ID A0A369S7J8_9METZ Unreviewed; 399 AA.
AC A0A369S7J8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=tRNA wybutosine-synthesizing protein 2 homolog {ECO:0000256|ARBA:ARBA00017179};
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=TrispH2_005197 {ECO:0000313|EMBL:RDD42003.1};
OS Trichoplax sp. H2.
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD42003.1, ECO:0000313|Proteomes:UP000253843};
RN [1] {ECO:0000313|EMBL:RDD42003.1, ECO:0000313|Proteomes:UP000253843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Panama {ECO:0000313|EMBL:RDD42003.1,
RC ECO:0000313|Proteomes:UP000253843};
RC TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD42003.1};
RX PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT "Trichoplax genomes reveal profound admixture and suggest stable wild
RT populations without bisexual reproduction.";
RL Sci. Rep. 8:11168-11168(2018).
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 -!- 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:RDD42003.1}.
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DR EMBL; NOWV01000063; RDD42003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369S7J8; -.
DR STRING; 287889.A0A369S7J8; -.
DR Proteomes; UP000253843; 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; 3.30.300.110; Met-10+ protein-like domains; 1.
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 PANTHER; PTHR23245; TRNA METHYLTRANSFERASE; 1.
DR PANTHER; PTHR23245:SF25; TRNA WYBUTOSINE-SYNTHESIZING PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF02475; Met_10; 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:UP000253843};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 127..399
FT /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT /evidence="ECO:0000259|PROSITE:PS51684"
SQ SEQUENCE 399 AA; 45242 MW; 4D9A666D2C405073 CRC64;
MEDKEAKATG QLLQCIEVTT AETQAVKAWL KQQALLHDEY KVKKMNGNLV VLPLCNNCTL
SQCQMLDLNK LCLSYRTVLI PMRSLQARKY KLDKISQPLH QSVADLYEKS TGIPLAANLA
AQIPNHWIKH DDMIVLPANS FTAQEWLALG DELWHLVCST LGAKRLAKNS AILNDNHRTP
NVEMLLGDCS WVTHMDNGIK YTFDITKCMF SPGNITEKIR ISNFDCSEEI IVDLYAGIGY
FVLPYLIHAK AKFVHACEWN PHAVEALEKS LILNKVREKC TVYFGDNRQH APKFIADRVN
LGLLPTSRPG WHIACAALRP DRGGWLHVHG NVNTYKVVQS ERKQFWQQWG EEVASELELI
LNQMHSDKSG WKATCKSVTH VKRYAPHIDH LIADVHCTV
//