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Database: UniProt
Entry: A0A3P2A207_9BACE
LinkDB: A0A3P2A207_9BACE
Original site: A0A3P2A207_9BACE 
ID   A0A3P2A207_9BACE        Unreviewed;       488 AA.
AC   A0A3P2A207;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN   ORFNames=EII33_10745 {ECO:0000313|EMBL:RRD89028.1};
OS   Bacteroides heparinolyticus.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=28113 {ECO:0000313|EMBL:RRD89028.1, ECO:0000313|Proteomes:UP000279562};
RN   [1] {ECO:0000313|EMBL:RRD89028.1, ECO:0000313|Proteomes:UP000279562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OH1047_COT-310 {ECO:0000313|EMBL:RRD89028.1,
RC   ECO:0000313|Proteomes:UP000279562};
RA   Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA   Eisen J.A., Holcombe L.J., O'Flynn C.;
RT   "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT   for Automated Genome-Based Taxonomic Assignment.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:RRD89028.1}.
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DR   EMBL; RQYF01000061; RRD89028.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P2A207; -.
DR   Proteomes; UP000279562; 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; cd02870; PseudoU_synth_RsuA_like; 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:SF2; S4 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; 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:UP000279562};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          253..320
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   REGION          1..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   488 AA;  56305 MW;  C682E447E29763E7 CRC64;
     MSTENEIWRD ASSSEENSEA GRDGNQFNRE GNYSRPSYNR EGGERPYRPR FASENSDRPQ
     RPYGGERSYR PRFNPNAEGG DRPQRSYNSD RPYRPRYNAE GGEHMQRSYG NSAGDRPYRP
     RYNNENGDRP YRPRYNAEGG DRPQRPYSND RPYGNDRSYT GERSYNNDRP YRPRFNPNVE
     GDDRPQRPYG NPTGDRPYRP RFNPGSGRPG GYGNKDSYSR PIRRSADYDP NAKYSKKKQM
     EYKEQFVDPN EPIRLNKFLA NAGVCSRREA DEFITAGVVS VNGEVVTELG TKIKRGDEVK
     FHDQLVNIER KVYVLLNKPK DTVTTSDDPQ ARRTVMDLVK GACDERIYPV GRLDRNTTGV
     LLLTNDGDLA SKLTHPKYLK KKIYHVHLDK NLTKADMEQI ASGIQLDDGE IHADAISYTD
     EQKKNDIGIE IHSGKNRIVR RIFESLGYKV VKLDRVFFAG LTKKGLRRGE WRYLSEPEVN
     FLRMGSFE
//
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