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 01-MAY-2013, entry version 84.
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; RINYDLA; -.
DR ProtClustDB; PRK12267; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0000049; F:tRNA binding; IEA:HAMAP.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:HAMAP.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_01228; Met_tRNA_synth_type2; 1; fused.
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; SSF50249; Nucleic_acid_OB; 1.
DR SUPFAM; SSF47323; tRNAsyn_1a_bind; 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
//
