ID A0A1J4TZT2_9BACT Unreviewed; 328 AA.
AC A0A1J4TZT2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN ORFNames=AUJ54_12635 {ECO:0000313|EMBL:OIO15575.1};
OS Ignavibacteria bacterium CG1_02_37_35.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1805220 {ECO:0000313|EMBL:OIO15575.1, ECO:0000313|Proteomes:UP000182308};
RN [1] {ECO:0000313|EMBL:OIO15575.1, ECO:0000313|Proteomes:UP000182308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_37_35 {ECO:0000313|EMBL:OIO15575.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIO15575.1}.
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DR EMBL; MNVA01000191; OIO15575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4TZT2; -.
DR STRING; 1805220.AUJ54_12635; -.
DR Proteomes; UP000182308; 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 RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 21..83
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT ACT_SITE 145
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 328 AA; 37312 MW; 3507B0DE7662803F CRC64;
MMNLITEKKF KIEVTSGKQK ERIDLYLTNV IENATRTRIQ KLIDAKLVLV NGKPTKANYK
VVPFDLIEVT IPISPRPEKA EPEDIPLNII YEDDYFLIVN KVAGMVAHPA FSNYTGTLVN
ALLHHTKSLS DVNEPIRPGI VHRIDKNTSG LLVVAKDDVT HAKLAKQFAK HSIEREYWAV
AWGIFKEKQG EITHNIVRSK SDRKKFTICK DDGKTAITLY EVIEDFEFTS LLKIHLQTGR
THQIRVHLSG IGHPIFGDET YGGRKLTYGA QLPKMRSRME NLLELMPRQA LHAKKLGFIH
PATNEFISFD SELPEDIQNL LLKLRPAC
//
