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Database: UniProt
Entry: A0A150UCW0_9BRAD
LinkDB: A0A150UCW0_9BRAD
Original site: A0A150UCW0_9BRAD 
ID   A0A150UCW0_9BRAD        Unreviewed;       687 AA.
AC   A0A150UCW0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN   ORFNames=SE92_18810 {ECO:0000313|EMBL:KYG22036.1};
OS   Bradyrhizobium sp. AT1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=574934 {ECO:0000313|EMBL:KYG22036.1, ECO:0000313|Proteomes:UP000075342};
RN   [1] {ECO:0000313|EMBL:KYG22036.1, ECO:0000313|Proteomes:UP000075342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AT1 {ECO:0000313|EMBL:KYG22036.1,
RC   ECO:0000313|Proteomes:UP000075342};
RA   Okubo T., Minamisawa K.;
RT   "Evolution of nitrogen fixation genes.";
RL   Submitted (JAN-2015) 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}.
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:KYG22036.1}.
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DR   EMBL; JXDL01000001; KYG22036.1; -; Genomic_DNA.
DR   RefSeq; WP_063197333.1; NZ_JXDL01000001.1.
DR   AlphaFoldDB; A0A150UCW0; -.
DR   STRING; 574934.SE92_18810; -.
DR   PATRIC; fig|574934.3.peg.3989; -.
DR   Proteomes; UP000075342; 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   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          369..428
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   REGION          1..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          615..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..369
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..664
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   687 AA;  78796 MW;  BE91DED5448F8CCC CRC64;
     MPRDSDKDND SRGRRGPARG PSKGGRSGKA RGPEKKFAKR GFEGKSEGDK RPPRGDRDSR
     PPRADRGDRP FRRREEGDAP RRDFSDRPKF KRDDRGSEGR GERSFKPRGD RPFSDSSSRD
     GEKRPFKPRG DRPSFGRDDR PPRRDRDDAR PAGRSSDRKF GDKKPYAPRG DRPERKFDGE
     RKFSRGGPRE DRGERSFKPR GDRPNFDRGD RPPRGDRPER KFDGERKFSR GAPDRDRGDR
     GPRKDFGGRD RGADKPWQKR DDRREGGRGD DRPRFSRARD DRPSGDRPFR DRPKFDRPRE
     RPEGRSDWHE HPRNEGRFGD RPRRENEDES RIFEKRPAFG GRGAYRERDR DSDRRPRREE
     EPKPKKAGER IAKALARAGL ASRRDAEEMV TQGRVTVNGR VINSPALDIT KNDVVLVDGK
     PLPERERTRL FLYHKPRGLM TTHDDPEGRP TVFDNLPEGL PRLISVGRLD FNTEGLLLLT
     NDGGLARTLE LPDTGWLRRY RVRAHGDVTQ AQLDALKDGV EIEGVKYGPI DATLERDQGA
     NVWLVFAIRE GKNREVRNVC AHLGLEVNRL IRVSYGPFQL GEVPEGQVEE IKSRVLREQL
     GDKIIEKSGA QFDVPSKASR VEDAPSEKKP ASKRGVIADR KGRRVLVQRT GSEEARERNE
     EQASGYGPPR RPKRGYHGKR DLTPRED
//
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