Reviewed, UniProtKB/Swiss-Prot P15624 (SYFB_YEAST)

Names and origin

Protein names

Recommended name:
    Phenylalanyl-tRNA synthetase beta chain
    EC=6.1.1.20
Alternative name(s):
    Phenylalanine--tRNA ligase beta chain
      Short name=PheRS

Gene names

Name:	FRS1
Ordered Locus Names:	YLR060W
ORF Names:	L2165

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	595 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 chains.
Subcellular location	Cytoplasm.
Miscellaneous	Present with 5440 molecules/cell in log phase SD medium. Ref.3
Sequence similarities	Belongs to the phenylalanyl-tRNA synthetase beta chain family. Type 2 subfamily.
Caution	Was originally (Ref.1) erroneously assigned as an alpha chain.

Ontologies

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

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FRS2	P15625	1	EBI-18684,EBI-18678

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 595	594	Phenylalanyl-tRNA synthetase beta chain		PRO_0000127023
Regions
	Region	86 – 90	5	CCA binding of tRNA Potential
Amino acid modifications
	Modified residue	124	1	Phosphoserine Ref.5
	Modified residue	375	1	Phosphoserine Ref.5
	Modified residue	437	1	Phosphothreonine Ref.4
Experimental info
	Sequence conflict	18	1	N → D AA sequence Ref.1
	Sequence conflict	426	1	G → D in AAA35151. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P15624-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 68DA23E49644F801	FASTA	595	67,365
	10 20 30 40 50 60 MPTVSVNKQQ LFDLLGKNYT SQEFDELCFE FGMEMDEDTT EEALKTGEEP ELKLDISANR 70 80 90 100 110 120 YDLLCIEGIS QSLNEYLERK ERPDYKLSKP TTKLIIDKST EQIRPFATAA VLRNIKLNEK 130 140 150 160 170 180 SYASFIALQD KLHANLCRNR SLVAMGTHDL DSIEGPFHYR ALPPKDIKFV PLNQTQEFTG 190 200 210 220 230 240 DKLIEFYKSP EQKNNIGRYV HIIEDSPVFP VIMDSKDRVC SLPPLINSEH SKISVNTRNI 250 260 270 280 290 300 LIDITATDKT KAEIVLNILT TMFSRYCDEP FTVEPVEIVS EHNGQSRLAP NFNDRIMDVS 310 320 330 340 350 360 IKYINSCLGL DQSADEIAHC LKKMSLHAVQ SKEDKDILHV DIPVTRPDIL HACDIMEDAA 370 380 390 400 410 420 VGYGFNNLPK GEKLSNANFI AKPLPINKVS DIFRVASSQA TWVEVLPLTL CSHDENFKFL 430 440 450 460 470 480 RQSDNGDLAV KLANPKTLEY QVVRTTLLPG ILKTVKENRK HSLPIKVFET GDVVFKDDKL 490 500 510 520 530 540 ERKAYNERHW AAIYVGKNSG FEIIQGLLGK IMQTFRTEWI ADYGAAASGR GYWIEEDDSV 550 560 570 580 590 KTYFPGRGAK VMFRSKEGAE PKQIGHLGVL HPEVMMNFDV PFAASFVEVN AEVFL

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: 3049607] [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: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[4]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-437, MASS SPECTROMETRY.
[5]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-375, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J03964 Genomic DNA. Translation: AAA35151.1. Different initiation. X94607 Genomic DNA. Translation: CAA64307.1. Z73232 Genomic DNA. Translation: CAA97591.1.
PIR	YFBYBC. S61634.
RefSeq	NP_013161.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6746N.
IntAct	P15624. 4 interactions.
STRING	P15624.
Proteomic databases
PeptideAtlas	P15624.
Genome annotation databases
Ensembl	YLR060W; YLR060W; YLR060W; Saccharomyces cerevisiae. [Genome view]
GeneID	850749.
KEGG	sce:YLR060W.
NMPDR	fig|4932.3.peg.4152.
Organism-specific databases
CYGD	YLR060w.
SGD	S000004050. FRS1.
Phylogenomic databases
HOGENOM	P15624.
OMA	LCSHDEN
OrthoDB	EOG9RFN8T
Enzyme and pathway databases
BRENDA	6.1.1.20. 250.
Gene expression databases
ArrayExpress	P15624.
Genevestigator	P15624.
GermOnline	YLR060W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR005146. B3/B4_tRNA-bd. IPR005147. B5. IPR009061. DNA_bd_put. IPR004531. Phe-tRNA-synth_IIc_bsu_arc. [Graphical view]
Gene3D	G3DSA:3.30.56.20. B5. 1 hit.
Pfam	PF03483. B3_4. 1 hit. PF03484. B5. 1 hit. [Graphical view]
SMART	SM00873. B3_4. 1 hit. SM00874. B5. 1 hit. [Graphical view]
TIGRFAMs	TIGR00471. pheT_arch. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	966879.

Entry information

Entry name

SYFB_YEAST

Accession

Primary (citable) accession number: P15624

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 95 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)