ID A0A1L0DKN7_9ASCO Unreviewed; 450 AA.
AC A0A1L0DKN7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMEA4029010_CIC11G00000003711 {ECO:0000313|EMBL:SGZ56456.1};
OS [Candida] intermedia.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ56456.1, ECO:0000313|Proteomes:UP000182334};
RN [1] {ECO:0000313|EMBL:SGZ56456.1, ECO:0000313|Proteomes:UP000182334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ56456.1,
RC ECO:0000313|Proteomes:UP000182334};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|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|ARBA:ARBA00004797, 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; LT635760; SGZ56456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L0DKN7; -.
DR STRING; 45354.A0A1L0DKN7; -.
DR OrthoDB; 122704at2759; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000182334; Chromosome v.
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:UP000182334};
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|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR038972}.
FT DOMAIN 168..444
FT /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT /evidence="ECO:0000259|PROSITE:PS51684"
SQ SEQUENCE 450 AA; 51046 MW; 36698C24989A87E3 CRC64;
MFGLRTFVSG HYTVQRSEVP YHPVKMPSKV GINNKHIIKS VKTLLEKHGI LDKSTKISSS
DGYSYIYSVA PVEDVESILD EYSDEIVVKE YLVPSAARSI SRSLESVVRA YLEDARAAGV
DVNVDLLMSK LPRKWSIYTP MVLFNTGGFD SEIWTEVFAS SINASSFFNV VRAAFPATIT
HFAINKPIVE EDVMRRPFNL VALHGDFGPE TSEVLFELPK PDDLEDAFWC HVVQNGIYQT
WAPRYTMFSR GNITEKKRVL DNFKNLKGLV VMDFYAGIGY FTLSYLANGG TLLCWELNPW
SIEGLVKGLS ENGYKYQVFS NGEFLTKEDY DRHLAQGVRA FVFHESNENV VTRLQQLGRL
PVSHINLGLL PSLQASWSTV KTVRDQWTSR DIVVHVHENE HKDRFEQLLS KIGDYFKGEV
IHFEKVKTFA PDIWHVVVDI GIGGGKEKEN
//