SYM_THEKO
ID SYM_THEKO Reviewed; 741 AA.
AC Q5JDZ7;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Methionine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00098};
DE EC=6.1.1.10 {ECO:0000255|HAMAP-Rule:MF_00098};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00098};
DE Short=MetRS {ECO:0000255|HAMAP-Rule:MF_00098};
GN Name=metG {ECO:0000255|HAMAP-Rule:MF_00098}; OrderedLocusNames=TK1049;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: Is required not only for elongation of protein synthesis but
CC also for the initiation of all mRNA translation through initiator
CC tRNA(fMet) aminoacylation. {ECO:0000255|HAMAP-Rule:MF_00098}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00098};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00098};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00098}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00098}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00098}.
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DR EMBL; AP006878; BAD85238.1; -; Genomic_DNA.
DR RefSeq; WP_011250000.1; NC_006624.1.
DR AlphaFoldDB; Q5JDZ7; -.
DR SMR; Q5JDZ7; -.
DR IntAct; Q5JDZ7; 1.
DR MINT; Q5JDZ7; -.
DR STRING; 69014.TK1049; -.
DR EnsemblBacteria; BAD85238; BAD85238; TK1049.
DR GeneID; 3234491; -.
DR KEGG; tko:TK1049; -.
DR PATRIC; fig|69014.16.peg.1026; -.
DR eggNOG; arCOG00810; Archaea.
DR HOGENOM; CLU_009710_1_2_2; -.
DR InParanoid; Q5JDZ7; -.
DR OMA; SDMHGTP; -.
DR OrthoDB; 6590at2157; -.
DR PhylomeDB; Q5JDZ7; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR CDD; cd02800; tRNA_bind_EcMetRS_like; 1.
DR Gene3D; 2.20.28.20; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR004495; Met-tRNA-synth_bsu_C.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
DR InterPro; IPR029038; MetRS_Zn.
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_Ia_anticodon-bd.
DR PANTHER; PTHR45765; PTHR45765; 1.
DR Pfam; PF19303; Anticodon_3; 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 SUPFAM; SSF57770; SSF57770; 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; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..741
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139198"
FT DOMAIN 641..741
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT MOTIF 11..21
FT /note="'HIGH' region"
FT MOTIF 345..349
FT /note="'KMSKS' region"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT BINDING 348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
SQ SEQUENCE 741 AA; 86371 MW; 6992952E4D80ABE0 CRC64;
MVRYMVTSAL PYANGPIHAG HLAGAYLPAD IFVRYLRLKG EEVLFICGTD EHGTPITFRA
LKEGRSPREI VDEFHEHIKT TFERAKISFD FFGRTELPVH YRLSQEFFLK ALENGHLVKK
VTKQAYCEHD KMFLPDRYVI GTCPYCGAEN QRGDQCEVCG HPLTPEILIN PRCNICGNPI
TFKDSAHYYI RMQDFEERLK KWVESQEHWK PNVRNTVLGW INEGLEERAI TRDLDWGIPV
PLDDEDVKGK VLYVWFEAPI GYISITIEHL KREGKENEWK KFWLNLDGET KVIHFIGKDN
IPFHAIFWPA FLMAYGKYRD EEVEAEWNLP YDIPANEYLN LEGKKFSTSR NWAIWVHEFL
DVWPADYLRY YLTAIMPETR DSDFSFEDFK KKINEELVNN LGNFVHRAMT FVNRYFDGVV
PERGELNDLD RQALEEIEKA FKETGELISN YRFKDALKRV MELAIFGNRY FDYQKPWKTA
KENRERTATT VNVSLQIVKA LGILLEPFLP DASEKIWHLL NLEEVKKWSF EELPAGHRVR
KAFPMFRKVT DGEIIYFIVN YIGRGNPDSA KILLNKYYKQ EDVVKVTLER FGEKRKDEAL
ALLKSIYGDE FKGEKPEKAG KAEKKEKVKE GKKMEYVSFD EFAKLDLRVG KIIEVNDHPN
ADRLYVVKVD LGDEVRQLVA GLKKYYKPEE LLGHYVVIIA NLEPKKLRGV ESQGMLLAAD
DGERVALLMP DKEVKLGARI R
