ID SYM_CORU7 Reviewed; 611 AA.
AC B1VFI1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 01-MAY-2013, entry version 42.
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=cu0560;
OS Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=504474;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43042 / DSM 7109;
RX PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S.,
RA Kalinowski J., Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B.,
RA Soriano F., Droege M., Puehler A.;
RT "The lifestyle of Corynebacterium urealyticum derived from its
RT complete genome sequence established by pyrosequencing.";
RL J. Biotechnol. 136:11-21(2008).
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: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC family. MetG type 1 subfamily.
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DR EMBL; AM942444; CAQ04520.1; -; Genomic_DNA.
DR RefSeq; YP_001799954.1; NC_010545.1.
DR ProteinModelPortal; B1VFI1; -.
DR STRING; 504474.cur_0560; -.
DR EnsemblBacteria; CAQ04520; CAQ04520; cu0560.
DR GeneID; 6186658; -.
DR KEGG; cur:cur_0560; -.
DR PATRIC; 21520838; VBICorUre58120_0561.
DR eggNOG; COG0143; -.
DR KO; K01874; -.
DR OMA; SYYFMGK; -.
DR ProtClustDB; PRK12268; -.
DR BioCyc; CURE504474:GJ8Y-571-MONOMER; -.
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:0006431; P:methionyl-tRNA aminoacylation; IEA:HAMAP.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1; -.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; tRNAsyn_1a_bind; 1.
DR TIGRFAMs; TIGR00398; metG; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; FALSE_NEG.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
FT CHAIN 1 611 Methionine--tRNA ligase.
FT /FTId=PRO_1000093708.
FT MOTIF 12 22 "HIGH" region.
FT MOTIF 348 352 "KMSKS" region.
FT METAL 144 144 Zinc (By similarity).
FT METAL 147 147 Zinc (By similarity).
FT METAL 157 157 Zinc (By similarity).
FT METAL 160 160 Zinc (By similarity).
FT BINDING 351 351 ATP (By similarity).
SQ SEQUENCE 611 AA; 68264 MW; 53C9A143C68A284B CRC64;
MSKRVLTSVA WPYANGPRHI GHVAGFGVPS DVFARYQRMI GNDVLMVSGT DEHGTPLLVQ
ADKENTTVRE LADRYNRIIV EDLVGLGLSY DLFTRTTTRN HYAIVQELFR GLNENGYMLK
QTTRGAVSPS TGRTLPDRYI EGTCPLCGAT DARGDQCDNC GNQLDPADLI DPRSKINGET
PEFVDTEHFM LDLPALAEAL EEWLKGRNDW RPNVLKFSLN LLKDIRPRAM SRDIDWGVPV
PIEGWQDNNA KKLYVWFDAV VGYLSASIEW AWRTGDPEAW RKWWNDPEAV SYYFMGKDNI
TFHSQIWPGE MLGYAGKGSK GGEQGELGEL NLPTEVVSSE FLTMSGSKFS SSKGVVIYVR
DFLKEFGPDA LRYFIAVAGP ENTDTDFTWD EFVRRINSEL ANEWGNLVNR TASMAHKNFG
EIPQPGEFTA EDQALLDEAK QAYTVVGDAL QLSKFKAGMT EAMRIAARAN QYIAAQEPWK
LAKDETQRER LATVLYVALQ VVSDVNTLMT PYLPFSAQKV FETLGGEGIW AAQPEIVEVK
DESPYTPVGV GLPEEGSSYP VIMGNYTEQK AIWQRTELAP GTALSKPKPL FQKLDPELAE
TGPEWAPVVK D
//
