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DescriptionRecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000256|HAMAP-Rule:MF_00290}; EC=2.1.1.216 {ECO:0000256|HAMAP-Rule:MF_00290}; AltName: Full=tRNA 2,2-dimethylguanosine-26 methyltransferase {ECO:0000256|HAMAP-Rule:MF_00290}; AltName: Full=tRNA(guanine-26,N(2)-N(2)) methyltransferase {ECO:0000256|HAMAP-Rule:MF_00290}; AltName: Full=tRNA(m(2,2)G26)dimethyltransferase {ECO:0000256|HAMAP-Rule:MF_00290};
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MyHits synonymsA2BK15_HYPBU , A2BK15 , 4DF0E2A9CE1D4EF5
match map segment
ihamap:tRNA_dimethyltr_TRM1 iprf:SAM_MT_TRM1 ipfam:TRM  
ID   A2BK15_HYPBU            Unreviewed;       396 AA.
AC   A2BK15;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   10-MAY-2017, entry version 66.
DE   RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000256|HAMAP-Rule:MF_00290};
DE            EC=2.1.1.216 {ECO:0000256|HAMAP-Rule:MF_00290};
DE   AltName: Full=tRNA 2,2-dimethylguanosine-26 methyltransferase {ECO:0000256|HAMAP-Rule:MF_00290};
DE   AltName: Full=tRNA(guanine-26,N(2)-N(2)) methyltransferase {ECO:0000256|HAMAP-Rule:MF_00290};
DE   AltName: Full=tRNA(m(2,2)G26)dimethyltransferase {ECO:0000256|HAMAP-Rule:MF_00290};
GN   Name=trm1 {ECO:0000256|HAMAP-Rule:MF_00290};
GN   OrderedLocusNames=Hbut_0460 {ECO:0000313|EMBL:ABM80326.1};
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Pyrodictiaceae; Hyperthermus.
OX   NCBI_TaxID=415426 {ECO:0000313|EMBL:ABM80326.1, ECO:0000313|Proteomes:UP000002593};
RN   [1] {ECO:0000313|EMBL:ABM80326.1, ECO:0000313|Proteomes:UP000002593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5
RC   {ECO:0000313|Proteomes:UP000002593};
RX   PubMed=17350933;
RA   Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A.,
RA   Awayez M., She Q., Garrett R.A., Klenk H.-P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
CC   -!- FUNCTION: Dimethylates a single guanine residue at position 26 of
CC       a number of tRNAs using S-adenosyl-L-methionine as donor of the
CC       methyl groups. {ECO:0000256|HAMAP-Rule:MF_00290}.
CC   -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + guanine(26) in
CC       tRNA = 2 S-adenosyl-L-homocysteine + N(2)-dimethylguanine(26) in
CC       tRNA. {ECO:0000256|HAMAP-Rule:MF_00290}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. Trm1 family. {ECO:0000256|HAMAP-
CC       Rule:MF_00290, ECO:0000256|PROSITE-ProRule:PRU00958,
CC       ECO:0000256|SAAS:SAAS00541185}.
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DR   EMBL; CP000493; ABM80326.1; -; Genomic_DNA.
DR   RefSeq; WP_011821644.1; NC_008818.1.
DR   ProteinModelPortal; A2BK15; -.
DR   STRING; 415426.Hbut_0460; -.
DR   EnsemblBacteria; ABM80326; ABM80326; Hbut_0460.
DR   GeneID; 4782654; -.
DR   KEGG; hbu:Hbut_0460; -.
DR   eggNOG; arCOG01219; Archaea.
DR   eggNOG; COG1867; LUCA.
DR   HOGENOM; HOG000229931; -.
DR   KO; K00555; -.
DR   OMA; FYNPRMA; -.
DR   OrthoDB; POG093Z0BNY; -.
DR   BioCyc; HBUT415426:GC56-460-MONOMER; -.
DR   Proteomes; UP000002593; Chromosome.
DR   GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00290; tRNA_dimethyltr_TRM1; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR002905; Trm1.
DR   InterPro; IPR022923; TRM1_arc_bac.
DR   PANTHER; PTHR10631; PTHR10631; 1.
DR   Pfam; PF02005; TRM; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00308; TRM1; 1.
DR   PROSITE; PS51626; SAM_MT_TRM1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002593};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00290,
KW   ECO:0000256|PROSITE-ProRule:PRU00958, ECO:0000256|SAAS:SAAS00423719,
KW   ECO:0000313|EMBL:ABM80326.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002593};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00958,
KW   ECO:0000256|SAAS:SAAS00423720};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00290,
KW   ECO:0000256|PROSITE-ProRule:PRU00958, ECO:0000256|SAAS:SAAS00423718};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00290, ECO:0000256|PROSITE-
KW   ProRule:PRU00958, ECO:0000256|SAAS:SAAS00423719,
KW   ECO:0000313|EMBL:ABM80326.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00290, ECO:0000256|PROSITE-
KW   ProRule:PRU00958, ECO:0000256|SAAS:SAAS00423721};
KW   tRNA-binding {ECO:0000256|PROSITE-ProRule:PRU00958,
KW   ECO:0000256|SAAS:SAAS00423720}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         8    393       ihamap:tRNA_dimethyltr_TRM1 [T]
FT   MYHIT         8    391       iprf:SAM_MT_TRM1 [T]
FT   MYHIT        35    391       ipfam:TRM [T]
SQ   SEQUENCE   396 AA;  44965 MW;  4DF0E2A9CE1D4EF5 CRC64;
     MDVGFPVRVV REGGVEIVVP DMDVYRRPNG VYEPAWAPVF YNPRMAFNRD IAVVFARTYA
     RLRGLDKLVV VEPLAGSGVR AVRYAVEAGA IVFASDIDSD AVYLSRVNAE RNKVSERVRV
     EKADANEFMA RLPRMGVKPT IIDIDPFGSP APFLDTAIQA LRPRGVLAVT ATDTAPLSGT
     HPRALRRRYD VRPGRLAWEK EQAVRILAGY IIRRAAAHEY GVRILLAYYV DYYVRIYAEL
     WRGAGRADKS LEQLGYGAYC YSCGYTSLAS NPLERCPYCQ AQLGIVGPLY IGKLCDESFI
     EEMLREAEKM WDILAEPDRV VKLLEQLLKE CDIVKPYYRL DKLCSILRMN MPKMNTVVEE
     LRNRGYNATR THFDPRGFKT NAPHWAVVKM LLETRR
//