
     MVQFPGFIRG VTQKSKIQNR MTVINLLVSQ NTQRLDLYLS SELQNLSRSR LQQLIEQGHV
     LLNDQVCTSK KVNVKVGDRI CVEIPSLQPL KLVAEDIPLD ILYEDEQLLI LNKPAGLVVH
     PAPGHLDGTL VNALLAHCAN LPGIGGVQRP GIVHRLDKDT TGAIAIAKTD IAYQHLQAQL
     QAKTARREYL GVVYGVPKTE SGIINLPISR HPQDRKKMAI VPTEQGGRTA ITHWQIRERL
     SNYTLIHFQL ETGRTHQIRV HSAKIGHPIV GDSVYGAGRS VGVNLAGHAL HAWQLKLQHP
     ISGDWIQVTA SPPQTFTTLL EVLRRRSER
//
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