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Protein

Phenylalanine--tRNA ligase, mitochondrial

Gene

MSF1

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

Functioni

Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation.

Catalytic activityi

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei155 – 1551SubstrateBy similarity
Binding sitei302 – 3021Substrate; via carbonyl oxygenBy similarity
Binding sitei329 – 3291Substrate; via carbonyl oxygenBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • magnesium ion binding Source: InterPro
  • phenylalanine-tRNA ligase activity Source: UniProtKB
  • tRNA binding Source: InterPro

GO - Biological processi

  • mitochondrial phenylalanyl-tRNA aminoacylation Source: SGD
  • phenylalanyl-tRNA aminoacylation Source: UniProtKB
  • tRNA processing Source: InterPro
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-34202-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylalanine--tRNA ligase, mitochondrial (EC:6.1.1.20)
Alternative name(s):
Phenylalanyl-tRNA synthetase
Short name:
PheRS
Gene namesi
Name:MSF1
Ordered Locus Names:YPR047W
ORF Names:YP9499.05
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR047W.
SGDiS000006251. MSF1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1717MitochondrionAdd
BLAST
Chaini18 – 469452Phenylalanine--tRNA ligase, mitochondrialPRO_0000035817Add
BLAST

Proteomic databases

MaxQBiP08425.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi36223. 50 interactions.
DIPiDIP-3901N.
IntActiP08425. 1 interaction.
MINTiMINT-500190.

Structurei

3D structure databases

ProteinModelPortaliP08425.
SMRiP08425. Positions 25-469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini372 – 46998FDX-ACBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni126 – 1294Substrate bindingBy similarity
Regioni162 – 1643Substrate bindingBy similarity
Regioni169 – 1713Substrate bindingBy similarity

Sequence similaritiesi

Contains 1 FDX-ACB domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00530000063467.
HOGENOMiHOG000165163.
InParanoidiP08425.
KOiK01889.
OMAiRIVYRHM.
OrthoDBiEOG7KSXJQ.

Family and domain databases

Gene3Di3.30.70.380. 1 hit.
InterProiIPR006195. aa-tRNA-synth_II.
IPR004530. Phe-tRNA-synth_IIc_mito.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR005121. PheS_beta_Fdx_antiC-bd.
[Graphical view]
PfamiPF03147. FDX-ACB. 1 hit.
PF01409. tRNA-synt_2d. 2 hits.
[Graphical view]
SMARTiSM00896. FDX-ACB. 1 hit.
[Graphical view]
SUPFAMiSSF54991. SSF54991. 1 hit.
TIGRFAMsiTIGR00469. pheS_mito. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
PS51447. FDX_ACB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08425-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLNRMMKTR TGLYRLYSTL KVPHVEINGI KYKTDPQTTN VTDSIIKLTD
60 70 80 90 100
RSLHLKESHP VGILRDLIEK KLNSVDNTFK IFNNFKPVVT TMENFDSLGF
110 120 130 140 150
PKDHPGRSKS DTYYINETHL LRTHTSAHEL ECFQKIRNDS DNIKSGFLIS
160 170 180 190 200
ADVYRRDEID KTHYPVFHQM EGATIWKRTK ADVGVKEPMY IEKIREDIRQ
210 220 230 240 250
VENLLNKENV KITVDDDTIP LKENNPKQEY MSDLEVDLCS QHLKRSIELI
260 270 280 290 300
VSEVFNKKIS SMIKNKANNT PKELKVRWIN AYFPWTAPSW EIEVWWQGEW
310 320 330 340 350
LELCGCGLIR QDVLLRAGYK PSETIGWAFG LGLDRIAMLL FEIPDIRLLW
360 370 380 390 400
SRDERFSRQF SKGLITSFKP YSKHPGSFRD VAFWLPEDKP DIHQVHENDL
410 420 430 440 450
MEIIRNIAGD LVESVKLVDS FTHPKTGRKS MCYRINYQSM DRNLTNAEVN
460
TLQDMVCSKL VKEYSVELR
Length:469
Mass (Da):54,829
Last modified:September 5, 2006 - v3
Checksum:iE728783D76C74C18
GO

