ID A0A127QWB6_9BURK Unreviewed; 331 AA.
AC A0A127QWB6;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-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=CPter291_1701 {ECO:0000313|EMBL:AMP13972.1};
OS Collimonas pratensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=279113 {ECO:0000313|EMBL:AMP13972.1, ECO:0000313|Proteomes:UP000074914};
RN [1] {ECO:0000313|EMBL:AMP13972.1, ECO:0000313|Proteomes:UP000074914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter291 {ECO:0000313|EMBL:AMP13972.1,
RC ECO:0000313|Proteomes:UP000074914};
RA Song C., Schmidt R., de Jager V., Krzyzanowska D., Jongedijk E., Cankar K.,
RA Beekwilder J., van Veen A., de Boer W., van Veen J.A., Garbeva P.;
RT "Exploring the genomic traits of fungus-feeding bacterial genus
RT Collimonas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP013236; AMP13972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A127QWB6; -.
DR PATRIC; fig|279113.10.peg.1692; -.
DR Proteomes; UP000074914; 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; 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 RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 22..81
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT ACT_SITE 139
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 331 AA; 37054 MW; A0553F0824CDCB74 CRC64;
MKPPPAPLQV QLLTIGEEDA GQRIDNFLLR ICKGVPKSHI YRVLRSGEVR VNKGRIDQTY
RLLEGDVIRV PPIRIAEKQE QVVPGAEFKI LLEDNHMLVI DKPAGVAVHG GSGVSYGVIE
QLRAARPQAK FLELVHRLDR DTSGILLLAK KRSALTNLHE QMRDGDTDKR YLVLVHGDWQ
NERQHVKLAL HKYTAADGER RVRVQADGQA SHTIFNLIRR YGDYALLEAE LKTGRTHQIR
VHLSASGFAI AGDDKYGDFA LNRALQKADG QRIALKRMFL HAYQITFAHP ETGKPVTLKA
PLPPECEKFL KSLPQESKLD VASAPSRTTG D
//
