ID   TYW3_BOVIN              Reviewed;         258 AA.
AC   Q5E9U4; Q24K18;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=tRNA wybutosine-synthesizing protein 3 homolog;
DE            Short=tRNA-yW-synthesizing protein 3;
DE            EC=2.1.1.282;
DE   AltName: Full=tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase;
GN   Name=TYW3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase
CC       that acts as a component of the wybutosine biosynthesis pathway.
CC       Wybutosine is a hyper modified guanosine with a tricyclic base found at
CC       the 3'-position adjacent to the anticodon of eukaryotic phenylalanine
CC       tRNA (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in
CC         tRNA(Phe) + S-adenosyl-L-methionine = 7-[(3S)-3-amino-3-
CC         carboxypropyl]wyosine(37) in tRNA(Phe) + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:36635, Rhea:RHEA-COMP:10378, Rhea:RHEA-
CC         COMP:10379, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:73543, ChEBI:CHEBI:73550; EC=2.1.1.282;
CC   -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC   -!- SIMILARITY: Belongs to the TYW3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI14026.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BT020826; AAX08843.1; -; mRNA.
DR   EMBL; BC114025; AAI14026.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_001015620.1; NM_001015620.1.
DR   AlphaFoldDB; Q5E9U4; -.
DR   SMR; Q5E9U4; -.
DR   STRING; 9913.ENSBTAP00000006849; -.
DR   PaxDb; Q5E9U4; -.
DR   PRIDE; Q5E9U4; -.
DR   Ensembl; ENSBTAT00000006849; ENSBTAP00000006849; ENSBTAG00000005196.
DR   GeneID; 519731; -.
DR   KEGG; bta:519731; -.
DR   CTD; 127253; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005196; -.
DR   VGNC; VGNC:36554; TYW3.
DR   eggNOG; KOG1228; Eukaryota.
DR   GeneTree; ENSGT00940000153304; -.
DR   HOGENOM; CLU_047426_1_1_1; -.
DR   InParanoid; Q5E9U4; -.
DR   OMA; GKWHHYA; -.
DR   OrthoDB; 1313208at2759; -.
DR   TreeFam; TF329327; -.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000005196; Expressed in tongue muscle and 105 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR   Gene3D; 3.30.1960.10; -; 1.
DR   InterPro; IPR003827; tRNA_yW-synthesising.
DR   InterPro; IPR036602; tRNA_yW-synthesising-like_sf.
DR   Pfam; PF02676; TYW3; 1.
DR   SUPFAM; SSF111278; SSF111278; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Phosphoprotein; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..258
FT                   /note="tRNA wybutosine-synthesizing protein 3 homolog"
FT                   /id="PRO_0000281841"
FT   REGION          199..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..251
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BSA9"
FT   CONFLICT        170
FT                   /note="L -> Q (in Ref. 2; AAI14026)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   258 AA;  29303 MW;  B0ABAB3BB79E095C CRC64;
     MDLSAEFKRW KAQCLSKADL SRKGSVDEDV LEIVQLLNGQ EQFFTTSSCA GRIILLDRSV
     NGSEVQKQNC CWLLVTHKAC VKDDVIVALQ KAKGDAILKF EPLVLHVQCR QLQDAQILHS
     VAIDSGFRNS GITVGKRGKT MLAVRSTHGL EVPLSHQGKL MVTEEYINFL LKIANQKMEE
     NKKRIERFYH CLQHALEKET VSTTSQPKEK VNTSYIRKKK RNPGKARGKR VNEEHDKELE
     NNDHDDPGIS DTIFPEDY