Sequence cautioni

The sequence AAA34800.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA89167.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA94994.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861K → E in AAA34800 (PubMed:3029120).Curated
Sequence conflicti233 – 2331D → H in AAA34800 (PubMed:3029120).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02691 Genomic DNA. Translation: AAA34800.1. Different initiation.
Z71255 Genomic DNA. Translation: CAA94994.1. Different initiation.
Z49219 Genomic DNA. Translation: CAA89167.1. Different initiation.
BK006949 Genomic DNA. Translation: DAA11471.1.
PIRiS54071. YFBYAM.
RefSeqiNP_015372.2. NM_001184144.1.

Genome annotation databases

EnsemblFungiiYPR047W; YPR047W; YPR047W.
GeneIDi856160.
KEGGisce:YPR047W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02691 Genomic DNA. Translation: AAA34800.1. Different initiation.
Z71255 Genomic DNA. Translation: CAA94994.1. Different initiation.
Z49219 Genomic DNA. Translation: CAA89167.1. Different initiation.
BK006949 Genomic DNA. Translation: DAA11471.1.
PIRiS54071. YFBYAM.
RefSeqiNP_015372.2. NM_001184144.1.

3D structure databases

ProteinModelPortaliP08425.
SMRiP08425. Positions 25-469.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36223. 50 interactions.
DIPiDIP-3901N.
IntActiP08425. 1 interaction.
MINTiMINT-500190.

Proteomic databases

MaxQBiP08425.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR047W; YPR047W; YPR047W.
GeneIDi856160.
KEGGisce:YPR047W.

Organism-specific databases

EuPathDBiFungiDB:YPR047W.
SGDiS000006251. MSF1.

Phylogenomic databases

GeneTreeiENSGT00530000063467.
HOGENOMiHOG000165163.
InParanoidiP08425.
KOiK01889.
OMAiRIVYRHM.
OrthoDBiEOG7KSXJQ.

Enzyme and pathway databases

BioCyciYEAST:G3O-34202-MONOMER.

Miscellaneous databases

PROiP08425.

Family and domain databases

Gene3Di3.30.70.380. 1 hit.
InterProiIPR006195. aa-tRNA-synth_II.
IPR004530. Phe-tRNA-synth_IIc_mito.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR005121. PheS_beta_Fdx_antiC-bd.
[Graphical view]
PfamiPF03147. FDX-ACB. 1 hit.
PF01409. tRNA-synt_2d. 2 hits.
[Graphical view]
SMARTiSM00896. FDX-ACB. 1 hit.
[Graphical view]
SUPFAMiSSF54991. SSF54991. 1 hit.
TIGRFAMsiTIGR00469. pheS_mito. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
PS51447. FDX_ACB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the yeast gene coding for the alpha subunit of mitochondrial phenylalanyl-tRNA synthetase."
    Koerner T.J., Myers A.M., Lee S., Tzagoloff A.
    J. Biol. Chem. 262:3690-3696(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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. "Evolution of aminoacyl-tRNA synthetase quaternary structure and activity: Saccharomyces cerevisiae mitochondrial phenylalanyl-tRNA synthetase."
    Sanni A., Walter P., Boulanger Y., Ebel J.-P., Fasiolo F.
    Proc. Natl. Acad. Sci. U.S.A. 88:8387-8391(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, SUBUNIT.
  5. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
    Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
    Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.

Entry informationi

Entry nameiSYFM_YEAST
AccessioniPrimary (citable) accession number: P08425
Secondary accession number(s): D6W455, Q12410
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: September 5, 2006
Last modified: July 6, 2016
This is version 156 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1800 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.