ID A0A1T5HG80_9BACT Unreviewed; 358 AA.
AC A0A1T5HG80;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN ORFNames=SAMN03080601_02290 {ECO:0000313|EMBL:SKC19687.1};
OS Alkalitalea saponilacus.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Alkalitalea.
OX NCBI_TaxID=889453 {ECO:0000313|EMBL:SKC19687.1, ECO:0000313|Proteomes:UP000191055};
RN [1] {ECO:0000313|EMBL:SKC19687.1, ECO:0000313|Proteomes:UP000191055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24412 {ECO:0000313|EMBL:SKC19687.1,
RC ECO:0000313|Proteomes:UP000191055};
RA Peterson S.W.;
RL Submitted (FEB-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}.
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DR EMBL; FUYV01000013; SKC19687.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5HG80; -.
DR STRING; 889453.SAMN03080601_02290; -.
DR KEGG; asx:CDL62_02625; -.
DR OrthoDB; 9807829at2; -.
DR Proteomes; UP000191055; 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:UP000191055};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 43..108
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 168
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 358 AA; 40789 MW; 0FB1F080E55B4D9A CRC64;
MQDYQEEFEE LEDENYSEET TDGESGEFYE HHSFTADTGQ SALRIDKFLV NRIENASRSK
IQEAAQAGCI RVNNQPVKAN YKVKPNDVVS VVMSYPPREI EIIAQDIPLN IVFEDDTLIV
INKEPGMVVH PGYGNYTGTL VNALAWHFKD QPWFNSDDPR PGLVHRIDKD TSGLLVIAKT
EEAKMHLASQ FFEKTSTRTY QAIVWGAPEP EEGTITGHIG RSLKDRKQMA VFSEGDYGKA
AVTHYTVLEK LGYVSLVECR LETGRTHQIR AHFKHIGHPL FNDERYGGNQ ILKGTTFTKY
KQFVENCFSI LPRQALHAKT LGFEHPKTGK YIEFNSELPE DITTVIEKWK NYIASRPQ
//
