ID A0A240CAP7_SERFI Unreviewed; 288 AA.
AC A0A240CAP7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN Name=rluF_2 {ECO:0000313|EMBL:SNW04929.1};
GN ORFNames=SAMEA4384070_04086 {ECO:0000313|EMBL:SNW04929.1};
OS Serratia ficaria.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=61651 {ECO:0000313|EMBL:SNW04929.1, ECO:0000313|Proteomes:UP000215134};
RN [1] {ECO:0000313|EMBL:SNW04929.1, ECO:0000313|Proteomes:UP000215134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12148 {ECO:0000313|EMBL:SNW04929.1,
RC ECO:0000313|Proteomes:UP000215134};
RG Pathogen Informatics;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(2604) in 23S rRNA = pseudouridine(2604) in 23S rRNA;
CC Xref=Rhea:RHEA:38875, Rhea:RHEA-COMP:10093, Rhea:RHEA-COMP:10094,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.21;
CC Evidence={ECO:0000256|ARBA:ARBA00036535};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(35) in tRNA(Tyr) = pseudouridine(35) in tRNA(Tyr);
CC Xref=Rhea:RHEA:60556, Rhea:RHEA-COMP:15607, Rhea:RHEA-COMP:15608,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000256|ARBA:ARBA00036390};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC {ECO:0000256|ARBA:ARBA00008348, ECO:0000256|RuleBase:RU003887}.
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DR EMBL; LT906479; SNW04929.1; -; Genomic_DNA.
DR RefSeq; WP_061798669.1; NZ_QTUE01000001.1.
DR AlphaFoldDB; A0A240CAP7; -.
DR STRING; 1411141.GCA_001590885_03397; -.
DR GeneID; 75029208; -.
DR KEGG; sfj:SAMEA4384070_4086; -.
DR OrthoDB; 9807213at2; -.
DR Proteomes; UP000215134; Chromosome 1.
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; cd02554; PseudoU_synth_RluF; 1.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.30.70.1560; Alpha-L RNA-binding motif; 1.
DR Gene3D; 3.30.70.580; Pseudouridine synthase I, catalytic domain, N-terminal subdomain; 1.
DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR InterPro; IPR042092; PsdUridine_s_RsuA/RluB/E/F_cat.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR InterPro; IPR000748; PsdUridine_synth_RsuA/RluB/E/F.
DR InterPro; IPR018496; PsdUridine_synth_RsuA/RluB_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR NCBIfam; TIGR00093; pseudouridine synthase; 1.
DR PANTHER; PTHR47683; PSEUDOURIDINE SYNTHASE FAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR47683:SF2; S4 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; PS01149; PSI_RSU; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU003887};
KW Reference proteome {ECO:0000313|Proteomes:UP000215134};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 7..63
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 238..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 288 AA; 32019 MW; 5F694BF533EA26CA CRC64;
MLTKPSTRLN KYISESGICS RRDADRYIEQ GNVFINGKRV ALGDRVFPGD VVKVNGQLIE
PRNEDDLVFI ALNKPVGIVS TTEDGEKDNI VDFVNHSTRI FPIGRLDKDS QGLIFLTNHG
DLVNKILRAG NDHEKEYRVT VNKPVTDEFI RGLGAGVPML GTVTKKCKVK KEAPFVFRIV
LVQGLNRQIR RMCEHFGYEV TKLERTRIMN VSLTGLPPGE WRDLTDDELI ELFKSIEDSS
SEAKPAKKAQ PAARKKPAGS GPKSAEKPGG APAGRKRFAQ PGRKKKGR
//