ID   TYW2_RAT                Reviewed;         437 AA.
AC   Q4V8B8; Q6AXV3;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 85.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; BC079303; AAH79303.2; -; mRNA.
DR   EMBL; BC097456; AAH97456.2; -; mRNA.
DR   RefSeq; NP_001116448.1; NM_001122976.2.
DR   AlphaFoldDB; Q4V8B8; -.
DR   SMR; Q4V8B8; -.
DR   STRING; 10116.ENSRNOP00000011874; -.
DR   PaxDb; Q4V8B8; -.
DR   PRIDE; Q4V8B8; -.
DR   Ensembl; ENSRNOT00000011876; ENSRNOP00000011874; ENSRNOG00000008978.
DR   GeneID; 314999; -.
DR   KEGG; rno:314999; -.
DR   UCSC; RGD:1307127; rat.
DR   CTD; 55039; -.
DR   RGD; 1307127; Trmt12.
DR   eggNOG; KOG1227; Eukaryota.
DR   GeneTree; ENSGT00940000153304; -.
DR   HOGENOM; CLU_022610_1_0_1; -.
DR   InParanoid; Q4V8B8; -.
DR   OMA; WQRHGNL; -.
DR   OrthoDB; 736943at2759; -.
DR   PhylomeDB; Q4V8B8; -.
DR   TreeFam; TF314137; -.
DR   UniPathway; UPA00375; -.
DR   PRO; PR:Q4V8B8; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000008978; Expressed in skeletal muscle tissue and 19 other tissues.
DR   Genevisible; Q4V8B8; RN.
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..437
FT                   /note="tRNA wybutosine-synthesizing protein 2 homolog"
FT                   /id="PRO_0000281839"
FT   REGION          331..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         208
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT   BINDING         215
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT   BINDING         255
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT   BINDING         283..284
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT   CONFLICT        384
FT                   /note="W -> C (in Ref. 1; AAH79303)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   437 AA;  49387 MW;  942F4E30D55CF800 CRC64;
     MERECEKSVV VAVVTEPRFT QRYRDYLEKQ KLLDRQYRVE KLRDGTVALP VLAETLSEHH
     LQELKNRVAP GSTCKLTQLL DPLPSKKARV CSPAQRLCLE VRRWVEDRGV TWSTELEADL
     PRSWQRHGDL MLLSEDCFQA TQWKRLEPEL WETVASALGV QRLAKRGRVL PDGTRTPTVT
     LLLGDHGWVE HVDNGIRYKF DVTQCMFSFG NITEKLRVAS LSCAGEVLVD LYAGIGYFTL
     PFLVHAGAAF VHACEWNPHA VVALRKNLEI NGVADRCQIH FGDNRKLKLS NTADRVNLGL
     IPSSEEGWPI ACQVLRKDVG GILHIHQNVE SFSGKNPQPP GSSNMEKKHW PHPQKITTDK
     QGNRTTGSCM GEMSSASKPE WQRWAESAES QIASLLHQVH GKPWRTRILH VHPVKSYAPH
     VDHIVLDLEC RPCPLVG