ID   TYW2_BOVIN              Reviewed;         438 AA.
AC   Q58D65;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=tRNA wybutosine-synthesizing protein 2 homolog;
DE            Short=tRNA-yW-synthesizing protein 2;
DE            EC=2.5.1.114;
DE   AltName: Full=tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase;
GN   Name=TRMT12; Synonyms=TYW2;
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).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent transferase that acts as a
CC       component of the wybutosine biosynthesis pathway. Wybutosine is a hyper
CC       modified guanosine with a tricyclic base found at the 3'-position
CC       adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes
CC       the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-
CC       adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14)
CC       to produce wybutosine-86 (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-demethylwyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine =
CC         4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) +
CC         H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:36355, Rhea:RHEA-
CC         COMP:10164, Rhea:RHEA-COMP:10378, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17509, ChEBI:CHEBI:59789, ChEBI:CHEBI:64315,
CC         ChEBI:CHEBI:73550; EC=2.5.1.114;
CC   -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TRM5/TYW2 family. {ECO:0000255|PROSITE-ProRule:PRU01021}.
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DR   EMBL; BT021732; AAX46579.1; -; mRNA.
DR   RefSeq; NP_001019723.1; NM_001024552.1.
DR   AlphaFoldDB; Q58D65; -.
DR   SMR; Q58D65; -.
DR   STRING; 9913.ENSBTAP00000027186; -.
DR   PaxDb; Q58D65; -.
DR   PRIDE; Q58D65; -.
DR   GeneID; 516516; -.
DR   KEGG; bta:516516; -.
DR   CTD; 55039; -.
DR   eggNOG; KOG1227; Eukaryota.
DR   InParanoid; Q58D65; -.
DR   OrthoDB; 736943at2759; -.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0102522; F:tRNA 4-demethylwyosine alpha-amino-alpha-carboxypropyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF02475; Met_10; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE   2: Evidence at transcript level;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..438
FT                   /note="tRNA wybutosine-synthesizing protein 2 homolog"
FT                   /id="PRO_0000281835"
FT   BINDING         209
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT   BINDING         216
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT   BINDING         256
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT   BINDING         284..285
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
SQ   SEQUENCE   438 AA;  49268 MW;  9951E07649892CA1 CRC64;
     MEGAGGKPTA VVAVVTEPRF TQRYREYLEK HKLLDRQHRV KKLRDGTVAL PVLREALLEQ
     HLRELRNRVA PGSTCVPTQL LDPVPSKKAQ SYSPAQRLCL EVSRWVEGRG VTWSAKLEAD
     LPRSWQRHGD LLLLSEDCFQ AKQWRHLEPE LWETVASALG AQRLAKRGRV SPDSTRTPAV
     SLLLGDHGWV EHVDNGIRYK FDVTQCMFSF GNITEKLRVA SLPCVGEVLV DLYAGIGYFT
     LPFLVHAEAA FVHACEWNPH AVVALRNNLE LNGVADRCQI HFGDNRKLKL SNVADRVNLG
     LIPSSEEGWP IACRVLKQDA GGILHIHQNV ESFPGKTLQP PGSSEMEEHW PSPHQIISNQ
     LNNGATSDSR RKTLSVATKP EWQRWAKAAE TRIATLLHQV HGKRWKTQIL HIQPVKSYAP
     HVDHIVLDLE CRPCHLVG