TYW32_PYRFU
ID TYW32_PYRFU Reviewed; 206 AA.
AC Q8TZG0;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00266};
DE EC=2.1.1.282 {ECO:0000255|HAMAP-Rule:MF_00266};
DE AltName: Full=tRNA wyosine derivatives biosynthesis protein Taw3 2 {ECO:0000255|HAMAP-Rule:MF_00266};
GN Name=taw3-2 {ECO:0000255|HAMAP-Rule:MF_00266}; OrderedLocusNames=PF2034;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that acts
CC as a component of the wyosine derivatives biosynthesis pathway.
CC Probably methylates N-4 position of wybutosine-86 to produce
CC wybutosine-72. {ECO:0000255|HAMAP-Rule:MF_00266}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in
CC tRNA(Phe) + S-adenosyl-L-methionine = 7-[(3S)-3-amino-3-
CC carboxypropyl]wyosine(37) in tRNA(Phe) + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:36635, Rhea:RHEA-COMP:10378, Rhea:RHEA-
CC COMP:10379, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73543, ChEBI:CHEBI:73550; EC=2.1.1.282;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00266};
CC -!- SIMILARITY: Belongs to the TYW3 family. {ECO:0000255|HAMAP-
CC Rule:MF_00266}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL82158.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE009950; AAL82158.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_014835510.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8TZG0; -.
DR SMR; Q8TZG0; -.
DR STRING; 186497.PF2034; -.
DR EnsemblBacteria; AAL82158; AAL82158; PF2034.
DR GeneID; 41713856; -.
DR KEGG; pfu:PF2034; -.
DR PATRIC; fig|186497.12.peg.2111; -.
DR eggNOG; arCOG04156; Archaea.
DR HOGENOM; CLU_047426_2_0_2; -.
DR OMA; GFKYTTF; -.
DR OrthoDB; 118297at2157; -.
DR PhylomeDB; Q8TZG0; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0031591; P:wybutosine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.1960.10; -; 1.
DR HAMAP; MF_00266; TYW3_archaea; 1.
DR InterPro; IPR022908; Taw3.
DR InterPro; IPR003827; tRNA_yW-synthesising.
DR InterPro; IPR036602; tRNA_yW-synthesising-like_sf.
DR Pfam; PF02676; TYW3; 1.
DR SUPFAM; SSF111278; SSF111278; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..206
FT /note="tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-
FT demethylwyosine(37)-N(4))-methyltransferase 2"
FT /id="PRO_0000157099"
SQ SEQUENCE 206 AA; 23469 MW; 33B0FBF85FE4D502 CRC64;
MKAKREALLS LFQAIKENKV DEDIVELLLL INSIKGVYTT SSCSGRIGII EEPSLGAKPL
SRWLIKVHRP IKFEEAKKAL KNAQKGLIFL KSQPPIFHVV TESLELARKI HEIGLSSGFK
YTTYKVISRR YLVEINGTEY LTVPLGKDGK VFVTDEYLEF VIEIGNQMLM RGKSRLPRLR
EKFEELKEEV GEDPLFTTLS TEKLSL