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Database: UniProt
Entry: A0A1I2XX88_9FIRM
LinkDB: A0A1I2XX88_9FIRM
Original site: A0A1I2XX88_9FIRM 
ID   A0A1I2XX88_9FIRM        Unreviewed;       316 AA.
AC   A0A1I2XX88;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN   ORFNames=SAMN05660649_04166 {ECO:0000313|EMBL:SFH17982.1};
OS   Desulfotruncus arcticus DSM 17038.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC   Desulfotruncus.
OX   NCBI_TaxID=1121424 {ECO:0000313|EMBL:SFH17982.1, ECO:0000313|Proteomes:UP000199337};
RN   [1] {ECO:0000313|Proteomes:UP000199337}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17038 {ECO:0000313|Proteomes:UP000199337};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FOOX01000019; SFH17982.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2XX88; -.
DR   STRING; 341036.SAMN05660649_04166; -.
DR   Proteomes; UP000199337; 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:UP000199337};
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        139
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ   SEQUENCE   316 AA;  35527 MW;  BECFE56E4BFF7A44 CRC64;
     MRNNEIYHVD NNRAGQRLDV YVTSSGNNLS RSYIQKLIGE GLVKVNGIEA RANYRLKEGD
     EIAVEIPPPT ELQVLPEQIQ LDIYYEDLDV IVINKPRGMV VHPAEGNFYG TMVNALLYHC
     RDLSGINGVL RPGIVHRIDK DTSGLLMAAK NDLAHERLAD QLKEHTVARG YLALAHGSMQ
     FDQGIINAPI GRDPRDRKKM AVTSRNSKNA ITHYRVLGRA GDYTFLELRL ETGRTHQIRV
     HLAHIGHPLA GDARYGPARP HFDLAGQFLH AYLLGFIHPR ETRYLEFKAP LPGVLLEILK
     SLDLAGSLEQ VYCFQK
//
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