ID A0A1H1PMU9_9PSED Unreviewed; 353 AA.
AC A0A1H1PMU9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN ORFNames=SAMN05216598_0597 {ECO:0000313|EMBL:SDS12473.1};
OS Pseudomonas asplenii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=53407 {ECO:0000313|EMBL:SDS12473.1, ECO:0000313|Proteomes:UP000199524};
RN [1] {ECO:0000313|Proteomes:UP000199524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23835 {ECO:0000313|Proteomes:UP000199524};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil.
CC {ECO:0000256|RuleBase:RU362028}.
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|RuleBase:RU362028};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(1911/1915/1917) in 23S rRNA =
CC pseudouridine(1911/1915/1917) in 23S rRNA; Xref=Rhea:RHEA:42524,
CC Rhea:RHEA-COMP:10097, Rhea:RHEA-COMP:10098, ChEBI:CHEBI:65314,
CC ChEBI:CHEBI:65315; EC=5.4.99.23;
CC Evidence={ECO:0000256|ARBA:ARBA00036882};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC {ECO:0000256|ARBA:ARBA00010876, ECO:0000256|RuleBase:RU362028}.
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DR EMBL; LT629777; SDS12473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1PMU9; -.
DR Proteomes; UP000199524; Chromosome i.
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; cd02869; PseudoU_synth_RluA_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; IPR006224; PsdUridine_synth_RluA-like_CS.
DR InterPro; IPR006225; PsdUridine_synth_RluC/D.
DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR NCBIfam; TIGR00005; rluA_subfam; 1.
DR PANTHER; PTHR21600; MITOCHONDRIAL RNA PSEUDOURIDINE SYNTHASE; 1.
DR PANTHER; PTHR21600:SF44; PSEUDOU_SYNTH_2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00849; PseudoU_synth_2; 1.
DR Pfam; PF01479; S4; 1.
DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR PROSITE; PS01129; PSI_RLU; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU362028};
KW Reference proteome {ECO:0000313|Proteomes:UP000199524};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 51..96
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|Pfam:PF01479"
FT DOMAIN 124..274
FT /note="Pseudouridine synthase RsuA/RluA-like"
FT /evidence="ECO:0000259|Pfam:PF00849"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 171
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 353 AA; 38930 MW; 82D5AB0E6FD6060E CRC64;
MMNAPLKASG QKTPYLTTSA QPKPKAVPTP SPSMSDKIEL RAEVPSELGG QRLDQVAAQL
FTEHSRSRLS TWIKDGRLTV DGAVIRPRDI VHGGAVLELT AEQEAQGEWV AQDIELDIVY
EDDDILVINK PAGLVVHPAA GHADGTLLNA LLHHVPDIIN VPRAGIVHRL DKDTTGLMVV
AKTIQAQTQL VAQLQSRTVS RIYECIVIGV VTAGGKINAP IGRHGQQRQR MAVMEGGKPA
VSHYRVLERF RSHTHVRVKL ETGRTHQIRV HMSHINFPLV GDPAYGGRFR IPPAASVTMV
ESLKNFPRQA LHARFLELDH PTSGERMSWE SPLPDDFVWL LSLLKQDREA FIG
//