(data stored in SCRATCH3701 zone)

SWISSPROT: TRMN6_VIBVY

ID   TRMN6_VIBVY             Reviewed;         239 AA.
AC   Q7MNQ4;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 2.
DT   11-DEC-2019, entry version 97.
DE   RecName: Full=tRNA1(Val) (adenine(37)-N6)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01872};
DE            EC=2.1.1.223 {ECO:0000255|HAMAP-Rule:MF_01872};
DE   AltName: Full=tRNA m6A37 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01872};
GN   OrderedLocusNames=VV0662;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- FUNCTION: Specifically methylates the adenine in position 37 of
CC       tRNA(1)(Val) (anticodon cmo5UAC). {ECO:0000255|HAMAP-Rule:MF_01872}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43160, Rhea:RHEA-COMP:10369, Rhea:RHEA-COMP:10370,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=2.1.1.223;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01872};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01872}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. tRNA
CC       (adenine-N(6)-)-methyltransferase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01872}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC93425.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; BA000037; BAC93425.1; ALT_INIT; Genomic_DNA.
DR   STRING; 672.VV93_v1c06010; -.
DR   EnsemblBacteria; BAC93425; BAC93425; BAC93425.
DR   KEGG; vvy:VV0662; -.
DR   HOGENOM; HOG000283147; -.
DR   KO; K15460; -.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0016430; F:tRNA (adenine-N6-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01872; tRNA_methyltr_YfiC; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   InterPro; IPR022882; tRNA_adenine-N6_MeTrfase.
DR   Pfam; PF05175; MTS; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7MNQ4.
DR   SWISS-2DPAGE; Q7MNQ4.
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..239
FT                   /note="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
FT                   /id="PRO_0000387449"
SQ   SEQUENCE   239 AA;  26579 MW;  4E3A06744E72DD9B CRC64;
     MKSGTLKTKG FKFKQFSIAS SNSGMPVSTD GVLLGAWADF HHSQNLLDIG TGTGLLSLMC
     AQRYAHLSIT AVDIDAHAME AAQENFSHSP WHSRLHLQHG DVLKLNFTHR FDGIICNPPY
     FNSGEQAQAT QRATARHTDT LAHDALLLRC RELLTPNGKA NFVLPLTEGE QFLQLAQQQG
     WHLHRLCRVK PSPNKPVHRL LFELGLSTAT TSEEHLTIND GSTYSAAFVK LCQDFYLKM
//

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