ID A0A1E5CYP9_9VIBR Unreviewed; 247 AA.
AC A0A1E5CYP9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=tRNA pseudouridine synthase C {ECO:0000256|ARBA:ARBA00040675};
DE EC=5.4.99.26 {ECO:0000256|ARBA:ARBA00038943};
DE AltName: Full=tRNA pseudouridine(65) synthase {ECO:0000256|ARBA:ARBA00041975};
DE AltName: Full=tRNA pseudouridylate synthase C {ECO:0000256|ARBA:ARBA00043049};
DE AltName: Full=tRNA-uridine isomerase C {ECO:0000256|ARBA:ARBA00041803};
GN ORFNames=A130_15805 {ECO:0000313|EMBL:OEE75947.1};
OS Vibrio genomosp. F6 str. FF-238.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1191298 {ECO:0000313|EMBL:OEE75947.1, ECO:0000313|Proteomes:UP000094165};
RN [1] {ECO:0000313|EMBL:OEE75947.1, ECO:0000313|Proteomes:UP000094165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FF-238 {ECO:0000313|EMBL:OEE75947.1,
RC ECO:0000313|Proteomes:UP000094165};
RX PubMed=22955834; DOI=10.1126/science.1219385;
RA Cordero O.X., Wildschutte H., Kirkup B., Proehl S., Ngo L., Hussain F.,
RA Le Roux F., Mincer T., Polz M.F.;
RT "Ecological populations of bacteria act as socially cohesive units of
RT antibiotic production and resistance.";
RL Science 337:1228-1231(2012).
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-65 in
CC transfer RNAs. {ECO:0000256|ARBA:ARBA00037670}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(65) in tRNA = pseudouridine(65) in tRNA;
CC Xref=Rhea:RHEA:42536, Rhea:RHEA-COMP:10103, Rhea:RHEA-COMP:10104,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.26;
CC Evidence={ECO:0000256|ARBA:ARBA00036607};
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:OEE75947.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJYW02000129; OEE75947.1; -; Genomic_DNA.
DR RefSeq; WP_017053989.1; NZ_AJYW02000129.1.
DR AlphaFoldDB; A0A1E5CYP9; -.
DR Proteomes; UP000094165; Unassembled WGS sequence.
DR GO; GO:0140098; F:catalytic activity, acting on RNA; IEA:UniProt.
DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd02563; PseudoU_synth_TruC; 1.
DR Gene3D; 3.30.2350.10; Pseudouridine synthase; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR006224; PsdUridine_synth_RluA-like_CS.
DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR PANTHER; PTHR21600; MITOCHONDRIAL RNA PSEUDOURIDINE SYNTHASE; 1.
DR PANTHER; PTHR21600:SF56; TRNA PSEUDOURIDINE SYNTHASE C; 1.
DR Pfam; PF00849; PseudoU_synth_2; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR PROSITE; PS01129; PSI_RLU; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000094165};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 11..170
FT /note="Pseudouridine synthase RsuA/RluA-like"
FT /evidence="ECO:0000259|Pfam:PF00849"
SQ SEQUENCE 247 AA; 28850 MW; 0F6E3431DCA52EDC CRC64;
MLDIIFQDEY FVAVNKPAGM LVHRSWLDKH ETQFVMQTLR DQIGQHVFPL HRLDRPTSGV
LVFALSSEVA SQVMPMFANH EMQKTYHAIV RGWIEEGDTL DYPLKVELDK IADKFAKEDK
EPQEAVTAYE PLAKVEIPYS TGRFPTSRYG LVEMAPKTGR KHQLRRHMAH LRHPIVGDTS
HGDGKHNKLF RENLESHRLL LHASELRFIH PFTQQELVLK AKFDETWLAL FERFEWQDIL
EKLEARS
//