(data stored in ACNUC7421 zone)

SWISSPROT: TRMB_PSEHT

ID   TRMB_PSEHT              Reviewed;         241 AA.
AC   Q3ILJ1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 82.
DE   RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
DE            EC=2.1.1.33 {ECO:0000255|HAMAP-Rule:MF_01057};
DE   AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
DE   AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
GN   Name=trmB {ECO:0000255|HAMAP-Rule:MF_01057};
GN   OrderedLocusNames=PSHAa0553;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at
CC       position 46 (m7G46) in tRNA. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01057}.
CC   -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01057}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. TrmB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01057}.
DR   EMBL; CR954246; CAI85641.1; -; Genomic_DNA.
DR   RefSeq; WP_011327254.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILJ1; -.
DR   SMR; Q3ILJ1; -.
DR   STRING; 326442.PSHAa0553; -.
DR   EnsemblBacteria; CAI85641; CAI85641; PSHAa0553.
DR   KEGG; pha:PSHAa0553; -.
DR   PATRIC; fig|326442.8.peg.522; -.
DR   eggNOG; ENOG4105CZ1; Bacteria.
DR   eggNOG; COG0220; LUCA.
DR   HOGENOM; HOG000073968; -.
DR   KO; K03439; -.
DR   OMA; PDPWHKS; -.
DR   OrthoDB; POG091H015P; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
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   TIGRFAMs; TIGR00091; TIGR00091; 1.
DR   PROSITE; PS51625; SAM_MT_TRMB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3ILJ1.
DR   SWISS-2DPAGE; Q3ILJ1.
KW   Complete proteome; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN         1    241       tRNA (guanine-N(7)-)-methyltransferase.
FT                                /FTId=PRO_0000229184.
FT   REGION      219    222       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01057}.
FT   ACT_SITE    146    146       {ECO:0000250}.
FT   BINDING      71     71       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01057}.
FT   BINDING      96     96       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01057}.
FT   BINDING     123    123       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01057}.
FT   BINDING     146    146       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01057}.
FT   BINDING     150    150       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01057}.
FT   BINDING     182    182       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01057}.
SQ   SEQUENCE   241 AA;  27444 MW;  788348BC055628E5 CRC64;
     MSESSNTNLE QAKQEGKYIR TIRSFVKREG RLTKGQAAAI EKCWPIMGLE HKNGMLDLSE
     VFGNNNDVVL EIGFGMGKSL VEMAKNAPHL NFIGIEVHRP GVGACLMDAD EAGITNLRIF
     EHDAVEVLAD CIADESLTTL QLFFPDPWHK KRHHKRRIVQ GEFVEKLRSQ LKMGGVFHMA
     TDWENYAEHM LEVMQAAPGF KNQSTTNDYV PRPDLRPLTK FEQRGHRLGH GVWDLMFERT
     K
//

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