ID A0A2W6MXN1_9HELI Unreviewed; 325 AA.
AC A0A2W6MXN1;
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=B6S12_02595 {ECO:0000313|EMBL:PZT48749.1};
OS Helicobacter valdiviensis.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1458358 {ECO:0000313|EMBL:PZT48749.1, ECO:0000313|Proteomes:UP000249746};
RN [1] {ECO:0000313|EMBL:PZT48749.1, ECO:0000313|Proteomes:UP000249746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WBE14 {ECO:0000313|EMBL:PZT48749.1,
RC ECO:0000313|Proteomes:UP000249746};
RA Fresia P., Jara R., Sierra R., Ferres I., Greif G., Iraola G., Collado L.;
RT "Genomic and clinical evidence uncovers the enterohepatic species
RT Helicobacter valdiviensis as a potential human intestinal pathogen.";
RL Submitted (MAR-2017) 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:PZT48749.1}.
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DR EMBL; NBIU01000004; PZT48749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W6MXN1; -.
DR OrthoDB; 128480at2; -.
DR Proteomes; UP000249746; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000249746};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 16..80
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT ACT_SITE 138
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 325 AA; 38002 MW; 2CA9F0A71E6B1D20 CRC64;
MQHIHSFSPN QEDFGTRLDQ FLVKSLNLSR NQIHSLLKNE RILLNNKKVQ KNGISLKEGD
KITLLEQEKT QKEEKELYIP FLYEDEDLLI LNKPIDLITH KANDKDLQFT LIDYLKKHSI
PLSNLGDNTR EGIVHRLDKT TSGAMIIAKN NSTHELLSLQ IKERQIQRYY LCVIDNPLKN
NIIIETPLMR HPKNRLKYIT TNSKDARGKE AKSAFFKIQS QGNLELIGAK LFSGRTHQIR
AHLASLNRHI LGDYFYGYQG DYSKRILLHS HFLSFIHPKS KKLIEIYAPL YKDMLSYIKE
NFYKDKHEIT AEFKIPLHEL FSTSF
//
