ID L5LBQ3_MYODS Unreviewed; 224 AA.
AC L5LBQ3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=tRNA pseudouridine synthase {ECO:0000256|RuleBase:RU003792};
DE EC=5.4.99.12 {ECO:0000256|RuleBase:RU003792};
GN ORFNames=MDA_GLEAN10007545 {ECO:0000313|EMBL:ELK23617.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK23617.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA;
CC Xref=Rhea:RHEA:22376, Rhea:RHEA-COMP:10085, Rhea:RHEA-COMP:10087,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.12;
CC Evidence={ECO:0000256|RuleBase:RU003792};
CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC {ECO:0000256|ARBA:ARBA00009375, ECO:0000256|RuleBase:RU003792}.
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DR EMBL; KB113360; ELK23617.1; -; Genomic_DNA.
DR AlphaFoldDB; L5LBQ3; -.
DR eggNOG; KOG4393; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.660; Pseudouridine synthase I, catalytic domain, C-terminal subdomain; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR001406; PsdUridine_synth_TruA.
DR InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom.
DR InterPro; IPR020095; PsdUridine_synth_TruA_C.
DR PANTHER; PTHR11142; PSEUDOURIDYLATE SYNTHASE; 1.
DR PANTHER; PTHR11142:SF0; TRNA PSEUDOURIDINE SYNTHASE-LIKE 1; 1.
DR Pfam; PF01416; PseudoU_synth_1; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU003792};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|RuleBase:RU003792}.
FT DOMAIN 82..153
FT /note="Pseudouridine synthase I TruA alpha/beta"
FT /evidence="ECO:0000259|Pfam:PF01416"
FT REGION 189..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 224 AA; 24669 MW; F6AFB73CC50D8153 CRC64;
MPPHPLREPQ AEQAAVGGQA QRVLQAFRVP SDFHARYAAT SRTYMYRLVT GCPRHDQLSV
FERNRCWAVH ADRLDVAAMR EAAQHLLGTH DFSAFQSAGS PSASSVRTLR RASVSPDPAG
PLVLPQESRR LQFWSLEFES QSFLYRQVKR ILQSRDPLGR HQTRVAPAHG LFLKSVLFGG
LRDLAVGSPD CAQQESQGPG GREALGSPDD FRLETSGPKA GGLE
//
