ID   TYW2_DANRE              Reviewed;         408 AA.
AC   Q0P466;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=zgc:153361;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2006) 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}.
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DR   EMBL; BC122254; AAI22255.1; -; mRNA.
DR   RefSeq; NP_001070632.1; NM_001077164.1.
DR   AlphaFoldDB; Q0P466; -.
DR   SMR; Q0P466; -.
DR   STRING; 7955.ENSDARP00000079349; -.
DR   PaxDb; Q0P466; -.
DR   GeneID; 564925; -.
DR   KEGG; dre:564925; -.
DR   CTD; 55039; -.
DR   ZFIN; ZDB-GENE-060825-182; trmt12.
DR   eggNOG; KOG1227; Eukaryota.
DR   InParanoid; Q0P466; -.
DR   OrthoDB; 736943at2759; -.
DR   PhylomeDB; Q0P466; -.
DR   UniPathway; UPA00375; -.
DR   PRO; PR:Q0P466; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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..408
FT                   /note="tRNA wybutosine-synthesizing protein 2 homolog"
FT                   /id="PRO_0000281840"
FT   BINDING         201
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT   BINDING         208
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT   BINDING         248
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT   BINDING         276..277
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
SQ   SEQUENCE   408 AA;  45530 MW;  D063A70E0D044273 CRC64;
     MDVVPCLKVP QRHAQMYRKY LESQGVLDRR YGAEKHSDGT VTLLVVASAL PQLDLVALKE
     HVAHDSFCEI VDIQAQLSKK SKVKSVHMKL VEAARSFLLS KGKEWSEDLG RDIPGRWQCH
     GDLVLFTEGC FSNAVWKEIG SEFWTAVALT LGVKRIAQIK KISQDGYRTP IVTMLLGDSS
     HVTHIDNHIR YEFDVTKCMF SSGNITEKLR IASFDCSGET VVDLYAGIGY FTLPYLVHAN
     AAHVHACEWN PDAVAALQRN LEINGVSNRC TVHQGDNRQL SLSDLADRVN LGLIPSSEEG
     WPVACRLLKR STGGIMHIHQ NVTAPFHHEP SELNSSVEGS SVEVSPLRIQ KDMQVWTAWA
     SETAKRICTL LLGITGSEWK TNIRHIEHVK TYAPHISHVV LDLECKPL