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Protein

Phenylalanine--tRNA ligase beta subunit

Gene

FRS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. phenylalanine-tRNA ligase activity Source: UniProtKB-EC
  4. RNA binding Source: InterPro

GO - Biological processi

  1. phenylalanyl-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-32214-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylalanine--tRNA ligase beta subunit (EC:6.1.1.20)
Alternative name(s):
Phenylalanyl-tRNA synthetase beta subunit
Short name:
PheRS
Gene namesi
Name:FRS1
Ordered Locus Names:YLR060W
ORF Names:L2165
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR060W.
SGDiS000004050. FRS1.

Subcellular locationi

GO - Cellular componenti

  1. phenylalanine-tRNA ligase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 595594Phenylalanine--tRNA ligase beta subunitPRO_0000127023Add
BLAST

Proteomic databases

MaxQBiP15624.
PaxDbiP15624.
PeptideAtlasiP15624.

Expressioni

Gene expression databases

GenevestigatoriP15624.

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits.

Binary interactionsi

WithEntry#Exp.IntActNotes
FRS2P156253EBI-18684,EBI-18678

Protein-protein interaction databases

BioGridi31335. 27 interactions.
DIPiDIP-6746N.
IntActiP15624. 5 interactions.
MINTiMINT-616734.
STRINGi4932.YLR060W.

Structurei

3D structure databases

ProteinModelPortaliP15624.
SMRiP15624. Positions 1-595.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini292 – 37079B5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni86 – 905CCA binding of tRNASequence Analysis

Sequence similaritiesi

Contains 1 B5 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0072.
GeneTreeiENSGT00530000063489.
HOGENOMiHOG000105095.
InParanoidiP15624.
KOiK01890.
OMAiIKVFETG.
OrthoDBiEOG77M8XG.

Family and domain databases

Gene3Di3.30.56.20. 1 hit.
InterProiIPR005146. B3/B4_tRNA-bd.
IPR009061. DNA-bd_dom_put.
IPR004531. Phe-tRNA-synth_IIc_bsu_arc.
IPR005147. tRNA_synthase_B5-dom.
[Graphical view]
PfamiPF03483. B3_4. 1 hit.
PF03484. B5. 1 hit.
[Graphical view]
SMARTiSM00873. B3_4. 1 hit.
SM00874. B5. 1 hit.
[Graphical view]
SUPFAMiSSF46955. SSF46955. 2 hits.
TIGRFAMsiTIGR00471. pheT_arch. 1 hit.
PROSITEiPS51483. B5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P15624-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTVSVNKQQ LFDLLGKNYT SQEFDELCFE FGMEMDEDTT EEALKTGEEP
60 70 80 90 100
ELKLDISANR YDLLCIEGIS QSLNEYLERK ERPDYKLSKP TTKLIIDKST
110 120 130 140 150
EQIRPFATAA VLRNIKLNEK SYASFIALQD KLHANLCRNR SLVAMGTHDL
160 170 180 190 200
DSIEGPFHYR ALPPKDIKFV PLNQTQEFTG DKLIEFYKSP EQKNNIGRYV
210 220 230 240 250
HIIEDSPVFP VIMDSKDRVC SLPPLINSEH SKISVNTRNI LIDITATDKT
260 270 280 290 300
KAEIVLNILT TMFSRYCDEP FTVEPVEIVS EHNGQSRLAP NFNDRIMDVS
310 320 330 340 350
IKYINSCLGL DQSADEIAHC LKKMSLHAVQ SKEDKDILHV DIPVTRPDIL
360 370 380 390 400
HACDIMEDAA VGYGFNNLPK GEKLSNANFI AKPLPINKVS DIFRVASSQA
410 420 430 440 450
TWVEVLPLTL CSHDENFKFL RQSDNGDLAV KLANPKTLEY QVVRTTLLPG
460 470 480 490 500
ILKTVKENRK HSLPIKVFET GDVVFKDDKL ERKAYNERHW AAIYVGKNSG
510 520 530 540 550
FEIIQGLLGK IMQTFRTEWI ADYGAAASGR GYWIEEDDSV KTYFPGRGAK
560 570 580 590
VMFRSKEGAE PKQIGHLGVL HPEVMMNFDV PFAASFVEVN AEVFL
Length:595
Mass (Da):67,365
Last modified:January 23, 2007 - v3
Checksum:i68DA23E49644F801
GO

