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Database: UniProt
Entry: A0A1H0RDK0_9BACI
LinkDB: A0A1H0RDK0_9BACI
Original site: A0A1H0RDK0_9BACI 
ID   A0A1H0RDK0_9BACI        Unreviewed;       303 AA.
AC   A0A1H0RDK0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-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=SAMN05216565_102149 {ECO:0000313|EMBL:SDP27259.1};
OS   Litchfieldia salsa.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Litchfieldia.
OX   NCBI_TaxID=930152 {ECO:0000313|EMBL:SDP27259.1, ECO:0000313|Proteomes:UP000199159};
RN   [1] {ECO:0000313|Proteomes:UP000199159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBRC-M10078 {ECO:0000313|Proteomes:UP000199159};
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; FNJU01000002; SDP27259.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0RDK0; -.
DR   STRING; 930152.SAMN05216565_102149; -.
DR   OrthoDB; 9807829at2; -.
DR   Proteomes; UP000199159; 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:UP000199159};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          15..75
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ   SEQUENCE   303 AA;  33984 MW;  DD988FB2844C99F2 CRC64;
     MNENMIIVEN EELSDRIDKV ITAQNSDWSR SQVQQWIKEG NVTVNGQKIK SNYKSNPGDK
     IEITIPSPEL LDVIPEEMNL EIFYEDSDVL VVNKPKGMVV HPAPGHYSGT LVNGLMAHCK
     DLSGINGVLR PGIVHRIDKD TSGLLMVAKN DLAHESLVQQ LVDKTVTRKY KAIVHGNIPH
     DQGTIDAPIG RDKRDRQSMT VTDDNSKEAV THFNVLERLK DFTYIECQLE TGRTHQIRVH
     MKYIGYPLAG DPKYGPKKTL SIGGQALHAG ILGFIHPRTK EYLEFEAPLP SEFEALLEEL
     KSN
//
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