ID   TYW2_MACFA              Reviewed;         448 AA.
AC   Q4R3U8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 49.
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; ORFNames=QtsA-14055;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE02218.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB179167; BAE02218.1; ALT_FRAME; mRNA.
DR   AlphaFoldDB; Q4R3U8; -.
DR   SMR; Q4R3U8; -.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0102522; F:tRNA 4-demethylwyosine alpha-amino-alpha-carboxypropyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProt.
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..448
FT                   /note="tRNA wybutosine-synthesizing protein 2 homolog"
FT                   /id="PRO_0000281837"
FT   BINDING         218
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT   BINDING         225
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT   BINDING         265
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT   BINDING         293..294
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
SQ   SEQUENCE   448 AA;  50254 MW;  E35D30DB65CCA5DE CRC64;
     MGENVVVSNM ERETGKPVAV VAVVTEPRFT QRYREYLERQ KLFDTQHRVE KMPDGWVALP
     VLGETLPEQH LQELRNRVAP GSACMLTRLP DPVPSKRAQG CSPAQKLCLE VSRWVEGRGV
     KWSAELEADL PRSWQRHGNL LLLSEDCFQA NQWKNLGPEL WETVASALGV QRLAKRGRVS
     PDGTRTPAVT LLLGDHGWVE HVDNGILYKF DVTQCMFSFG NITEKLRVAS LSCAGEVLVD
     LYAGIGYFTL PFLVHAGAAF VHACEWNPHA VVALRNNLEI NGVADRCQIH FGDNRKLKLS
     NIADRVILGL IPSSEEGWPI ACQVLRQDAG GILHIHQNVE SFPGKNLQPL EVSKTEKEHW
     LYPQQITTNQ WKNGATRDTR GKMLSPATKP EWQRWAESAE TRIATLLQQV HGKPWKTQIL
     HIQPVKSYAP HVDHIVLDLE CCPCPSVG