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TRM1_PYRWO
ID   TRM1_PYRWO              Reviewed;          73 AA.
AC   P20300;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase;
DE            EC=2.1.1.216;
DE   AltName: Full=tRNA 2,2-dimethylguanosine-26 methyltransferase;
DE   AltName: Full=tRNA(guanine-26,N(2)-N(2)) methyltransferase;
DE   AltName: Full=tRNA(m(2,2)G26)dimethyltransferase;
DE   Flags: Fragment;
GN   Name=trm1;
OS   Pyrococcus woesei.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=2262;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49860 / DSM 3773 / JCM 8421 / Vul4;
RX   PubMed=2165475; DOI=10.1128/jb.172.8.4329-4338.1990;
RA   Zwickl P., Fabry S., Bogedain C., Haas A., Hensel R.;
RT   "Glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic
RT   archaebacterium Pyrococcus woesei: characterization of the enzyme, cloning
RT   and sequencing of the gene, and expression in Escherichia coli.";
RL   J. Bacteriol. 172:4329-4338(1990).
RN   [2]
RP   SIMILARITY.
RX   PubMed=7899076; DOI=10.1093/nar/23.4.565;
RA   Ouzounis C., Kyrpides N., Sander C.;
RT   "Novel protein families in archaean genomes.";
RL   Nucleic Acids Res. 23:565-570(1995).
CC   -!- FUNCTION: Dimethylates a single guanine residue at position 26 of a
CC       number of tRNAs using S-adenosyl-L-methionine as donor of the methyl
CC       groups. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) +
CC         N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43140, Rhea:RHEA-COMP:10359, Rhea:RHEA-COMP:10360,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.216;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00958};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Trm1 family. {ECO:0000255|PROSITE-ProRule:PRU00958}.
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DR   PIR; S10650; S10650.
DR   AlphaFoldDB; P20300; -.
DR   SMR; P20300; -.
DR   GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002905; Trm1.
DR   Pfam; PF02005; TRM; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51626; SAM_MT_TRM1; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; RNA-binding; S-adenosyl-L-methionine; Transferase;
KW   tRNA processing; tRNA-binding.
FT   CHAIN           1..>73
FT                   /note="tRNA (guanine(26)-N(2))-dimethyltransferase"
FT                   /id="PRO_0000147692"
FT   DOMAIN          6..73
FT                   /note="Trm1 methyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00958"
FT   NON_TER         73
SQ   SEQUENCE   73 AA;  8094 MW;  A5413AEFDF00C00C CRC64;
     MSMELFEVHE GKAKVLVPKA KTIYDSPVFY NPRMAPNRDV VVLLLNVLKP KIVLDALSAT
     GIRGIRFALE TPA
 
 
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