SYM_THEMA
ID SYM_THEMA Reviewed; 629 AA.
AC O33925;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Methionine--tRNA ligase;
DE EC=6.1.1.10;
DE AltName: Full=Methionyl-tRNA synthetase;
DE Short=MetRS;
GN Name=metG; Synonyms=metS; OrderedLocusNames=TM_1085;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=9380682; DOI=10.1073/pnas.94.20.10606;
RA Guipaud O., Marguet E., Noll K.M., Bouthier de la Tour C., Forterre P.;
RT "Both DNA gyrase and reverse gyrase are present in the hyperthermophilic
RT bacterium Thermotoga maritima.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:10606-10611(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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:0000250}.
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;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 2A subfamily. {ECO:0000305}.
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DR EMBL; U76417; AAB87143.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD36162.1; -; Genomic_DNA.
DR PIR; E72297; E72297.
DR RefSeq; NP_228891.1; NC_000853.1.
DR RefSeq; WP_004080396.1; NZ_CP011107.1.
DR AlphaFoldDB; O33925; -.
DR SMR; O33925; -.
DR STRING; 243274.THEMA_08930; -.
DR DNASU; 897213; -.
DR EnsemblBacteria; AAD36162; AAD36162; TM_1085.
DR KEGG; tma:TM1085; -.
DR eggNOG; COG0073; Bacteria.
DR eggNOG; COG0143; Bacteria.
DR InParanoid; O33925; -.
DR OMA; SDMHGTP; -.
DR OrthoDB; 761140at2; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR004495; Met-tRNA-synth_bsu_C.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR023457; Met-tRNA_synth_2.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
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; PTHR43326; PTHR43326; 1.
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; 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..629
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139257"
FT DOMAIN 529..629
FT /note="tRNA-binding"
FT MOTIF 10..20
FT /note="'HIGH' region"
FT MOTIF 297..301
FT /note="'KMSKS' region"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 629 AA; 73004 MW; B0E0759F7C78ACEC CRC64;
MKFYITTPIY YVNSEPHIGS AYTTIVADII ARYKRFMGYD VFFLTGTDEH GQKVLQAAQQ
AGKDPQEFCD ELAEKFKRLW KELKITNDYF IRTTDEMHMK TVQEFVAKMK ENGDVYKGIY
KGWYCVPCET FWNEDEVIKE GEERFCPECK RPVKWVEEEN YFFRLSKYRD SLLKYYEEHP
DFVEPDFRRN EMLKILEGGL KDLSITRTTF KWGVPMKDDP EHVIYVWVDA LINYISAIGY
GWNDEMFNKW WPADLHLIGK EINRFHSIIW PAMLMSVGLP LPKKVFAHGW LTVNGQKISK
SLGNAIDPRF FVKRYGNDVV RYYLIRDIMF GKDGDFSEER LVHRLNSDLA NDYGNLLHRI
TAMIKKYFNG RLPSPSAQEG FDSWLKERFF ETKDAYHELM DSYRLTEALD KIWEFIADVN
KYFNDTKPWI LGKEGNMERL GTVLYNSLEA VFKVALMTLP VMPDTSEEVF RRVSFEEKPS
KEHLENWGVL KPGSTVIHGE PLFKKIDAKD FKKVVETVSA EQNAITIDDF SKVDLRIAKV
LEAEKVPNSR KLLRLIIDLG TEKRQIVAGI AEHYRPEELV GKLIVVVANL KPAKLMGIES
QGMLLAAKSG DTLRLLTVDG EITPGAKVS
