(data stored in SCRATCH zone)

SWISSPROT: C6AYA2_RHILS

ID   C6AYA2_RHILS            Unreviewed;       233 AA.
AC   C6AYA2;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 60.
DE   RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01057};
DE            EC=2.1.1.33 {ECO:0000256|HAMAP-Rule:MF_01057};
DE   AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01057};
DE   AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01057};
GN   Name=trmB {ECO:0000256|HAMAP-Rule:MF_01057};
GN   OrderedLocusNames=Rleg_0014 {ECO:0000313|EMBL:ACS54326.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54326.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54326.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54326.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
CC   -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at
CC       position 46 (m7G46) in tRNA. {ECO:0000256|HAMAP-Rule:MF_01057}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(46) in tRNA
CC       = S-adenosyl-L-homocysteine + N(7)-methylguanine(46) in tRNA.
CC       {ECO:0000256|HAMAP-Rule:MF_01057}.
CC   -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01057}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. TrmB family. {ECO:0000256|HAMAP-
CC       Rule:MF_01057}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01057}.
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DR   EMBL; CP001622; ACS54326.1; -; Genomic_DNA.
DR   RefSeq; WP_012755765.1; NC_012850.1.
DR   ProteinModelPortal; C6AYA2; -.
DR   EnsemblBacteria; ACS54326; ACS54326; Rleg_0014.
DR   KEGG; rlg:Rleg_0014; -.
DR   HOGENOM; HOG000073969; -.
DR   KO; K03439; -.
DR   OMA; PDPWHKS; -.
DR   OrthoDB; POG091H015P; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01057; tRNA_methyltr_TrmB; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR   PANTHER; PTHR23417; PTHR23417; 1.
DR   Pfam; PF02390; Methyltransf_4; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51625; SAM_MT_TRMB; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6AYA2.
DR   SWISS-2DPAGE; C6AYA2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01057,
KW   ECO:0000256|SAAS:SAAS00097779, ECO:0000313|EMBL:ACS54326.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01057,
KW   ECO:0000256|SAAS:SAAS00097748};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01057,
KW   ECO:0000256|SAAS:SAAS00466110, ECO:0000313|EMBL:ACS54326.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01057}.
FT   REGION      212    215       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01057}.
FT   BINDING      64     64       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01057}.
FT   BINDING      89     89       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01057}.
FT   BINDING     116    116       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01057}.
FT   BINDING     138    138       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01057}.
FT   BINDING     142    142       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01057}.
FT   BINDING     174    174       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01057}.
SQ   SEQUENCE   233 AA;  26656 MW;  768DBF739F1931D8 CRC64;
     MTDMERRGRA TEAFFGRRKG KALREQQAET LNSLLPAFLI DLTAAPPEPL TSLFPVPVER
     LRLEIGFGGG EHLIHRALNT PSTGFIGVEP FVNSMQKLLS RIGETGASNI RVYNDDATQL
     LDWLPDGSLD QVDLLYPDPW PKRKHWKRRF VSKTNLDRFH RVLKPGGLFC FASDIDTYVN
     WTLIKCRDHG GFDWMADNAA DWLTPYEGWP STRYEAKARR EGRSSAYLTF RKI
//

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