ID A0A2V4NR10_9RHOB Unreviewed; 347 AA.
AC A0A2V4NR10;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN ORFNames=DI396_11225 {ECO:0000313|EMBL:PYC47126.1};
OS Litorivita pollutaquae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Litorivita.
OX NCBI_TaxID=2200892 {ECO:0000313|EMBL:PYC47126.1, ECO:0000313|Proteomes:UP000248012};
RN [1] {ECO:0000313|EMBL:PYC47126.1, ECO:0000313|Proteomes:UP000248012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSX-11 {ECO:0000313|EMBL:PYC47126.1,
RC ECO:0000313|Proteomes:UP000248012};
RA Hetharua B.H., Min D., Liao H., Tian Y.;
RT "Oceanovita maritima gen. nov., sp. nov., a marine bacterium in the family
RT Rhodobacteraceae isolated from surface seawater of Lundu port Xiamen,
RT China.";
RL Submitted (MAY-2018) 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}.
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:PYC47126.1}.
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DR EMBL; QFVT01000007; PYC47126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V4NR10; -.
DR OrthoDB; 9807829at2; -.
DR Proteomes; UP000248012; 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:UP000248012};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 16..76
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT ACT_SITE 143
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 347 AA; 38275 MW; ED8F976DD48F0A62 CRC64;
MSGVQTQVVA PDDTDQRLDR WLRRMYPHVS QGRIEKMCRK GELRVNGGRV KASTRLEAGQ
TVRIPPLPSV AEAKSASAGK ITEADAKMIR NCVIYRDDDV IVLNKPPGLA VQGGSGMTRH
VDGLAEALRF GMEDKPRLVH RIDKDTSGVL VLARTRLAAK ALTAAFRHRE TRKLYWAAVA
GVPTPRMGTI KYGLIKAPGH GAKGEGEKMH CIHPREVDKT EGAKRAHSDY AVMDVAGKRT
AWVALVPITG RTHQLRAHMA EIGHPIIGDG KYGGSGQENL GDGWGAQLGG EVSRKLHLHA
RSLKIEHPTT KNILHITAPL PDHMKRTWDI LQWDEKAQPE DPFEEFE
//