Sequence cautioni

The sequence AAA35151.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181N → D AA sequence (PubMed:3049607).Curated
Sequence conflicti426 – 4261G → D in AAA35151 (PubMed:3049607).Curated
Sequence conflicti544 – 5441F → L in AAT92797 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03964 Genomic DNA. Translation: AAA35151.1. Different initiation.
X94607 Genomic DNA. Translation: CAA64307.1.
Z73232 Genomic DNA. Translation: CAA97591.1.
AY692778 Genomic DNA. Translation: AAT92797.1.
BK006945 Genomic DNA. Translation: DAA09378.1.
PIRiS61634. YFBYBC.
RefSeqiNP_013161.1. NM_001181947.1.

Genome annotation databases

EnsemblFungiiYLR060W; YLR060W; YLR060W.
GeneIDi850749.
KEGGisce:YLR060W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03964 Genomic DNA. Translation: AAA35151.1. Different initiation.
X94607 Genomic DNA. Translation: CAA64307.1.
Z73232 Genomic DNA. Translation: CAA97591.1.
AY692778 Genomic DNA. Translation: AAT92797.1.
BK006945 Genomic DNA. Translation: DAA09378.1.
PIRiS61634. YFBYBC.
RefSeqiNP_013161.1. NM_001181947.1.

3D structure databases

ProteinModelPortaliP15624.
SMRiP15624. Positions 1-595.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31335. 27 interactions.
DIPiDIP-6746N.
IntActiP15624. 5 interactions.
MINTiMINT-616734.
STRINGi4932.YLR060W.

Proteomic databases

MaxQBiP15624.
PaxDbiP15624.
PeptideAtlasiP15624.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR060W; YLR060W; YLR060W.
GeneIDi850749.
KEGGisce:YLR060W.

Organism-specific databases

EuPathDBiFungiDB:YLR060W.
SGDiS000004050. FRS1.

Phylogenomic databases

eggNOGiCOG0072.
GeneTreeiENSGT00530000063489.
HOGENOMiHOG000105095.
InParanoidiP15624.
KOiK01890.
OMAiIKVFETG.
OrthoDBiEOG77M8XG.

Enzyme and pathway databases

BioCyciYEAST:G3O-32214-MONOMER.

Miscellaneous databases

NextBioi966879.
PROiP15624.

Gene expression databases

GenevestigatoriP15624.

Family and domain databases

Gene3Di3.30.56.20. 1 hit.
InterProiIPR005146. B3/B4_tRNA-bd.
IPR009061. DNA-bd_dom_put.
IPR004531. Phe-tRNA-synth_IIc_bsu_arc.
IPR005147. tRNA_synthase_B5-dom.
[Graphical view]
PfamiPF03483. B3_4. 1 hit.
PF03484. B5. 1 hit.
[Graphical view]
SMARTiSM00873. B3_4. 1 hit.
SM00874. B5. 1 hit.
[Graphical view]
SUPFAMiSSF46955. SSF46955. 2 hits.
TIGRFAMsiTIGR00471. pheT_arch. 1 hit.
PROSITEiPS51483. B5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and expression of the genes encoding the alpha and beta subunits of yeast phenylalanyl-tRNA synthetase."
    Sanni A., Mirande M., Ebel J.-P., Boulanger Y., Waller J.-P., Fasiolo F.
    J. Biol. Chem. 263:15407-15415(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(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: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Phenylalanyl-tRNA synthetase from baker's yeast. Repeated sequences in the two subunits."
    Robbe-Saul S., Fasiolo F., Boulanger Y.
    FEBS Lett. 84:57-62(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, CLEAVAGE OF INITIATOR METHIONINE.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYFB_YEAST
AccessioniPrimary (citable) accession number: P15624
Secondary accession number(s): D6VY62, E9P8X0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 137 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 5440 molecules/cell in log phase SD medium.1 Publication

Caution

Was originally erroneously assigned as an alpha subunit.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

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 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.