SYMM_YEAST
ID SYMM_YEAST Reviewed; 575 AA.
AC P22438; D6VUV5;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Methionine--tRNA ligase, mitochondrial;
DE EC=6.1.1.10 {ECO:0000305|PubMed:2645139};
DE AltName: Full=Methionyl-tRNA synthetase;
DE Short=MetRS;
GN Name=MSM1; OrderedLocusNames=YGR171C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=D273-10B/A1;
RX PubMed=2645139; DOI=10.1111/j.1432-1033.1989.tb14562.x;
RA Tzagoloff A., Vambutas A., Akai A.;
RT "Characterization of MSM1, the structural gene for yeast mitochondrial
RT methionyl-tRNA synthetase.";
RL Eur. J. Biochem. 179:365-371(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Catalyzes the attachment of methionine to tRNA(Met) in the
CC mitochondrion. {ECO:0000269|PubMed:2645139}.
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 Evidence={ECO:0000305|PubMed:2645139};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13482;
CC Evidence={ECO:0000305|PubMed:2645139};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:2645139}.
CC -!- MISCELLANEOUS: Present with 3120 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; X14629; CAA32778.1; -; Genomic_DNA.
DR EMBL; Z72956; CAA97197.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08266.1; -; Genomic_DNA.
DR PIR; S64485; SYBYMM.
DR RefSeq; NP_011687.1; NM_001181300.1.
DR AlphaFoldDB; P22438; -.
DR SMR; P22438; -.
DR BioGRID; 33423; 58.
DR IntAct; P22438; 2.
DR MINT; P22438; -.
DR STRING; 4932.YGR171C; -.
DR MaxQB; P22438; -.
DR PaxDb; P22438; -.
DR PRIDE; P22438; -.
DR EnsemblFungi; YGR171C_mRNA; YGR171C; YGR171C.
DR GeneID; 853081; -.
DR KEGG; sce:YGR171C; -.
DR SGD; S000003403; MSM1.
DR VEuPathDB; FungiDB:YGR171C; -.
DR eggNOG; KOG0436; Eukaryota.
DR GeneTree; ENSGT00550000075136; -.
DR HOGENOM; CLU_009710_9_0_1; -.
DR InParanoid; P22438; -.
DR OMA; MDTQAFC; -.
DR BioCyc; YEAST:G3O-30867-MON; -.
DR PRO; PR:P22438; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P22438; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IMP:SGD.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IMP:SGD.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR43326; PTHR43326; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; SSF47323; 1.
DR TIGRFAMs; TIGR00398; metG; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..575
FT /note="Methionine--tRNA ligase, mitochondrial"
FT /id="PRO_0000139272"
FT MOTIF 20..32
FT /note="'HIGH' region"
FT MOTIF 341..345
FT /note="'KMSKS' region"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 14
FT /note="V -> I (in Ref. 1; CAA32778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 66734 MW; E105AD353D5C82B3 CRC64;
MQCRSIVHRL YSKVSHVTTP IFYPNAKPHL GHLYSSLLSD VYHRWQLFKG NLSFFTTGTD
EHGLKIQCAS ESNGFDQPKK FVDKLYPEFV QLDKIYGINY TRFIRTTDPD HIENVMKLWE
LCLKNGYIYM GEHKGWYSIS DETFYPESKV IKDPKNDGKY LNTESKNEVV YQSETNYFFR
LSLFNKKIVD HIRKNPDFIF PASKRDQILK ELETGGTLPD LSISRPSARL KWGIPTPNDP
SQKVYVWFDA LCNYLSSIGG IPSILSNATE VVSRHYSDKS NVKGQLLIPY PKEVQRNTIH
VIGKDIAKFH TVYWPSFLLA AGLPLPRQIV VHGHWLCNGM KMSKSLGNVV DPIDMARYYG
ADIVRWFLLE NSKLEEDGDF QEAKLYETRE LLVSKWGNLI NRCCGSKFNI ERAVMKFSDK
ANFQFQEIFQ NEPIVSERIE NLAKLLNKSQ EVFDEKIAIF QYPQLLRHVW SIINDANTLV
QNSKPWEREL DQQDNIIFLA METSRILSIL CQSIIPSLSQ SFLDRIDVSK EKRTINYARL
GSDKTYGKQS NKKGREVPLK KIPFRLQEEQ TNMRS
