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Protein

Methionine--tRNA ligase, mitochondrial

Gene

MSM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei344 – 3441ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • methionine-tRNA ligase activity Source: SGD

GO - Biological processi

  • methionyl-tRNA aminoacylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30867-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine--tRNA ligase, mitochondrial (EC:6.1.1.10)
Alternative name(s):
Methionyl-tRNA synthetase
Short name:
MetRS
Gene namesi
Name:MSM1
Ordered Locus Names:YGR171C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR171C.
SGDiS000003403. MSM1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 575575Methionine--tRNA ligase, mitochondrialPRO_0000139272Add
BLAST

Proteomic databases

MaxQBiP22438.
PeptideAtlasiP22438.

Interactioni

Protein-protein interaction databases

BioGridi33423. 47 interactions.
IntActiP22438. 2 interactions.
MINTiMINT-2783147.

Structurei

3D structure databases

ProteinModelPortaliP22438.
SMRiP22438. Positions 13-533.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi20 – 3213"HIGH" regionAdd
BLAST
Motifi341 – 3455"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000075136.
HOGENOMiHOG000200401.
InParanoidiP22438.
KOiK01874.
OMAiTYPAFCT.
OrthoDBiEOG7647BG.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR014758. Met-tRNA_synth.
IPR015413. Methionyl/Leucyl_tRNA_Synth.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PfamiPF09334. tRNA-synt_1g. 1 hit.
[Graphical view]
PRINTSiPR01041. TRNASYNTHMET.
SUPFAMiSSF47323. SSF47323. 2 hits.
TIGRFAMsiTIGR00398. metG. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22438-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQCRSIVHRL YSKVSHVTTP IFYPNAKPHL GHLYSSLLSD VYHRWQLFKG
60 70 80 90 100
NLSFFTTGTD EHGLKIQCAS ESNGFDQPKK FVDKLYPEFV QLDKIYGINY
110 120 130 140 150
TRFIRTTDPD HIENVMKLWE LCLKNGYIYM GEHKGWYSIS DETFYPESKV
160 170 180 190 200
IKDPKNDGKY LNTESKNEVV YQSETNYFFR LSLFNKKIVD HIRKNPDFIF
210 220 230 240 250
PASKRDQILK ELETGGTLPD LSISRPSARL KWGIPTPNDP SQKVYVWFDA
260 270 280 290 300
LCNYLSSIGG IPSILSNATE VVSRHYSDKS NVKGQLLIPY PKEVQRNTIH
310 320 330 340 350
VIGKDIAKFH TVYWPSFLLA AGLPLPRQIV VHGHWLCNGM KMSKSLGNVV
360 370 380 390 400
DPIDMARYYG ADIVRWFLLE NSKLEEDGDF QEAKLYETRE LLVSKWGNLI
410 420 430 440 450
NRCCGSKFNI ERAVMKFSDK ANFQFQEIFQ NEPIVSERIE NLAKLLNKSQ
460 470 480 490 500
EVFDEKIAIF QYPQLLRHVW SIINDANTLV QNSKPWEREL DQQDNIIFLA
510 520 530 540 550
METSRILSIL CQSIIPSLSQ SFLDRIDVSK EKRTINYARL GSDKTYGKQS
560 570
NKKGREVPLK KIPFRLQEEQ TNMRS
Length:575
Mass (Da):66,734
Last modified:October 1, 1996 - v2
Checksum:iE105AD353D5C82B3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141V → I in CAA32778 (PubMed:2645139).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14629 Genomic DNA. Translation: CAA32778.1.
Z72956 Genomic DNA. Translation: CAA97197.1.
BK006941 Genomic DNA. Translation: DAA08266.1.
PIRiS64485. SYBYMM.
RefSeqiNP_011687.1. NM_001181300.1.

Genome annotation databases

EnsemblFungiiYGR171C; YGR171C; YGR171C.
GeneIDi853081.
KEGGisce:YGR171C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14629 Genomic DNA. Translation: CAA32778.1.
Z72956 Genomic DNA. Translation: CAA97197.1.
BK006941 Genomic DNA. Translation: DAA08266.1.
PIRiS64485. SYBYMM.
RefSeqiNP_011687.1. NM_001181300.1.

3D structure databases

ProteinModelPortaliP22438.
SMRiP22438. Positions 13-533.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33423. 47 interactions.
IntActiP22438. 2 interactions.
MINTiMINT-2783147.

Proteomic databases

MaxQBiP22438.
PeptideAtlasiP22438.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR171C; YGR171C; YGR171C.
GeneIDi853081.
KEGGisce:YGR171C.

Organism-specific databases

EuPathDBiFungiDB:YGR171C.
SGDiS000003403. MSM1.

Phylogenomic databases

GeneTreeiENSGT00550000075136.
HOGENOMiHOG000200401.
InParanoidiP22438.
KOiK01874.
OMAiTYPAFCT.
OrthoDBiEOG7647BG.

Enzyme and pathway databases

BioCyciYEAST:G3O-30867-MONOMER.

Miscellaneous databases

NextBioi973050.
PROiP22438.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR014758. Met-tRNA_synth.
IPR015413. Methionyl/Leucyl_tRNA_Synth.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PfamiPF09334. tRNA-synt_1g. 1 hit.
[Graphical view]
PRINTSiPR01041. TRNASYNTHMET.
SUPFAMiSSF47323. SSF47323. 2 hits.
TIGRFAMsiTIGR00398. metG. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of MSM1, the structural gene for yeast mitochondrial methionyl-tRNA synthetase."
    Tzagoloff A., Vambutas A., Akai A.
    Eur. J. Biochem. 179:365-371(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: D273-10B/A1.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYMM_YEAST
AccessioniPrimary (citable) accession number: P22438
Secondary accession number(s): D6VUV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3120 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.