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Database: UniProt
Entry: E6J894_9ACTN
LinkDB: E6J894_9ACTN
Original site: E6J894_9ACTN 
ID   E6J894_9ACTN            Unreviewed;       252 AA.
AC   E6J894;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN   ORFNames=ES5_07212 {ECO:0000313|EMBL:EFV92199.1};
OS   Dietzia cinnamea P4.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC   Dietzia.
OX   NCBI_TaxID=910954 {ECO:0000313|EMBL:EFV92199.1, ECO:0000313|Proteomes:UP000004165};
RN   [1] {ECO:0000313|EMBL:EFV92199.1, ECO:0000313|Proteomes:UP000004165}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P4 {ECO:0000313|EMBL:EFV92199.1,
RC   ECO:0000313|Proteomes:UP000004165};
RX   PubMed=21901521; DOI=10.1007/s10482-011-9633-7;
RA   Procopio L., Alvarez V.M., Jurelevicius D.A., Hansen L., Sorensen S.J.,
RA   Cardoso J.S., Padula M., Leitao A.C., Seldin L., van Elsas J.D.;
RT   "Insight from the draft genome of Dietzia cinnamea P4 reveals mechanisms of
RT   survival in complex tropical soil habitats and biotechnology potential.";
RL   Antonie Van Leeuwenhoek 101:289-302(2012).
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:EFV92199.1}.
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DR   EMBL; AEKG01000136; EFV92199.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6J894; -.
DR   Proteomes; UP000004165; 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; 3.30.2350.10; Pseudouridine synthase; 1.
DR   Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
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   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   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          12..72
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
SQ   SEQUENCE   252 AA;  27493 MW;  411ED36037FF6B36 CRC64;
     MTESAGRDGA PVRLQKILAQ AGVASRRASE DLIARGRVEV DGKIVREMGV KVDPATAVIR
     VDGTRIVLDD TLVHLALNKP RGYHTTMSDE MGRPCVGDLV ADRIDAGQRL FHVGRLDADT
     EGLLLVTNDG ELAHRLMHPS YEVSKTYMAT VTGVVGKGIG KQLREGVELE DGPAKVDQFS
     LLDVHDGRSL VKVVLHEGRK HIVRRLLAEV GHPVESLVRT RFGSVALGDQ RAGTFRKLNR
     REVSDLYEAV GL
//
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