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Database: UniProt/SWISS-PROT
Entry: SYM_THETN
LinkDB: SYM_THETN
Original site: SYM_THETN 
ID   SYM_THETN               Reviewed;         638 AA.
AC   Q8RDD1;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   19-FEB-2014, entry version 87.
DE   RecName: Full=Methionine--tRNA ligase;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionyl-tRNA synthetase;
DE            Short=MetRS;
GN   Name=metG; OrderedLocusNames=TTE0110;
OS   Thermoanaerobacter tengcongensis (strain DSM 15242 / JCM 11007 / NBRC
OS   100824 / MB4) (Caldanaerobacter subterraneus subsp. tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J.,
RA   Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L.,
RA   Tan H., Chen R., Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
CC   -!- FUNCTION: Is required not only for elongation of protein synthesis
CC       but also for the initiation of all mRNA translation through
CC       initiator tRNA(fMet) aminoacylation (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-methionine + tRNA(Met) = AMP +
CC       diphosphate + L-methionyl-tRNA(Met).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. MetG type 2A subfamily.
CC   -!- SIMILARITY: Contains 1 tRNA-binding domain.
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DR   EMBL; AE008691; AAM23414.1; -; Genomic_DNA.
DR   RefSeq; NP_621810.1; NC_003869.1.
DR   ProteinModelPortal; Q8RDD1; -.
DR   STRING; 273068.TTE0110; -.
DR   EnsemblBacteria; AAM23414; AAM23414; TTE0110.
DR   GeneID; 996595; -.
DR   KEGG; tte:TTE0110; -.
DR   PATRIC; 23894857; VBITheTen82880_0104.
DR   eggNOG; COG0143; -.
DR   HOGENOM; HOG000200401; -.
DR   KO; K01874; -.
DR   OMA; ANEWGNL; -.
DR   OrthoDB; EOG6CVV9B; -.
DR   ProtClustDB; PRK12267; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004495; Met-tRNA-synth_Ia_bsu_C.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR023457; Met-tRNA_synth_2.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR009080; tRNAsynth_1a_anticodon-bd.
DR   InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
DR   TIGRFAMs; TIGR00399; metG_C_term; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   RNA-binding; tRNA-binding; Zinc.
FT   CHAIN         1    638       Methionine--tRNA ligase.
FT                                /FTId=PRO_0000139259.
FT   DOMAIN      538    638       tRNA-binding.
FT   MOTIF        12     22       "HIGH" region.
FT   MOTIF       296    300       "KMSKS" region.
FT   METAL       127    127       Zinc (By similarity).
FT   METAL       130    130       Zinc (By similarity).
FT   METAL       144    144       Zinc (By similarity).
FT   METAL       147    147       Zinc (By similarity).
FT   BINDING     299    299       ATP (By similarity).
SQ   SEQUENCE   638 AA;  73552 MW;  93360852EFF5EF1C CRC64;
     MKKTFYITTP IYYPSDKLHI GHSYTTVAAD AMARFKRLTG YDVMFLTGTD EHGQKIQRIA
     REKGMSPKEY VDGIVEWIKD LWKTMDISYD HFIRTTDAYH EEIVQKIFMK LYEQGDIYKG
     EYEGWYCTPC ESFWTESQLV DGKCPDCGRP VERVTEEGYF FRLSAYGDKL LKYYEEHPDF
     IQPESRRNEM INFIKAGLED LFVSRSTFDW GIKVPFDPKH VIYVWIDALS NYITALGYMT
     ENDEKFKKYW PADVHLVGKE IVRFHTIIWP AMLMALGLPL PKKVFGHGWL ILEGGKMSKS
     KGNVVDPKEL VDRYGVDAIR YFLLREVPFG ADGVFSNEAL INRINSDLAN DLGNLLSRTV
     TMIEKYFDGV LPKPSSQEEI DEDLINVAQN LPQKVEEYMD KLQFSNALIE IWKLVSRANK
     YIDETMPWVL AKDESKRGRL GTVLYNLAES LRFIGILISP FMPNTPKKMF EQLGITEDLT
     TWESLKFGLL KEGTRVKRGE ILFPRIDVEK ELASLEKKTE EKTKETKEEK IDYITIEDFS
     KVQLRVAEIL EAEKVEGSDK LIKMKLKVGE EIRQIVGGIG KYYSPEELIG KKIIIVYNLQ
     PRKLMGIESQ GMLLAATNEG KMALLTVDKD IESGSKIS
//
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