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Database: UniProt
Entry: A0A2I0HHV8_PUNGR
LinkDB: A0A2I0HHV8_PUNGR
Original site: A0A2I0HHV8_PUNGR 
ID   A0A2I0HHV8_PUNGR        Unreviewed;       760 AA.
AC   A0A2I0HHV8;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, 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};
GN   ORFNames=CRG98_048405 {ECO:0000313|EMBL:PKI31203.1};
OS   Punica granatum (Pomegranate).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Lythraceae; Punica.
OX   NCBI_TaxID=22663 {ECO:0000313|EMBL:PKI31203.1, ECO:0000313|Proteomes:UP000233551};
RN   [1] {ECO:0000313|EMBL:PKI31203.1, ECO:0000313|Proteomes:UP000233551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AG2017 {ECO:0000313|Proteomes:UP000233551};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PKI31203.1};
RA   Akparov Z., Amiraslanov A., Hajiyeva S., Abbasov M., Kaur K., Hamwieh A.,
RA   Solovyev V., Salamov A., Braich B., Kosarev P., Mahmoud A., Hajiyev E.,
RA   Babayeva S., Izzatullayeva V., Mammadov A., Mammadov A., Sharifova S.,
RA   Ojaghi J., Eynullazada K., Bayramov B., Abdulazimova A., Shahmuradov I.;
RT   "De-novo sequencing of pomegranate (Punica granatum L.) genome.";
RL   Submitted (NOV-2017) 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. {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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PKI31203.1}.
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DR   EMBL; PGOL01009137; PKI31203.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0HHV8; -.
DR   STRING; 22663.A0A2I0HHV8; -.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000233551; Unassembled WGS sequence.
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; IPR011498; Kelch_2.
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; PF07646; Kelch_2; 1.
DR   Pfam; PF13418; Kelch_4; 1.
DR   Pfam; PF13964; Kelch_6; 1.
DR   Pfam; PF02475; Met_10; 1.
DR   SMART; SM00612; Kelch; 3.
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:UP000233551};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          498..757
FT                   /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51684"
SQ   SEQUENCE   760 AA;  83855 MW;  B31317B12DFBD7D4 CRC64;
     MPIEKLFLWG HSACVIDKGS TKKVLVHGGF GGMGRHARRN DSLLLDPLDG TVEAIDTAGA
     PSPRMGHTAS LIGEQMFVIG GRADPTSILS EIWALNTATN QWTLLNCNGD SFPPRHRHAA
     AVLGSRIYVF GGLNNDTIFS SIFVLDEKDL RWEELKVGGE QPCARHSHSM VAFGSQIFMF
     GGYNGEKALG DLYSFNVKTR VWRKEKALGR SPYARFSHSM FVYKHCLGII GGCPVKQHFQ
     ELSLLDMHSQ SWKHFSLNSV GKELFVRSTV SVVGDDLVIV GGGASCYAFG TKFSEPMNIA
     LHTLAASNQF PFNCQQVQQL ENPQNLGEAL GSSSEDGKGL SETWKSASNW YLQFERKHAK
     PGKDLLKKFG WLDHGRKVCS SSNGTRICFP VTEKLYILFH EKGRVDPSID TSHGSESNIV
     ELPPLKESVG QGISLNEISS SKALNLLKQC GGTILAYETA EFRKSVRSPS IVIKQAAASL
     IKQKGLPEKL LEQLPSRWER LGDIVVLPGT SFKDPLWDTI GGELWPIIAK ALNTNRLARQ
     GCVAPTGTRD STLKMLVGDN GWVDHRENGI LYSFDATKCM FSWGNLSEKL RMARLDCGDE
     IIVDLFAGIG YFTLSFLVRA KAKLVYACEW NPHAIEALHH NLKANSVADR CIVLEGDNRI
     TAPKGVADRV CLGLLPSSEG SWVTAVRVLR KEGGMLHVHG NVKDSDENTW VEHVANSIHS
     IATSEGRCWE VTIGHVERVK WYAPHIRHLV ADVRCKGNQR
//
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