Aspartyl-tRNA synthetase, cytoplasmic - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P04802 (SYDC_YEAST)

Last modified February 9, 2010. Version 122. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Aspartyl-tRNA synthetase, cytoplasmic
    EC=6.1.1.12
Alternative name(s):
    Aspartate--tRNA ligase
      Short name=AspRS

Gene names

Name:	DPS1
Synonyms:	APS, APS1
Ordered Locus Names:	YLL018C
ORF Names:	L1295

Organism

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

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	557 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Miscellaneous	Present with 5750 molecules/cell in log phase SD medium. Ref.10
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

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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	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	aspartyl-tRNA aminoacylation Inferred from direct assay. Source: SGD
Cellular component	cytoplasm Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from direct assay. Source: SGD aspartate-tRNA ligase activity Inferred from direct assay. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
itself		1	EBI-18655,EBI-18655
PRP40	P33203	1	EBI-18655,EBI-701
SET2	P46995	1	EBI-18655,EBI-16985

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.5

Chain

2 – 557

556

Aspartyl-tRNA synthetase, cytoplasmic

PRO_0000111014

Amino acid modifications

Modified residue

N-acetylserine Ref.9

Modified residue

Phosphoserine Ref.14 Ref.15

Modified residue

243

Phosphothreonine Ref.15

Modified residue

301

Phosphoserine Ref.15 Ref.11 Ref.12

Modified residue

502

Phosphoserine Ref.15

Modified residue

546

Phosphoserine Ref.15 Ref.13

Experimental info

Mutagenesis

273

P → G: Loss of activity; important for dimerization. Ref.8

Secondary structure

557

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P04802-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 6656279B3E9011A5
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FASTA

557

63,516

        10         20         30         40         50         60 
MSQDENIVKA VEESAEPAQV ILGEDGKPLS KKALKKLQKE QEKQRKKEER ALQLEAEREA 

        70         80         90        100        110        120 
REKKAAAEDT AKDNYGKLPL IQSRDSDRTG QKRVKFVDLD EAKDSDKEVL FRARVHNTRQ 

       130        140        150        160        170        180 
QGATLAFLTL RQQASLIQGL VKANKEGTIS KNMVKWAGSL NLESIVLVRG IVKKVDEPIK 

       190        200        210        220        230        240 
SATVQNLEIH ITKIYTISET PEALPILLED ASRSEAEAEA AGLPVVNLDT RLDYRVIDLR 

       250        260        270        280        290        300 
TVTNQAIFRI QAGVCELFRE YLATKKFTEV HTPKLLGAPS EGGSSVFEVT YFKGKAYLAQ 

       310        320        330        340        350        360 
SPQFNKQQLI VADFERVYEI GPVFRAENSN THRHMTEFTG LDMEMAFEEH YHEVLDTLSE 

       370        380        390        400        410        420 
LFVFIFSELP KRFAHEIELV RKQYPVEEFK LPKDGKMVRL TYKEGIEMLR AAGKEIGDFE 

       430        440        450        460        470        480 
DLSTENEKFL GKLVRDKYDT DFYILDKFPL EIRPFYTMPD PANPKYSNSY DFFMRGEEIL 

       490        500        510        520        530        540 
SGAQRIHDHA LLQERMKAHG LSPEDPGLKD YCDGFSYGCP PHAGGGIGLE RVVMFYLDLK 

