ID A0A147GTS7_9BURK Unreviewed; 352 AA.
AC A0A147GTS7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN ORFNames=NS331_13050 {ECO:0000313|EMBL:KTT20938.1};
OS Pseudacidovorax intermedius.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Pseudacidovorax.
OX NCBI_TaxID=433924 {ECO:0000313|EMBL:KTT20938.1, ECO:0000313|Proteomes:UP000072741};
RN [1] {ECO:0000313|EMBL:KTT20938.1, ECO:0000313|Proteomes:UP000072741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS331 {ECO:0000313|EMBL:KTT20938.1,
RC ECO:0000313|Proteomes:UP000072741};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil at
CC positions 955, 2504 and 2580 in 23S ribosomal RNA.
CC {ECO:0000256|ARBA:ARBA00002876}.
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(955/2504/2580) in 23S rRNA =
CC pseudouridine(955/2504/2580) in 23S rRNA; Xref=Rhea:RHEA:42528,
CC Rhea:RHEA-COMP:10099, Rhea:RHEA-COMP:10100, ChEBI:CHEBI:65314,
CC ChEBI:CHEBI:65315; EC=5.4.99.24;
CC Evidence={ECO:0000256|ARBA:ARBA00000381};
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:KTT20938.1}.
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DR EMBL; LDSL01000074; KTT20938.1; -; Genomic_DNA.
DR RefSeq; WP_058642418.1; NZ_LDSL01000074.1.
DR AlphaFoldDB; A0A147GTS7; -.
DR PATRIC; fig|433924.3.peg.4667; -.
DR OrthoDB; 9785808at2; -.
DR Proteomes; UP000072741; 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 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:SF93; PSEUDOURIDYLATE SYNTHASE RPUSD4, MITOCHONDRIAL; 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; 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:UP000072741};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 35..96
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT ACT_SITE 155
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 352 AA; 38695 MW; C2FB46234963DDFA CRC64;
MTNIIGRKPG PKAPAPRAPA PEVRLVTVDA ESAGQRLDNF LFRHLKGVPK THVYRIIRSG
EVRVNKGRVQ ADSRVEEGDV VRLPPVRVSA APAAAEPAAP ARDFDLLMED EVLLAVDKPA
GTAVHGGSGV SFGVIEQLRA ARPAARFLEL VHRLDRETSG ILLVAKRRSA LTALQAQFRT
RETGKTYLAL VEGDWPARRK VLDAPLARYL LPPRDGAAEG ERRVKVVDKD HPDAMRALTL
VRVLARLQLP GDDVPMSLLA VTIKTGRTHQ IRVHLAHEGH PIAGDDKYGD FERRRTLARL
GLRRMFLHAW RLRFQHPVSE APVALQAALP DELAQLLPPQ ALAALTDPHD DT
//
