(data stored in ACNUC7421 zone)

SWISSPROT: SYM_THEFY

ID   SYM_THEFY               Reviewed;         606 AA.
AC   Q47SZ0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 113.
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};
GN   OrderedLocusNames=Tfu_0389;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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. {ECO:0000255|HAMAP-
CC       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-
CC       Rule:MF_00098};
CC   -!- SUBUNIT: Monomer. {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
CC       family. MetG type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00098}.
DR   EMBL; CP000088; AAZ54427.1; -; Genomic_DNA.
DR   RefSeq; WP_011290836.1; NC_007333.1.
DR   SMR; Q47SZ0; -.
DR   STRING; 269800.Tfu_0389; -.
DR   PRIDE; Q47SZ0; -.
DR   EnsemblBacteria; AAZ54427; AAZ54427; Tfu_0389.
DR   KEGG; tfu:Tfu_0389; -.
DR   eggNOG; ENOG4105CKH; Bacteria.
DR   eggNOG; COG0143; LUCA.
DR   HOGENOM; HOG000200402; -.
DR   KO; K01874; -.
DR   OMA; MRMAGHD; -.
DR   OrthoDB; 761140at2; -.
DR   BioCyc; TFUS269800:G1G4Q-393-MONOMER; -.
DR   Proteomes; UP000000434; 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; IEA:UniProtKB-UniRule.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 2.20.28.20; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR   InterPro; IPR041872; Anticodon_Met.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF57770; SSF57770; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47SZ0.
DR   SWISS-2DPAGE; Q47SZ0.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome; Zinc.
FT   CHAIN         1    606       Methionine--tRNA ligase.
FT                                /FTId=PRO_0000331920.
FT   MOTIF        14     24       "HIGH" region.
FT   MOTIF       351    355       "KMSKS" region.
FT   METAL       146    146       Zinc. {ECO:0000255|HAMAP-Rule:MF_00098}.
FT   METAL       149    149       Zinc. {ECO:0000255|HAMAP-Rule:MF_00098}.
FT   METAL       159    159       Zinc. {ECO:0000255|HAMAP-Rule:MF_00098}.
FT   METAL       162    162       Zinc. {ECO:0000255|HAMAP-Rule:MF_00098}.
FT   BINDING     354    354       ATP. {ECO:0000255|HAMAP-Rule:MF_00098}.
SQ   SEQUENCE   606 AA;  67359 MW;  96EAA452AAE10D8C CRC64;
     MSSKRHILTA VAWPYANGPR HIGHVSGFGV PSDVFARFQR MSGNNVLMVS GTDEHGTPIQ
     VLADQEGVSA RELADRYNRI IAEDLVALGL SYDLFTRTTT ANHYAVVQEL FTGLYRNGYI
     FSKTTKGAIS PSTGRTLPDR YVEGTCPICG YDGARGDQCD NCGKQLDPTD LINPRSKING
     ETPEFVDTEH FMLDLPAFAE QLSEWLKSKG GEWRPNVLKF SLNLLDELQP RAITRDLDWG
     VPIPLEGWRD QPNKRLYVWF DAVIGYLSAS IEWAKRTGDP EAWRKWWQNS DAESFYFMGK
     DNIVFHSEIW PAMLLGYSGK GSKGGEPGSL GALNLPTEVV SSEFLTMEGR KFSSSRRVVI
     YVRDFLERYD ADALRYYIIA AGPETQDTDF TWAEFVRRNN DELVATWGNL VNRSISMAAK
     NIGHIPEAGE LTDADRAVLD ASKAAFATVG ERLNRAQFKA ALQEAMRVVA EANKYFSEQA
     PWKLKKTDPK RMETVLHVAL QLVSDAKTLL TPFLPASSNK VYEMLGGTGT WTGMPRLEEA
     TDSIGGEEGV STYPVITGDY ADNEARWESI PIVPGTPLKP PTPLFRKLDQ SVVDEELARL
     EAAAGA
//

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