ID A0A0Q5MNS3_9MICO Unreviewed; 307 AA.
AC A0A0Q5MNS3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN ORFNames=ASF89_07220 {ECO:0000313|EMBL:KQR64328.1};
OS Frigoribacterium sp. Leaf172.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1736285 {ECO:0000313|EMBL:KQR64328.1, ECO:0000313|Proteomes:UP000051720};
RN [1] {ECO:0000313|EMBL:KQR64328.1, ECO:0000313|Proteomes:UP000051720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf172 {ECO:0000313|EMBL:KQR64328.1,
RC ECO:0000313|Proteomes:UP000051720};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR64328.1, ECO:0000313|Proteomes:UP000051720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf172 {ECO:0000313|EMBL:KQR64328.1,
RC ECO:0000313|Proteomes:UP000051720};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC {ECO:0000256|ARBA:ARBA00010876, ECO:0000256|RuleBase:RU362028}.
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:KQR64328.1}.
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DR EMBL; LMPB01000002; KQR64328.1; -; Genomic_DNA.
DR RefSeq; WP_055797731.1; NZ_LMPB01000002.1.
DR AlphaFoldDB; A0A0Q5MNS3; -.
DR STRING; 1736285.ASF89_07220; -.
DR OrthoDB; 9807829at2; -.
DR Proteomes; UP000051720; 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; cd02869; PseudoU_synth_RluA_like; 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 SMART; SM00363; 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:UP000051720};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 16..79
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT ACT_SITE 139
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 307 AA; 32573 MW; 24FE2E8A33ED7DAF CRC64;
MSEYRSLPVP DGLAGERVDA ALAKLLGFSR TFAAEVVGGG GVSVDSKPVG KSDRLDAGAW
LEVEWTPKEG PSIVARDVPG MGIVHDDDEI VVVDKPVGVA AHPSVGWTGP TVLGGLAAAG
FTVATSGAAE RAGIVHRLDV GTSGLMVVAK TERAYTVLKQ AFRERTVDKI YNAVVQGHPD
PLTGTIDAPI GRHPSSDWKF AVVVDGKPSV THYETIEAFP AASLLEIHLE TGRTHQIRVH
MSAQRHPCVG DTTYGADPTL TARLGLTRQW LHAVSLGFRH PATGEQVVYR SDHPADLRHA
LDVLGES
//