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Database: UniProt/SWISS-PROT
Entry: TRMB_NOSS1
LinkDB: TRMB_NOSS1
Original site: TRMB_NOSS1 
ID   TRMB_NOSS1              Reviewed;         219 AA.
AC   Q8YVX4;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-SEP-2014, entry version 71.
DE   RecName: Full=tRNA (guanine-N(7)-)-methyltransferase;
DE            EC=2.1.1.33;
DE   AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase;
DE   AltName: Full=tRNA(m7G46)-methyltransferase;
GN   Name=trmB; OrderedLocusNames=alr1845;
OS   Nostoc sp. (strain PCC 7120 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T.,
RA   Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M.,
RA   Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
CC   -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at
CC       position 46 (m7G46) in tRNA (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(46) in tRNA
CC       = S-adenosyl-L-homocysteine + N(7)-methylguanine(46) in tRNA.
CC   -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. TrmB family.
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DR   EMBL; BA000019; BAB73544.1; -; Genomic_DNA.
DR   PIR; AG2036; AG2036.
DR   RefSeq; NP_485885.1; NC_003272.1.
DR   RefSeq; WP_010996013.1; NC_003272.1.
DR   ProteinModelPortal; Q8YVX4; -.
DR   STRING; 103690.alr1845; -.
DR   DNASU; 1105437; -.
DR   EnsemblBacteria; BAB73544; BAB73544; BAB73544.
DR   GeneID; 1105437; -.
DR   KEGG; ana:alr1845; -.
DR   PATRIC; 22773769; VBINosSp37423_2361.
DR   eggNOG; COG0220; -.
DR   HOGENOM; HOG000237936; -.
DR   KO; K03439; -.
DR   OMA; RVTIQFP; -.
DR   OrthoDB; EOG6K6VBC; -.
DR   UniPathway; UPA00989; -.
DR   GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01057; tRNA_methyltr_TrmB; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases-like.
DR   InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase.
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;
KW   Complete proteome; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN         1    219       tRNA (guanine-N(7)-)-methyltransferase.
FT                                /FTId=PRO_0000171285.
FT   ACT_SITE    125    125       By similarity.
FT   BINDING      47     47       S-adenosyl-L-methionine (By similarity).
FT   BINDING      72     72       S-adenosyl-L-methionine (By similarity).
FT   BINDING      99     99       S-adenosyl-L-methionine (By similarity).
FT   BINDING     125    125       S-adenosyl-L-methionine (By similarity).
FT   BINDING     129    129       Substrate (By similarity).
FT   BINDING     161    161       Substrate (By similarity).
SQ   SEQUENCE   219 AA;  24847 MW;  6B255C82EA25C83C CRC64;
     MISGVSALPF VRVRQHVNPL AQKYLTPANP LEWEKAYSTP HQPLHLDIGC ARGRFVLQMA
     QVEPNWNFLG LEIRESLVIE ANQFRSQLGL TNLHYLYCNA NNSLQPLLSS LPTGILQRVT
     IQFPDPWFKT RHAKRRVVQP ELVQDIANYL AVGGVVFLQS DMEFVAVEMC DRFAANPAFK
     KVGTGEWLTE NPLPVATERE TTTQNRGEPV YRALFERSS
//
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