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Database: UniProt
Entry: A0A2N8N5Z3_9BACT
LinkDB: A0A2N8N5Z3_9BACT
Original site: A0A2N8N5Z3_9BACT 
ID   A0A2N8N5Z3_9BACT        Unreviewed;       353 AA.
AC   A0A2N8N5Z3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN   ORFNames=BHU16_08390 {ECO:0000313|EMBL:PNE24192.1};
OS   Tannerella sp. oral taxon 808.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Tannerella.
OX   NCBI_TaxID=712711 {ECO:0000313|EMBL:PNE24192.1, ECO:0000313|Proteomes:UP000235918};
RN   [1] {ECO:0000313|EMBL:PNE24192.1, ECO:0000313|Proteomes:UP000235918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cell103 {ECO:0000313|EMBL:PNE24192.1};
RA   Beall C.J., Campbell A.G., Griffen A.L., Podar M., Leys E.J.;
RT   "Genomics of the uncultivated, periodontitis-associated bacterium
RT   Tannerella sp. BU045 (oral taxon 808).";
RL   Submitted (SEP-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:PNE24192.1}.
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DR   EMBL; MIQB01000089; PNE24192.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N8N5Z3; -.
DR   Proteomes; UP000235918; 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:UP000235918};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          38..103
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   ACT_SITE        163
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ   SEQUENCE   353 AA;  40005 MW;  20072008762D7BCD CRC64;
     MTLDQALADG LFSEEETDNE EALYEHFRFT ADPNQSLLRI DKFLTDRMTH TSRNRIQLAA
     EAGWIRVDGQ PVKSNYRVKP GDIVTIVMTR PRHEFEILPE DIPLDIIYED PDLLVVNKPA
     GLVVHPGFGN YTGTLVNALA FHLRNLPGYD PNDPRLGLVH RIDKDTSGLL VVAKNVDAKT
     RLSRQFFEKT TSRRYLALSW GIPKEDEGRI EGNIGRDIHD RLRMAVYPAG SEEGKPAITH
     YHVAERLGYV SLLECELETG RTHQIRAHMS HIGHPIFNDT RYGGDHILKG RPTGSYRQFV
     LNAFALCPRQ ALHAETLGFI HPTTGRELFF SAPLPSDMQA LVDKWRDYCL SNT
//
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