ID A0A2S4M478_9BURK Unreviewed; 431 AA.
AC A0A2S4M478;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Ribosomal large subunit pseudouridine synthase D {ECO:0000256|ARBA:ARBA00040039};
DE EC=5.4.99.23 {ECO:0000256|ARBA:ARBA00038942};
DE AltName: Full=23S rRNA pseudouridine(1911/1915/1917) synthase {ECO:0000256|ARBA:ARBA00042264};
DE AltName: Full=rRNA pseudouridylate synthase D {ECO:0000256|ARBA:ARBA00042840};
DE AltName: Full=rRNA-uridine isomerase D {ECO:0000256|ARBA:ARBA00043148};
GN ORFNames=B0G62_111173 {ECO:0000313|EMBL:POR49504.1};
OS Paraburkholderia eburnea.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1189126 {ECO:0000313|EMBL:POR49504.1, ECO:0000313|Proteomes:UP000237381};
RN [1] {ECO:0000313|EMBL:POR49504.1, ECO:0000313|Proteomes:UP000237381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 18070 {ECO:0000313|EMBL:POR49504.1,
RC ECO:0000313|Proteomes:UP000237381};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:POR49504.1}.
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DR EMBL; PQGA01000011; POR49504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4M478; -.
DR OrthoDB; 9785808at2; -.
DR Proteomes; UP000237381; 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:SF44; PSEUDOU_SYNTH_2 DOMAIN-CONTAINING PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000237381};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 79..144
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 201
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 431 AA; 47083 MW; F0B3F924FDC0A3B2 CRC64;
MTRSVIPGAG APGAQNSISD YSLGDVPDAG AADEALDDDL IEGESVSDST PVSGLSRTRV
AREDQEARRA EVPDELAGER LDKVLARVFP EFSRNRLQGW IEAQRVHVDG KPAKVRQPVP
LGAVIELVPD LLPEQLAFTP EPVPLDIVYE DDAILVINKP AGMVVHPAAG NWSGTILNGL
LHRYGEAAAG LPRAGIVHRL DKETSGLMVV ARTLEAQTDL VRQLQARTVK RRYLALVWGN
MPDEGTIDAP IGRDPRDRVR MAVVSGASGK PARTHYRRID KTIWHQQPIS AIHCDLETGR
THQIRVHCAH IRHPLLGDPV YGHARGKRSV AALPGDFARQ ALHAYRLGLI HPVTGRAMQW
RAEVPDDMDA LIEALGFGGE DNEDSSAFDE MFDSAYTDEG YVIGSNVEDY ADDEDEGEDH
DHDDHDGDKP A
//
