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Database: UniProt
Entry: A0A1M7TI23_9RHOB
LinkDB: A0A1M7TI23_9RHOB
Original site: A0A1M7TI23_9RHOB 
ID   A0A1M7TI23_9RHOB        Unreviewed;       343 AA.
AC   A0A1M7TI23;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN   ORFNames=SAMN05216200_106191 {ECO:0000313|EMBL:SHN70377.1};
OS   Oceanicella actignis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Oceanicella.
OX   NCBI_TaxID=1189325 {ECO:0000313|EMBL:SHN70377.1, ECO:0000313|Proteomes:UP000184066};
RN   [1] {ECO:0000313|EMBL:SHN70377.1, ECO:0000313|Proteomes:UP000184066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10808 {ECO:0000313|EMBL:SHN70377.1,
RC   ECO:0000313|Proteomes:UP000184066};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000073};
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC       {ECO:0000256|ARBA:ARBA00008348, ECO:0000256|RuleBase:RU003887}.
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DR   EMBL; FRDL01000006; SHN70377.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M7TI23; -.
DR   STRING; 1189325.SAMN04488119_10612; -.
DR   OrthoDB; 9807213at2; -.
DR   Proteomes; UP000184066; 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; 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:SF3; RIBOSOMAL LARGE SUBUNIT PSEUDOURIDINE SYNTHASE B; 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:UP000184066};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          9..68
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   343 AA;  36966 MW;  7E50A68FFFA0D9E8 CRC64;
     MTSEKNEMER IARRLSRAGV ASRREAERMI AEGRVKVNGR RIDSPALNVG PDDRIEVDGQ
     PVAAPERPRL WRYHKPAGLV TSARDEKGRP TVFDSLPAEL PRVMSVGRLD LNSEGLLLLT
     NDGALKRRLE LPSTGWLRKY RVRVKGAPTP EALAPLERGV TVDGERFQPM VVTIDRQQGA
     NAWLTIGIRE GRNREIRRAL ESLGFLVNRL IRISYGPFQL GDLAPGAVEE IRPKVLREQL
     GIAIDPSDRA PAPPRPEGEA GQASAPAGKG ARRGRGLRGR EDGAPQGKAA RPASPAPAGK
     PGPAHKPRAP EGAKPRAPEG GAPDAHGRGG RGAPTGAGRR GRR
//
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