ID A0A1V8ULB3_9PEZI Unreviewed; 371 AA.
AC A0A1V8ULB3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=B0A51_07546 {ECO:0000313|EMBL:OQO24123.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO24123.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-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 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}.
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:OQO24123.1}.
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DR EMBL; NAEU01000352; OQO24123.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8ULB3; -.
DR STRING; 1974281.A0A1V8ULB3; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000192386; 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:UP000192386};
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 69..364
FT /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT /evidence="ECO:0000259|PROSITE:PS51684"
SQ SEQUENCE 371 AA; 41747 MW; 13067E56EFA174CB CRC64;
MLHAVQQWRT QAGFSLSTED EYTLVKQLNH SYVIYGTLLL FPVSLLESQT WKAINGQDQT
ALQDLLILVA KHLKVTHIAV TKPIPPQVDG DDSQDNVVRS PSKFMPLYGD FGRETDGRPP
TQDDFNKAYW VTAKQNGVFQ TWAPRWTMFS RGNISEKARI LELPAVASAV AEGVEDGRGC
TAVDLYAGIG YFVFSYLKAG VSKVVCWDLN PWSIEGLRRG AAVNKRKTVT HAEHFGVDHM
VDEDARLLIF NESNEHAIDR LATLRRRLPP VRHVSCGLLP TSRGSWTTAF AVLDPIAGGW
VHVHENFELS EIADRAEGVR KEFQRMYDMT DHAEYAKVVL EHINRVKTYA PGVFHVVLDI
YIPPYRTAPC V
//
