P15625 (SYFA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phenylalanine--tRNA ligase alpha subunit
EC=6.1.1.20

Alternative name(s):
Phenylalanyl-tRNA synthetase alpha subunit
Short name=PheRS

Gene names

Name:	FRS2
Ordered Locus Names:	YFL022C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).
Subunit structure	Tetramer of two alpha and two beta subunits.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
Caution	Was originally (Ref.1) erroneously assigned as a beta subunit.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	phenylalanyl-tRNA aminoacylation Traceable author statement Ref.1. Source: SGD
Cellular_component	phenylalanine-tRNA ligase complex Inferred from direct assay Ref.1. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phenylalanine-tRNA ligase activity Inferred from mutant phenotype Ref.1. Source: SGD tRNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FRS1	P15624	3	EBI-18678,EBI-18684

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 503	502	Phenylalanine--tRNA ligase alpha subunit		PRO_0000126828
Regions
	Region	2 – 173	172	Contains the major tRNA-Phe binding sites
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.5
	Modified residue	39	1	Phosphoserine Ref.6
	Modified residue	117	1	Phosphoserine Ref.6
Experimental info
	Sequence conflict	177	1	N → S in AAA35152. Ref.1
	Sequence conflict	289	1	D → E in AAA35152. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P15625 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 50B7EAC675AB559B	FASTA	503	57,511
	10 20 30 40 50 60 MSDFQLEILK KLDELDEIKS TLATFPQHGS QDVLSALNSL KAHNKLEFSK VDTVTYDLTK 70 80 90 100 110 120 EGAQILNEGS YEIKLVKLIQ ELGQLQIKDV MSKLGPQVGK VGQARAFKNG WIAKNASNEL 130 140 150 160 170 180 ELSAKLQNTD LNELTDETQS ILAQIKNNSH LDSIDAKILN DLKKRKLIAQ GKITDFNVTK 190 200 210 220 230 240 GPEFSTDLTK LETDLTSDMV STNAYKDLKF KPYNFNSQGV QISSGALHPL NKVREEFRQI 250 260 270 280 290 300 FFSMGFTEMP SNQYVETGFW NFDALYVPQQ HPARDLQDTF YIKDPLTADL PDDKTYMDNI 310 320 330 340 350 360 KAVHEQGRFG SIGYRYNWKP EECQKLVLRT HSTAISARML HDLAKDPKPT RLFSIDRVFR 370 380 390 400 410 420 NEAVDATHLA EFHQVEGVLA DYNITLGDLI KFMEEFFERM GVTGLRFKPT YNPYTEPSME 430 440 450 460 470 480 IFSWHEGLQK WVEIGNSGMF RPEMLESMGL PKDLRVLGWG LSLERPTMIK YKVQNIRELL 490 500 GHKVSLDFIE TNPAARLDED LYE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae." Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T. Nat. Genet. 10:261-268(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Identification of the major tRNA(Phe) binding domain in the tetrameric structure of cytoplasmic phenylalanyl-tRNA synthetase from baker's yeast." Fasiolo F., Sanni A., Potier S., Ebel J.-P., Boulanger Y. FEBS Lett. 242:351-356(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, DOMAIN TRNA-BINDING.
[5]	"Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins." Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E. Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT SER-2.
[6]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-117, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J03965 Genomic DNA. Translation: AAA35152.1. D50617 Genomic DNA. Translation: BAA09216.1. BK006940 Genomic DNA. Translation: DAA12418.1.
PIR	YFBYAC. S56232.
RefSeq	NP_116631.1. NM_001179944.2.
3D structure databases
ProteinModelPortal	P15625.
SMR	P15625. Positions 155-500.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5428N.
IntAct	P15625. 9 interactions.
MINT	MINT-479586.
STRING	4932.YFL022C.
Proteomic databases
PaxDb	P15625.
PeptideAtlas	P15625.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YFL022C; YFL022C; YFL022C.
GeneID	850522.
KEGG	sce:YFL022C.
Organism-specific databases
SGD	S000001872. FRS2.
Phylogenomic databases
eggNOG	COG0016.
GeneTree	ENSGT00390000006387.
HOGENOM	HOG000230294.
KO	K01889.
OMA	WKGYSVK.
OrthoDB	EOG4MGWGX.
Gene expression databases
Genevestigator	P15625.
GermOnline	YFL022C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR006195. aa-tRNA-synth_II. IPR004529. Phe-tRNA-synth_IIc_asu. IPR002319. Phenylalanyl-tRNA_Synthase. [Graphical view]
Pfam	PF01409. tRNA-synt_2d. 1 hit. [Graphical view]
TIGRFAMs	TIGR00468. pheS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	966257.

Entry information

Entry name

SYFA_YEAST

Accession

Primary (citable) accession number: P15625
Secondary accession number(s): D6VTK8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 133 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program