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Protein

Tyrosine--tRNA ligase, mitochondrial

Gene

MSY1

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

Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).By similarity

Catalytic activityi

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei306 – 3061ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • RNA binding Source: InterPro
  • tyrosine-tRNA ligase activity Source: SGD

GO - Biological processi

  • mitochondrial tyrosyl-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-34000-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine--tRNA ligase, mitochondrial (EC:6.1.1.1)
Alternative name(s):
Tyrosyl-tRNA synthetase
Short name:
TyrRS
Gene namesi
Name:MSY1
Ordered Locus Names:YPL097W
ORF Names:LPG11W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL097W.
SGDiS000006018. MSY1.

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
Chaini? – 492Tyrosine--tRNA ligase, mitochondrialPRO_0000035835
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

MaxQBiP48527.

Interactioni

Protein-protein interaction databases

BioGridi36083. 5 interactions.
DIPiDIP-3826N.
MINTiMINT-494509.

Structurei

3D structure databases

ProteinModelPortaliP48527.
SMRiP48527. Positions 55-490.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi94 – 10310"HIGH" region
Motifi303 – 3075"KMSKS" region

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00390000013709.
HOGENOMiHOG000242790.
InParanoidiP48527.
KOiK01866.
OMAiFKLYCGA.
OrthoDBiEOG72G1JR.

Family and domain databases

Gene3Di3.10.290.10. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002942. S4_RNA-bd.
IPR002307. Tyr-tRNA-ligase.
IPR024088. Tyr-tRNA-ligase_bac-type.
[Graphical view]
PANTHERiPTHR11766. PTHR11766. 1 hit.
PfamiPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSiPR01040. TRNASYNTHTYR.
TIGRFAMsiTIGR00234. tyrS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P48527-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLELRSCSNL VNSSRRLVPL VTYSGLSAIT LPKSRFYSQP SALEVQGTSD
60 70 80 90 100
SRSDNILDEL KQRGLVSQVS QPESFLRTKL NGNDKIKLYC GVDPTAQSLH
110 120 130 140 150
LGNLVPLMVL LHFYVKGHDI VTVIGGATGK VGDPSGRKTE RDVMENDIRQ
160 170 180 190 200
SNVASISQQL QRFFKNGLEY YRNRCALTED VPSGKYTPRN NFNWWKDIKM
210 220 230 240 250
LDFLADFGRH IRVQSMLARD SISSRLQTKN GLGFNEFTYQ VLQAYDFYHL
260 270 280 290 300
YKEENVTIQV GGNDQWGNIT AGIDLINRIQ PIKNKGLPFG ITVPLLTTAT
310 320 330 340 350
GEKFGKSAGN AVFIDPSINT AYDVYQFFYN TLDADVPKFL KIFTFLNSSE
360 370 380 390 400
IKKIVETHIK SPSLRYGQTL LAKEVTDMLY GVGSGSDSEA LSNIIFGRYD
410 420 430 440 450
GTLSAAKLVD LCKKARILQY ADREIDLIKL ICKLVNCSVS EARRKLSQGS
460 470 480 490
VYLHHSKSKV NENISNLAPF LIDDRVLILR IGKQKCFIIE MR
Length:492
Mass (Da):55,287
Last modified:February 1, 1996 - v1
Checksum:i2159116E1CB5ED2E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42333 Genomic DNA. Translation: AAA67122.1.
U43281 Genomic DNA. Translation: AAB68202.1.
BK006949 Genomic DNA. Translation: DAA11335.1.
PIRiS59733.
RefSeqiNP_015228.1. NM_001183911.1.

Genome annotation databases

EnsemblFungiiYPL097W; YPL097W; YPL097W.
GeneIDi856007.
KEGGisce:YPL097W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42333 Genomic DNA. Translation: AAA67122.1.
U43281 Genomic DNA. Translation: AAB68202.1.
BK006949 Genomic DNA. Translation: DAA11335.1.
PIRiS59733.
RefSeqiNP_015228.1. NM_001183911.1.

3D structure databases

ProteinModelPortaliP48527.
SMRiP48527. Positions 55-490.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36083. 5 interactions.
DIPiDIP-3826N.
MINTiMINT-494509.

Proteomic databases

MaxQBiP48527.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL097W; YPL097W; YPL097W.
GeneIDi856007.
KEGGisce:YPL097W.

Organism-specific databases

EuPathDBiFungiDB:YPL097W.
SGDiS000006018. MSY1.

Phylogenomic databases

GeneTreeiENSGT00390000013709.
HOGENOMiHOG000242790.
InParanoidiP48527.
KOiK01866.
OMAiFKLYCGA.
OrthoDBiEOG72G1JR.

Enzyme and pathway databases

BioCyciYEAST:G3O-34000-MONOMER.

Miscellaneous databases

NextBioi980887.
PROiP48527.

Family and domain databases

Gene3Di3.10.290.10. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002942. S4_RNA-bd.
IPR002307. Tyr-tRNA-ligase.
IPR024088. Tyr-tRNA-ligase_bac-type.
[Graphical view]
PANTHERiPTHR11766. PTHR11766. 1 hit.
PfamiPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSiPR01040. TRNASYNTHTYR.
TIGRFAMsiTIGR00234. tyrS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nuclear gene MSY1 of Saccharomyces cerevisiae codes for mitochondrial tyrosyl-tRNA synthetase."
    Hill J.E., Tzagoloff A.A.
    Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 24657 / D273-10B.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(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: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  7. "Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics."
    Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.
    J. Proteome Res. 5:1543-1554(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYYM_YEAST
AccessioniPrimary (citable) accession number: P48527
Secondary accession number(s): D6W3R9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 996 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.