ID A0A1G1YFS7_9BACT Unreviewed; 318 AA.
AC A0A1G1YFS7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN ORFNames=A3J59_00850 {ECO:0000313|EMBL:OGY51084.1};
OS Candidatus Buchananbacteria bacterium RIFCSPHIGHO2_02_FULL_56_16.
OC Bacteria; Candidatus Buchananbacteria.
OX NCBI_TaxID=1797542 {ECO:0000313|EMBL:OGY51084.1, ECO:0000313|Proteomes:UP000177310};
RN [1] {ECO:0000313|EMBL:OGY51084.1, ECO:0000313|Proteomes:UP000177310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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:OGY51084.1}.
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DR EMBL; MHIL01000024; OGY51084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1YFS7; -.
DR STRING; 1797542.A3J59_00850; -.
DR Proteomes; UP000177310; 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 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 RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 12..69
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT ACT_SITE 138
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 318 AA; 36395 MW; 6DCCF0EF87BF4239 CRC64;
MKFTIAEAAS RQRLDKFLTG QLVARSRAAI QKLIKSGGVS VNGRPQVPHY VLKIGDEVTA
IDQPAERGET VPRQPVTTPR VVAEQDDFLI IEKPAGLLVH PTEKNESHTL VSWLLERYPS
LRTVGEQQYR AGIIHRLDRD VSGIMVVPKN NEMFSHLKEQ FKQRKVHKEY QALVYGRVSQ
PIGTIELPIG RRKDGKFVAH PRQGQQKLQD RDKIAKTSFE VLEYLKDYTL LKVTIATGRT
HQIRVHLSAI GHPILGDQIY RAKKKFFHFL RRRIKVVQPG RIFLHSTMIG FQDRRGQRQA
FRVPLPPTLT EFLNGLKT
//
