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Database: UniProt
Entry: A0A0M7BDQ5_9RHOB
LinkDB: A0A0M7BDQ5_9RHOB
Original site: A0A0M7BDQ5_9RHOB 
ID   A0A0M7BDQ5_9RHOB        Unreviewed;       514 AA.
AC   A0A0M7BDQ5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN   Name=rluB {ECO:0000313|EMBL:CUH40319.1};
GN   ORFNames=JSE7799_03051 {ECO:0000313|EMBL:CUH40319.1};
OS   Jannaschia seosinensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=313367 {ECO:0000313|EMBL:CUH40319.1, ECO:0000313|Proteomes:UP000049455};
RN   [1] {ECO:0000313|EMBL:CUH40319.1, ECO:0000313|Proteomes:UP000049455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7799 {ECO:0000313|EMBL:CUH40319.1,
RC   ECO:0000313|Proteomes:UP000049455};
RA   Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA   Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA   Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL   Submitted (SEP-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}.
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DR   EMBL; CYPR01000203; CUH40319.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M7BDQ5; -.
DR   STRING; 313367.JSE7799_03051; -.
DR   OrthoDB; 9807213at2; -.
DR   Proteomes; UP000049455; 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:UP000049455};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          9..70
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   REGION          242..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..332
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..369
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..477
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  55578 MW;  EE67AF25848F26B1 CRC64;
     MANESRDGER IAKVIARAGL ASRRDAEGMV ADLRVTVNGR TVSNVAHNVV PGDRVAVDGQ
     PLPEPEAARV WLYHKPAGLV TTARDEKGRE TVFDALPEEM GRVLSVGRLD LTSEGLLLLT
     NDGALKRQLE LPATGWLRRY RVRVNGTPDE AALERLRTGI EVEGETFAPM QVTLDRQKGA
     NAWLTIGLRE GKNREIRRAM DAVGLYVNRL IRVSYGPFQL GSLEPGEVEE VKPRVLRDQL
     GGTYEGELAE GRKETAMADE KGGPKGGAKG GRPSGPGGRK PRPSGDRLVE HGRGKPREGG
     PKGNAQGKPR GPGNARAEDA ARPDRPRTGK PPVTRNDGDG SRPARPARPD GKPAHAKGGP
     RRSDDAGRPA RPGGKPFAAR DGDRKPRDGD AKPRFAKDGD RKPRDGDGKP RFAKDGDRKP
     RDGDSKPHFA KDGGRKPRRE DDRGPRRDDK AGGPKRDAAP DRPKETKAER TARMRADTSV
     SIRKGGQKGR GISKPAKPAS TKRMRKPGDD DPKG
//
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