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Database: UniProt
Entry: A0A453BEB5_AEGTS
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ID   A0A453BEB5_AEGTS        Unreviewed;       759 AA.
AC   A0A453BEB5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase {ECO:0000256|ARBA:ARBA00012265};
DE            EC=2.5.1.114 {ECO:0000256|ARBA:ARBA00012265};
DE   AltName: Full=tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase {ECO:0000256|ARBA:ARBA00031315};
OS   Aegilops tauschii subsp. strangulata (Goatgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET2Gv20475500.4, ECO:0000313|Proteomes:UP000015105};
RN   [1] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=25035499; DOI=10.1126/science.1250092;
RG   International Wheat Genome Sequencing Consortium,;
RA   Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA   Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT   "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL   Science 345:1250092-1250092(2014).
RN   [2] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA   Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA   Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT   "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL   Nat. Plants 3:946-955(2017).
RN   [3] {ECO:0000313|EnsemblPlants:AET2Gv20475500.4}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2019) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00037786}.
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         Evidence={ECO:0000256|ARBA:ARBA00036405};
CC   -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004797}.
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DR   AlphaFoldDB; A0A453BEB5; -.
DR   EnsemblPlants; AET2Gv20475500.4; AET2Gv20475500.4; AET2Gv20475500.
DR   Gramene; AET2Gv20475500.4; AET2Gv20475500.4; AET2Gv20475500.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000015105; Chromosome 2D.
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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR   Gene3D; 3.30.300.110; Met-10+ protein-like domains; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR23245; TRNA METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR23245:SF25; TRNA WYBUTOSINE-SYNTHESIZING PROTEIN 2 HOMOLOG; 1.
DR   Pfam; PF01344; Kelch_1; 2.
DR   Pfam; PF02475; Met_10; 1.
DR   SUPFAM; SSF117281; Kelch motif; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000015105};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          527..759
FT                   /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51684"
SQ   SEQUENCE   759 AA;  83958 MW;  58B17FFC8A28136E CRC64;
     MHEGKLSASS GIRSSHLSIT ELKISGEPVE KLFLWGQSAC AFTIGGKQQV LTFGGFGGPG
     RHSRRNYSLL LDRTSGLLKE INVKDSPSPR MGHTTTAVGN HIYAVGGRAG PSEILGDVWV
     LQSTENRWSR VECSGDIFHP RHRHAAAAAA LKIYVFGGLS NEGIYSCLNI LDTESMRWNV
     ISAAGEWPCA RHSHSLVSYG STLFMFGGHD GQRALNDFYS FDTTTLSWNK EITSGRTPSP
     RFSHCMFIYK HYIGILGGCP IRENNQEIAL LHLKHRVWFH VSIPALGQCL CVRSSSVVTD
     DDLVVIGGGA SCYAFGTKFC QPVKIDLHLL ESVFELAYKK NDNAVQSWDA TYTMDLKERE
     QNGTFISHKV KSMVDAATNG IAGSDPLVFQ LEKKYAKLAK DILKKFGWLD LARKVRVSQD
     NVLVLFPVSR NFHTLVTDQH SKLLDDDSCI SKGLLGCPEK KLIGDSIALH EALEILSSFH
     GSFLKDELAL SRKAYKSPQI IMRELISSLL ERKGMPSWLL EQLPTRWETL GDITVLPKTC
     FKDLLWESVR EELWQLVAKS LGAQRLARQG KIMPNGTRDS TLELLVGDNG WVTHYENGIS
     YSLDATKCMF SSGNRSEKLR MGQLDCRDEV VVDLFSGIGY FVLPFLVKAN AKLVYACEWN
     PHALEALQRN VMDNHVADRC VILEGDNRLT APKGVADRVC LGLIPSSECS WATAVRALRV
     GGGVLHIHGN VNDSDEARWL DNVVESISSI ATARGTACL
//
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