(data stored in ACNUC7421 zone)

SWISSPROT: C3MF16_SINFN

ID   C3MF16_SINFN            Unreviewed;       232 AA.
AC   C3MF16;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 55.
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   ECO:0000313|EMBL:ACP23853.1};
GN   OrderedLocusNames=NGR_c00490 {ECO:0000313|EMBL:ACP23853.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23853.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23853.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP23853.1; -; Genomic_DNA.
DR   RefSeq; WP_012706638.1; NC_012587.1.
DR   RefSeq; YP_002824606.1; NC_012587.1.
DR   STRING; 394.NGR_c00490; -.
DR   EnsemblBacteria; ACP23853; ACP23853; NGR_c00490.
DR   GeneID; 7790628; -.
DR   KEGG; rhi:NGR_c00490; -.
DR   PATRIC; fig|394.7.peg.2841; -.
DR   eggNOG; ENOG4105CZ1; Bacteria.
DR   eggNOG; COG0220; LUCA.
DR   HOGENOM; HOG000073969; -.
DR   KO; K03439; -.
DR   OMA; PDPWHKS; -.
DR   OrthoDB; POG091H015P; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000001054; 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; C3MF16.
DR   SWISS-2DPAGE; C3MF16.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01057,
KW   ECO:0000256|SAAS:SAAS00097779, ECO:0000313|EMBL:ACP23853.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
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:ACP23853.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01057}.
FT   REGION      211    214       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01057}.
FT   BINDING      63     63       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01057}.
FT   BINDING      88     88       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01057}.
FT   BINDING     115    115       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01057}.
FT   BINDING     137    137       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01057}.
FT   BINDING     141    141       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01057}.
FT   BINDING     173    173       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01057}.
SQ   SEQUENCE   232 AA;  26651 MW;  18994DAF2DEBDD18 CRC64;
     MTEPRRARAT EAFFGRRKGK QLRERQAAQL ENLLPVLRLD LKEPAPTDLS ALFPTAVNRV
     RLEIGFGGGE HLIHRAAEDP STGFIGVEPF INSMAKLLGQ IEAREIDNVR LYDDDATQVL
     DWLPPASVDQ VDLLYPDPWP KRKHWKRRFV SKVNLDRFAR VLKPGGLFCF ASDIDSYVNW
     TLIHCRDHAA FEWTAERSAD WLTPFSGWPS TRYEAKARRE GRSSAYLTFR RA
//

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