ID G2FEG9_9GAMM Unreviewed; 318 AA.
AC G2FEG9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN Name=rluD {ECO:0000313|EMBL:EGW54738.1};
GN ORFNames=TevJSym_ai00180 {ECO:0000313|EMBL:EGW54738.1};
OS endosymbiont of Tevnia jerichonana (vent Tica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW54738.1, ECO:0000313|Proteomes:UP000005167};
RN [1] {ECO:0000313|EMBL:EGW54738.1, ECO:0000313|Proteomes:UP000005167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA Sievert S.M., Schweder T.;
RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT jerichonana share an identical physiology as revealed by proteogenomic
RT analyses.";
RL ISME J. 0:0-0(2011).
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 -!- 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, 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:EGW54738.1}.
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DR EMBL; AFZB01000009; EGW54738.1; -; Genomic_DNA.
DR RefSeq; WP_006474478.1; NZ_AFZB01000009.1.
DR AlphaFoldDB; G2FEG9; -.
DR PATRIC; fig|1049564.3.peg.1303; -.
DR eggNOG; COG0564; Bacteria.
DR Proteomes; UP000005167; 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 Isomerase {ECO:0000256|RuleBase:RU362028, ECO:0000313|EMBL:EGW54738.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005167};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 19..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 318 AA; 35451 MW; 0A2EAB689452ED28 CRC64;
MSEEIETLIS EVGLEQAGRR LDQVVAEQFA QFSRSRLQRW IKDGRLLLDG RPGKPKQKVR
GGERLELVPQ LEQEVTSRPQ PIPLDILFED ESLLVVNKPA GLVVHPAVGN PDGTLLNALL
HYFPAISQVP RGGIVHRLDK ETSGLLVVAK TLQAQTALVA QLQARSMKRE YRAFAQGVMA
AGGKVDAPIG RHPVHRTRMA VVANGKPAVT HYRVIERYRF HTDLRIQLET GRTHQIRVHM
AQIRFPLVGD PVYGGRLRLP TGISDALAEG LRAFKRQALH ARRLELVHPE SGEQMSWEAP
LPEDMEQLLG LLRADAAE
//
