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Database: UniProt
Entry: A0A061GHU1_THECC
LinkDB: A0A061GHU1_THECC
Original site: A0A061GHU1_THECC 
ID   A0A061GHU1_THECC        Unreviewed;       758 AA.
AC   A0A061GHU1;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
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};
GN   ORFNames=TCM_030223 {ECO:0000313|EMBL:EOY28697.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY28697.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY28697.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
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   EMBL; CM001884; EOY28697.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061GHU1; -.
DR   EnsemblPlants; EOY28697; EOY28697; TCM_030223.
DR   Gramene; EOY28697; EOY28697; TCM_030223.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000026915; Chromosome 6.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PF13964; Kelch_6; 1.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        669..687
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          567..758
FT                   /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51684"
SQ   SEQUENCE   758 AA;  83948 MW;  64D070EAACD40ED9 CRC64;
     MGMAQSVVRV VIVMKVRMVC REILEMPKLD IDPNETTPFS CQSLAGTDGI RSFSLSITKM
     VIVGEPVERL FLWGHSACTV DNIDKTMVLV FGGFGGIGRH ARRNDSFLLD PLLGNLKEIN
     VVGCPSPRLG HTSSLVGDCM FVIGGRADPL NILSDVWVLN TVKNEWRLLD CTGRAFPPRH
     RHAAAVVGSK IYVFGGLNND TISSSLHVLD TNTLQWEELV VHGEWPCARH SHSMVTYGSK
     LFMFGGYHGE KALGDLYSFD TQTCLWKVEK VGGRSPHARF SHSMFVYKNY IGIIGGCPVR
     QHCQELALLD IRSLVWKHVT LNSIDKELFV RCTANVVHDN LVMVGGGAAC YAFGTKFSEP
     VKIELLPLLS LDDHENAPKM GENQVNNQEE GMTANGNDLI QASHVGNALG STQSPKPQSL
     NVGNQMVASS WVVQLERKYA KLGKDILKKF GWLDLERKAY ALDDGLRISF PVTEKFCAIF
     PEDKFEGLID HHPSKTFRAE SVLLNEVSSS AALDILKKCG ATKLPDEVIE ARKASKSPLK
     IMTEAVASLI RHKGLSVKLL EQLPSRWERV GDIVVLPVSS FKDPVWDSIG EELWPIIARS
     LNTCRLARQG RVAPNGTRDS TLEILMGDSG WVDHRENGIL YSFDATKCMF SWGNLSEKMR
     MANLDCTDAV IVDLFAGIGY FVLPFLVRAK AKLVYACEWN PHAIEALKRN LQANSVSDRC
     IILEGDNRIT APKGVADRVC LGLLPSRVRV EYYTCMGM
//
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