ID A0A0A1T2Z6_9HYPO Unreviewed; 373 AA.
AC A0A0A1T2Z6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=tRNA wybutosine-synthesizing protein 2 {ECO:0000256|PIRNR:PIRNR038972};
DE Short=tRNA-yW-synthesizing protein 2 {ECO:0000256|PIRNR:PIRNR038972};
DE AltName: Full=tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase {ECO:0000256|PIRNR:PIRNR038972};
GN ORFNames=VHEMI07278 {ECO:0000313|EMBL:CEJ91576.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ91576.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ91576.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(2015).
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 ECO:0000256|PIRNR:PIRNR038972}.
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|PIRNR:PIRNR038972}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR038972}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM5/TYW2 family. {ECO:0000256|PIRNR:PIRNR038972}.
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DR EMBL; CDHN01000004; CEJ91576.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1T2Z6; -.
DR STRING; 1531966.A0A0A1T2Z6; -.
DR HOGENOM; CLU_023588_0_0_1; -.
DR OrthoDB; 122704at2759; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000039046; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0031591; P:wybutosine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR026274; tRNA_wybutosine_synth_prot_2.
DR PANTHER; PTHR23245; TRNA METHYLTRANSFERASE; 1.
DR PANTHER; PTHR23245:SF25; TRNA WYBUTOSINE-SYNTHESIZING PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF02475; Met_10; 1.
DR PIRSF; PIRSF038972; Trm12; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR038972};
KW Reference proteome {ECO:0000313|Proteomes:UP000039046};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR038972};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR038972};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR038972}.
FT DOMAIN 82..372
FT /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT /evidence="ECO:0000259|PROSITE:PS51684"
SQ SEQUENCE 373 AA; 41537 MW; 2AFC34BB1BF3FC61 CRC64;
MPKPPPYNPM QSAVSKWAAQ ATCIDDGVAA GLLATAPKRF TIYEPMAIFP SGSFTSPIWA
RTISQCSESD LSPLWITIAQ ELSNVAKSPV THLAINEGIP LLKGGETEEN ILRSPTGLQM
IHGDFGPSQT ESEQPTDAEF NVALWVTTKQ NGIHQTWAPR WTMFSRGNVK EKARLLTFPR
PAAQEDAPWA VDMYAGIGYF VFSYATMGMR ILGWELNPWS VEGLRRGALM NKWTVKVVRG
QDLTLPMTEI MATGEQIVIF QDDNQNAQSK IAELHDMETA HNIRHLNGGL LPTSELIWQA
AAAITSKSPE TWLHLHENVA TDDIEGQAEE MEARFKTWTQ GTVAECRSSH VEKVKTFAPG
VWHCVFDIYI RRT
//
