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Database: UniProt
Entry: F1W4C5_9BURK
LinkDB: F1W4C5_9BURK
Original site: F1W4C5_9BURK 
ID   F1W4C5_9BURK            Unreviewed;       621 AA.
AC   F1W4C5;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN   ORFNames=IMCC9480_1745 {ECO:0000313|EMBL:EGF30293.1};
OS   Oxalobacteraceae bacterium IMCC9480.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae.
OX   NCBI_TaxID=937450 {ECO:0000313|EMBL:EGF30293.1, ECO:0000313|Proteomes:UP000004494};
RN   [1] {ECO:0000313|EMBL:EGF30293.1, ECO:0000313|Proteomes:UP000004494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC9480 {ECO:0000313|EMBL:EGF30293.1,
RC   ECO:0000313|Proteomes:UP000004494};
RX   PubMed=21572000; DOI=10.1128/JB.05088-11;
RA   Oh H.M., Lee K., Jang Y., Kang I., Kim H.J., Kang T.W., Kim S.Y., Cho J.C.;
RT   "Genome sequence of strain IMCC9480, a xanthorhodopsin-bearing
RT   betaproteobacterium isolated from the Arctic Ocean.";
RL   J. Bacteriol. 193:3421-3421(2011).
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC       {ECO:0000256|ARBA:ARBA00008348, ECO:0000256|RuleBase:RU003887}.
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:EGF30293.1}.
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DR   EMBL; AEPR01000778; EGF30293.1; -; Genomic_DNA.
DR   AlphaFoldDB; F1W4C5; -.
DR   Proteomes; UP000004494; 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; cd02556; PseudoU_synth_RluB; 1.
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:UP000004494};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          207..268
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   REGION          1..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..471
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   621 AA;  65648 MW;  5BBC837D2D4250F2 CRC64;
     MNPPKPNDDS TIDAIPAASA EPKVPRKRTP RAKPPVQAVA EASAAPAIAT VASGEPAAPS
     MSLSSTPDAA AAPRRNVRGP RNLRRTRDPV ERNAVAQDGT AVVAQEGAPD PAQPAQVRPP
     RQHAPREARP RSNEDRPKGQ GGAQKSRQKQ PAGNAARNAP RGTDADSVFS FVTSAAFDDS
     TGDEPGNGRS PAAKVVRRDL TADDDAPKLH KVLAEAGLGS RRDMEELIIS GRVSVNGEPA
     HIGQRILAQD QVRINGKLIQ RRVSKKPPRV LVYHKPAGEI VSHDDPDGRP SVFERLPNMK
     AGKWLAVGRL DFNTEGLLLF TTSGDLANRL MHPRYNIDRE YAVRTLGELE EGMRQKLLAG
     VELDDGVAQF SRVADGGGEG VNKWYRVTIG EGRNREVRRM FEAIGLTVSR LIRTRYGAMV
     LPPNLKRGRW EEMDEHSVRD LLKISGLEKT VGKSEPSRGR SDEHDSEGGV NGNRIERAPA
     TARHGAPNGN RANAPEPGQW QGKGRSGPAR GPGGFAGQGQ PRGPGAYPAQ GQGGQGQGRG
     APAKARSRQP DPMQTALGFP GMGQPRRSNG PRGPGQGGQG GQGRGGQGGF GGNQGGNQGG
     GQGGFGGNQG GPGGQRRRSR G
//
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