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Database: UniProt
Entry: A0L0I8
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Original site: A0L0I8 
ID   TRMN6_SHESA             Reviewed;         241 AA.
AC   A0L0I8;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   01-OCT-2014, entry version 53.
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=Shewana3_3333;
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANA-3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Newman D., Salticov C., Konstantinidis K., Klappenback J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the adenine in position 37 of
CC       tRNA(1)(Val) (anticodon cmo5UAC). {ECO:0000255|HAMAP-
CC       Rule:MF_01872}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + adenine(37) in
CC       tRNA(1)(Val) = S-adenosyl-L-homocysteine + N(6)-methyladenine(37)
CC       in tRNA(1)(Val). {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}.
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DR   EMBL; CP000469; ABK49557.1; -; Genomic_DNA.
DR   RefSeq; WP_011718136.1; NC_008577.1.
DR   RefSeq; YP_870963.1; NC_008577.1.
DR   ProteinModelPortal; A0L0I8; -.
DR   STRING; 94122.Shewana3_3333; -.
DR   EnsemblBacteria; ABK49557; ABK49557; Shewana3_3333.
DR   GeneID; 4477634; -.
DR   KEGG; shn:Shewana3_3333; -.
DR   PATRIC; 23574654; VBISheSp134792_3693.
DR   eggNOG; COG4123; -.
DR   HOGENOM; HOG000283147; -.
DR   KO; K15460; -.
DR   OMA; FKQFHIN; -.
DR   OrthoDB; EOG66TGB2; -.
DR   BioCyc; SSP94122:GJ9K-3447-MONOMER; -.
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:InterPro.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01872; tRNA_methyltr_YfiC; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases-like.
DR   InterPro; IPR022882; tRNA_adenine-N6_MeTrfase.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN         1    241       tRNA1(Val) (adenine(37)-N6)-
FT                                methyltransferase.
FT                                /FTId=PRO_0000387428.
SQ   SEQUENCE   241 AA;  27119 MW;  48EECDE26762E5BF CRC64;
     MAFTFKQFHI DDLNCGMPVS TDGVILGAWA PLSRAKHILD IGAGSGLLSL MAAQRSQGQI
     TAVELEEKAA AACQYNMTQS PWADRCKLIH GDIQHVCQQA EYQEYFDHII CNPPYFEHGP
     KANEQHRAMA RHTDTLGFTP LLEAISQCLS HEGHASLILP IQSLTRFKAC LHQTQLYLVK
     EVRVKSMENK DANRVLLLLA KILLTQSQDE PCQHTELTLR GEDGRYTEQM IALTKDFYLK
     L
//
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