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Database: UniProt
Entry: A0A3D8IU72_9HELI
LinkDB: A0A3D8IU72_9HELI
Original site: A0A3D8IU72_9HELI 
ID   A0A3D8IU72_9HELI        Unreviewed;       323 AA.
AC   A0A3D8IU72;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN   ORFNames=CQA62_05485 {ECO:0000313|EMBL:RDU68839.1};
OS   Helicobacter cholecystus.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=45498 {ECO:0000313|EMBL:RDU68839.1, ECO:0000313|Proteomes:UP000257067};
RN   [1] {ECO:0000313|EMBL:RDU68839.1, ECO:0000313|Proteomes:UP000257067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700242 {ECO:0000313|EMBL:RDU68839.1,
RC   ECO:0000313|Proteomes:UP000257067};
RA   Mannion A.J., Shen Z., Fox J.G.;
RT   "Novel Campyloabacter and Helicobacter Species and Strains.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:RDU68839.1}.
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DR   EMBL; NXLU01000006; RDU68839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8IU72; -.
DR   OrthoDB; 128480at2; -.
DR   Proteomes; UP000257067; 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; 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; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|RuleBase:RU362028};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257067};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          17..81
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ   SEQUENCE   323 AA;  36872 MW;  E0BF302843ADA856 CRC64;
     MKKFIITSKD IDISEKLRLD HFLTSALQES KSQVHQVIKK GLVLLNSKPC NKNGIFLKEG
     DCLCVLSPQK EEQESKSDFI GEIAILYEDE DVLVLNKPPH LVVHSAPSVK EATLVDYLKS
     RGFKLSNLAG EERYGIVHRL DKPTSGAIAI AKSNQAHNVL SEQLKHKIMG RYYLAITDLP
     LKDRVDVECN MGRNPNHRLK MAKLFEGRYS KTSFIPLLQG REGSLCVAKL YTGRTHQIRL
     HLETLSRHIL GDELYGKKDH TSLRLMLHAY MMYFTHPISK EPIFIQAPLF EDMIGFLKQN
     FLMEEVNEAI SKKHILHCFG DCF
//
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