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Database: UniProt
Entry: A0A1R1CKU5_9BACL
LinkDB: A0A1R1CKU5_9BACL
Original site: A0A1R1CKU5_9BACL 
ID   A0A1R1CKU5_9BACL        Unreviewed;       321 AA.
AC   A0A1R1CKU5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN   ORFNames=BK133_25540 {ECO:0000313|EMBL:OMF22756.1};
OS   Paenibacillus sp. FSL H8-0548.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1920422 {ECO:0000313|EMBL:OMF22756.1, ECO:0000313|Proteomes:UP000187405};
RN   [1] {ECO:0000313|EMBL:OMF22756.1, ECO:0000313|Proteomes:UP000187405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H8-0548 {ECO:0000313|EMBL:OMF22756.1,
RC   ECO:0000313|Proteomes:UP000187405};
RA   Beno S.M.;
RT   "Paenibacillus species isolates.";
RL   Submitted (NOV-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}.
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:OMF22756.1}.
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DR   EMBL; MRTK01000051; OMF22756.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R1CKU5; -.
DR   STRING; 1920422.BK133_25540; -.
DR   Proteomes; UP000187405; 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; RIBOSOMAL LARGE SUBUNIT PSEUDOURIDINE SYNTHASE D; 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:UP000187405};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00182}.
FT   DOMAIN          31..97
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   ACT_SITE        156
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ   SEQUENCE   321 AA;  36008 MW;  4CC7CDCF06344DB2 CRC64;
     MERTRIKTIM SSNLYNEEPL EWIAEEEQSG ERVDKFVTDL IDNQGVSRTQ VQEWIKAGAV
     QVDGKIAKAN VKIVPGNRVV LQIPEPEEAA IVPENIPLEI IYEDSDLIVV NKKRGMVVHP
     APGHSSGTLV NALMYHCKDL SGINGMIRPG IVHRIDKDTT GLLMAAKNDL AHISLAEQLK
     EHTVTRKYIA LVHGNLPHDQ GTIDAPIGRD LNDRKLFTVT ERNSRNAVTH FHVLERLGDY
     TVVELQLETG RTHQIRVHMK YIGHPLAGDP VYGRNKTVAL KGQALHATRL GFTHPRSGER
     LEFEMPLPAD FEYVLSNLRS R
//
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