ID A0A1H0U2E1_9ACTN Unreviewed; 375 AA.
AC A0A1H0U2E1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN ORFNames=SAMN04487981_12868 {ECO:0000313|EMBL:SDP60311.1};
OS Streptomyces sp. cf386.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1761904 {ECO:0000313|EMBL:SDP60311.1, ECO:0000313|Proteomes:UP000198720};
RN [1] {ECO:0000313|Proteomes:UP000198720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF386 {ECO:0000313|Proteomes:UP000198720};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC {ECO:0000256|ARBA:ARBA00008348, ECO:0000256|RuleBase:RU003887}.
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DR EMBL; FNHV01000028; SDP60311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0U2E1; -.
DR STRING; 1761904.SAMN04487981_12868; -.
DR OrthoDB; 9807213at2; -.
DR Proteomes; UP000198720; 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 Reference proteome {ECO:0000313|Proteomes:UP000198720};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 139..199
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 375 AA; 40950 MW; 80464A00C5871F38 CRC64;
MRSSSGRNSS GNNGGSRGGN SGGRGGSSGG RGNYRGAGNN RDDKQGGRPK KPRPEERRYD
VGPGATQDGP KSGRGASARG GAKGGPKQGQ QRGTGRGRTA PASSREYDAR AEERNRERYA
GKKDVKLPKT FPGAEQEGER LQKVLARAGY GSRRSCEELI EQARVEVNGE IVLEQGKRVD
PEKDEVKVDG LTVATQSYQF FSLNKPAGVV STMEDPEGRQ CLGDYVTNRE TRLFHVGRLD
TETEGVILLT NHGELAHRLT HPKYGVKKTY LAAIVGPIPR DLGKKLKDGI QLEDGYARAD
HFRVVEQTGK NYLVEVTLHE GRKHIVRRML AEAGFPVEKL VRTSFGPITL GDQKSGWLRR
LSNTEVGMLM QEVDL
//
