ID Q7VMD1_HAEDU Unreviewed; 354 AA.
AC Q7VMD1;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN OrderedLocusNames=HD_1052 {ECO:0000313|EMBL:AAP95926.1};
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412 {ECO:0000313|EMBL:AAP95926.1, ECO:0000313|Proteomes:UP000001022};
RN [1] {ECO:0000313|Proteomes:UP000001022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724 {ECO:0000313|Proteomes:UP000001022};
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-2605
CC in 23S ribosomal RNA. {ECO:0000256|ARBA:ARBA00037383}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(2605) in 23S rRNA = pseudouridine(2605) in 23S rRNA;
CC Xref=Rhea:RHEA:42520, Rhea:RHEA-COMP:10095, Rhea:RHEA-COMP:10096,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.22;
CC Evidence={ECO:0000256|ARBA:ARBA00036944};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC {ECO:0000256|ARBA:ARBA00008348, ECO:0000256|RuleBase:RU003887}.
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DR EMBL; AE017143; AAP95926.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7VMD1; -.
DR STRING; 233412.HD_1052; -.
DR KEGG; hdu:HD_1052; -.
DR eggNOG; COG1187; Bacteria.
DR HOGENOM; CLU_024979_1_1_6; -.
DR OrthoDB; 9807213at2; -.
DR Proteomes; UP000001022; 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; cd02556; PseudoU_synth_RluB; 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: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:UP000001022};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 75..133
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 354 AA; 40041 MW; A7C1225FF2760D62 CRC64;
MTTFHKKAAN KRPVSFKSRQ QDDITSFKKS ENKAHKSQSV KNRSKAVANS VAKSTLKLPA
SEQMLQDKKT KIVGEKLQKI LARAGQGSRR ELEEVIAAGR VSVDGKIASL GDRVHVNATT
KIRIDGTLIN LVTAQKEICR VLMYYKPEGE LCTRADPEGR ATVFDRLPRL SGSRWIAVGR
LDINTSGLLL FTTDGDLANR LMHPSHEVER EYSVRVFGQV DDAMLQRLRK GVQLEDGPAN
FKQIKAVGGT GLNQWFDVTL TEGRNREVRR LWESQGVEVS RLIRIRYGNI KLEKGLPRGG
WEEMGLEQVN YLRDLVGLPA ETETKVDVTK NRRRTNIRQI RKAVKQHSKY RTKN
//