       550 
NIRRASLFPR DPKRLRP

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence polymorphisms in the yeast gene encoding aspartyl tRNA synthase." Reid G.A. Nucleic Acids Res. 16:1212-1212(1988) [PubMed: 3278298] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Nucleotide sequence of the gene coding for yeast cytoplasmic aspartyl-tRNA synthetase (APS); mapping of the 5' and 3' termini of AspRS mRNA." Sellami M., Fasiolo F., Dirheimer G., Ebel J.-P., Gangloff J. Nucleic Acids Res. 14:1657-1666(1986) [PubMed: 3513127] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The sequence of 32kb on the left arm of yeast chromosome XII reveals six known genes, a new member of the seripauperins family and a new ABC transporter homologous to the human multidrug resistance protein." Purnelle B., Goffeau A. Yeast 13:183-188(1997) [PubMed: 9046100] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"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. Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	"The complete amino acid sequence of cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae." Amiri I., Mejdoub H., Hounwanou N., Boulanger Y., Reinbolt J. Biochimie 67:607-613(1985) [PubMed: 3902099] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-557.
[6]	"Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on a 43.7 kb fragment of chromosome XII including an open reading frame homologous to the human cystic fibrosis transmembrane conductance regulator protein CFTR." Miosga T., Zimmermann F.K. Yeast 12:693-708(1996) [PubMed: 8810043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81. Strain: ATCC 90840 / EAY235 / FY23.
[7]	"Identification of structurally and functionally important histidine residues in cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae." Gasparini S., Vincendon P., Eriani G., Gangloff J., Boulanger Y., Reinbolt J., Kern D. Biochemistry 30:4284-4289(1991) [PubMed: 2021621] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, MUTAGENESIS.
[8]	"Role of dimerization in yeast aspartyl-tRNA synthetase and importance of the class II invariant proline." Eriani G., Cavarelli J., Martin F., Dirheimer G., Moras D., Gangloff J. Proc. Natl. Acad. Sci. U.S.A. 90:10816-10820(1993) [PubMed: 8248175] [Abstract] Cited for: MUTAGENESIS OF PRO-273.
[9]	"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: 9298649] [Abstract] Cited for: ACETYLATION AT SER-2.
[10]	"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].
[11]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, MASS SPECTROMETRY.
[12]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, MASS SPECTROMETRY.
[13]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, MASS SPECTROMETRY.
[14]	"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 SER-14, MASS SPECTROMETRY.
[15]	"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-14; THR-243; SER-301; SER-502 AND SER-546, MASS SPECTROMETRY.
[16]	"Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp)." Ruff M., Krishnaswamy S., Boeglin M., Poterszman A., Mitschler A., Podjarny A., Rees B., Thierry J.-C., Moras D. Science 252:1682-1689(1991) [PubMed: 2047877] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[17]	"The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction." Cavarelli J., Eriani G., Rees B., Ruff M., Boeglin M., Mitschler A., Martin F., Gangloff J., Thierry J.-C., Moras D. EMBO J. 13:327-337(1994) [PubMed: 8313877] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), MUTAGENESIS.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X03606 Genomic DNA. Translation: CAA27269.1.
X06665 Genomic DNA. Translation: CAA29865.1.
X97560 Genomic DNA. Translation: CAA66172.1.
Z73123 Genomic DNA. Translation: CAA97464.1.
Z73122 Genomic DNA. Translation: CAA97463.1.
X91488 Genomic DNA. Translation: CAA62772.1.

PIR

SYBYDC. A23508.

RefSeq

NP_013083.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ASY	X-ray	2.90	A/B	68-557	[»]
1ASZ	X-ray	3.00	A/B	68-557	[»]
1EOV	X-ray	2.30	A	71-556	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4093N.

IntAct

P04802. 24 interactions.

STRING

P04802.

Proteomic databases

PRIDE

P04802.

Genome annotation databases

Ensembl

YLL018C; YLL018C; YLL018C; Saccharomyces cerevisiae. [Genome view]

GeneID

850643.

KEGG

sce:YLL018C.

NMPDR

fig|4932.3.peg.4075.

Organism-specific databases

CYGD

YLL018c.

SGD

S000003941. DPS1.

Phylogenomic databases

eggNOG

HOGENOM

OMA

OrthoDB

PhylomeDB

P04802.

Enzyme and pathway databases

BRENDA

6.1.1.12. 250.

Gene expression databases

ArrayExpress

P04802.

Genevestigator

P04802.

GermOnline

YLL018C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II_cons-dom.
IPR002312. Asp-tRNA-synth_IIb.
IPR004523. Asp-tRNA-synth_IIb_arc/euk.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004365. NA_bd_OB_tRNA-helicase.
[Graphical view]

Gene3D

G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.

PANTHER

PTHR22594. aa-tRNA-synt_II. 1 hit.

Pfam

PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]

PRINTS

PR01042. TRNASYNTHASP.

TIGRFAMs

TIGR00458. aspS_arch. 1 hit.

PROSITE

PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

966579.

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Entry information

Entry name

SYDC_YEAST

Accession

Primary (citable) accession number: P04802

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 122 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents