ID A0A160NUL7_STRLU Unreviewed; 379 AA.
AC A0A160NUL7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN ORFNames=SLA_1307 {ECO:0000313|EMBL:BAU82249.1};
OS Streptomyces laurentii.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=39478 {ECO:0000313|EMBL:BAU82249.1, ECO:0000313|Proteomes:UP000217676};
RN [1] {ECO:0000313|EMBL:BAU82249.1, ECO:0000313|Proteomes:UP000217676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31255 {ECO:0000313|EMBL:BAU82249.1,
RC ECO:0000313|Proteomes:UP000217676};
RA Doi K., Fujino Y., Nagayoshi Y., Ohshima T., Ogata S.;
RT "Complete Genome Sequence of Thiostrepton-Producing Streptomyces laurentii
RT ATCC 31255.";
RL Genome Announc. 4:e00360-16(2016).
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC {ECO:0000256|ARBA:ARBA00008348, ECO:0000256|RuleBase:RU003887}.
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DR EMBL; AP017424; BAU82249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A160NUL7; -.
DR KEGG; slau:SLA_1307; -.
DR Proteomes; UP000217676; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000217676};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 144..203
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 379 AA; 41634 MW; 40588EC1DD9A84AE CRC64;
MRSSSGRNSG NNGGSRGAKS GGRGNYRGAG NQRDERGQGQ GQGQSAGRPR RTRPEERGYD
VSMPSDERRG GGTGGGDRRG RGDAARGGAK GGPKQSPKRG GGWTAPARSR EYDTRSEERN
RERYADKPQI KTPKTFPGAE QEGERLQKVL ARAGYGSRRA CEELIEQARV EVNGEIVLEQ
GLRVADKDEI RVDGLTVATQ SYQFFALNKP AGVVSTMEDP DGRQCLGDYV TNRETRLFHV
GRLDTETEGI ILLTNHGELA HRLTHPKYGV KKTYLAAITG PLPREVGKRL KDGIQLEDGY
ARADHFRVVE QTGKNYLVEV VLHEGRKHIV RRMLAEAGFP VDKLVRTAFG PITLGDQKSG
WLRRLSNTEV GMLMKEVGL
//
