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Database: UniProt
Entry: A0A2G5TMI3_9PELO
LinkDB: A0A2G5TMI3_9PELO
Original site: A0A2G5TMI3_9PELO 
ID   A0A2G5TMI3_9PELO        Unreviewed;       489 AA.
AC   A0A2G5TMI3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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   Name=Cni-F40F9.10 {ECO:0000313|EMBL:PIC28321.1};
GN   Synonyms=Cnig_chr_V.g20281 {ECO:0000313|EMBL:PIC28321.1};
GN   ORFNames=B9Z55_020281 {ECO:0000313|EMBL:PIC28321.1};
OS   Caenorhabditis nigoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC28321.1, ECO:0000313|Proteomes:UP000230233};
RN   [1] {ECO:0000313|Proteomes:UP000230233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA   Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA   Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT   "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT   competition proteins.";
RL   Submitted (OCT-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   -!- 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:PIC28321.1}.
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DR   EMBL; PDUG01000005; PIC28321.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5TMI3; -.
DR   Proteomes; UP000230233; Chromosome v.
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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          71..270
FT                   /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT                   /evidence="ECO:0000259|Pfam:PF02475"
FT   REGION          281..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..322
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   489 AA;  55588 MW;  A6305E62149AC8FF CRC64;
     MSSPLKTHCN HFSSGPTRDQ LMERTSSLRR KTSDGVLAKA SNFGQMLEDV RKLALSKSLW
     DDEMQRDLPK KWEKHGDMIV FPQNTFTHIN WRYIGRELWA VVAQSLNVAR VGRKRQIDEE
     RTAHVDLLHG ADAWVDYVDE RGIKFCYNAT VRVFDNSKKA EMKRISKWAC QGQTIVDMYA
     SLGYYSLTFL VSCEAKQVVA IDWNDEILES LIRSAQVNQV DDRLLVIHGD CRRVCPDQTA
     DRVYLGLLPS CRAHWLAACK ALKPDGGIIH INEILDMNEK KKEPVKKVEP EKASSVEKKK
     KTVTEGKEKT SSDKENLPKK KKVLRQKTLP VLSAVHEDST KPETESTSAP PAEPSADQNP
     PPEANGAPEA SEEGVEKKKK FTRSASIVEE MENRVLPEIK VWKEYENEGW SRLTNRHQEF
     AMDCAQSCTR FLNNIHLSDV MYSVTVVNMI RYGEVSKGKE HVVLELLCCQ QDASAEHLIS
     KFNSENLKS
//
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