Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P04802

- SYDC_YEAST

UniProt

P04802 - SYDC_YEAST

Protein

Aspartate--tRNA ligase, cytoplasmic

Gene

DPS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei281 – 2811AspartateBy similarity
    Binding sitei325 – 3251AspartateBy similarity
    Binding sitei478 – 4781ATPBy similarity
    Binding sitei481 – 4811AspartateBy similarity
    Binding sitei485 – 4851AspartateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi325 – 3273ATPBy similarity
    Nucleotide bindingi333 – 3353ATPBy similarity
    Nucleotide bindingi528 – 5314ATPBy similarity

    GO - Molecular functioni

    1. aspartate-tRNA ligase activity Source: SGD
    2. ATP binding Source: UniProtKB-KW
    3. RNA binding Source: SGD

    GO - Biological processi

    1. aspartyl-tRNA aminoacylation Source: SGD

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32123-MONOMER.
    SABIO-RKP04802.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartate--tRNA ligase, cytoplasmic (EC:6.1.1.12)
    Alternative name(s):
    Aspartyl-tRNA synthetase
    Short name:
    AspRS
    Gene namesi
    Name:DPS1
    Synonyms:APS, APS1
    Ordered Locus Names:YLL018C
    ORF Names:L1295
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    SGDiS000003941. DPS1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. nucleus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi273 – 2731P → G: Loss of activity; important for dimerization. 3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 557556Aspartate--tRNA ligase, cytoplasmicPRO_0000111014Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei14 – 141Phosphoserine1 Publication
    Modified residuei301 – 3011Phosphoserine3 Publications
    Modified residuei502 – 5021Phosphoserine2 Publications
    Modified residuei546 – 5461Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP04802.
    PaxDbiP04802.
    PRIDEiP04802.

    Expressioni

    Gene expression databases

    GenevestigatoriP04802.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi31235. 55 interactions.
    DIPiDIP-4093N.
    IntActiP04802. 15 interactions.
    MINTiMINT-510718.
    STRINGi4932.YLL018C.

    Structurei

    Secondary structure

    1
    557
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi73 – 775
    Helixi85 – 873
    Helixi96 – 983
    Turni101 – 1066
    Beta strandi108 – 12013
    Beta strandi122 – 13211
    Beta strandi135 – 1428
    Beta strandi145 – 1495
    Helixi151 – 1577
    Beta strandi165 – 17410
    Beta strandi182 – 19817
    Helixi208 – 2114
    Helixi215 – 2206
    Helixi228 – 2336
    Helixi235 – 2384
    Helixi242 – 26423
    Beta strandi274 – 2785
    Beta strandi280 – 2845
    Beta strandi288 – 2914
    Beta strandi294 – 2985
    Helixi303 – 3119
    Beta strandi316 – 3249
    Beta strandi331 – 3333
    Beta strandi336 – 34611
    Helixi352 – 37221
    Helixi374 – 38310
    Beta strandi393 – 3953
    Beta strandi398 – 4014
    Helixi402 – 41110
    Beta strandi418 – 4203
    Helixi424 – 43714
    Beta strandi441 – 4466
    Helixi450 – 4523
    Beta strandi461 – 4633
    Beta strandi466 – 4749
    Beta strandi477 – 4859
    Helixi489 – 49810
    Turni506 – 5083
    Helixi509 – 5157
    Beta strandi522 – 5287
    Helixi529 – 5368
    Helixi542 – 5454
    Beta strandi546 – 5483

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ASYX-ray2.90A/B68-557[»]
    1ASZX-ray3.00A/B68-557[»]
    1EOVX-ray2.30A71-557[»]
    ProteinModelPortaliP04802.
    SMRiP04802. Positions 68-557.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04802.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni303 – 3064AspartateBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0017.
    GeneTreeiENSGT00550000074880.
    HOGENOMiHOG000226032.
    KOiK01876.
    OMAiFCVGPVF.
    OrthoDBiEOG7PK972.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    InterProiIPR004364. aa-tRNA-synt_II.
    IPR018150. aa-tRNA-synt_II-like.
    IPR006195. aa-tRNA-synth_II.
    IPR004523. Asp-tRNA_synthase.
    IPR002312. Asp/Asn-tRNA-synth_IIb.
    IPR012340. NA-bd_OB-fold.
    IPR004365. NA-bd_OB_tRNA.
    [Graphical view]
    PANTHERiPTHR22594. PTHR22594. 1 hit.
    PTHR22594:SF10. PTHR22594:SF10. 1 hit.
    PfamiPF00152. tRNA-synt_2. 1 hit.
    PF01336. tRNA_anti-codon. 1 hit.
    [Graphical view]
    PRINTSiPR01042. TRNASYNTHASP.
    SUPFAMiSSF50249. SSF50249. 1 hit.
    TIGRFAMsiTIGR00458. aspS_nondisc. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P04802-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQDENIVKA VEESAEPAQV ILGEDGKPLS KKALKKLQKE QEKQRKKEER    50
    ALQLEAEREA REKKAAAEDT AKDNYGKLPL IQSRDSDRTG QKRVKFVDLD 100
    EAKDSDKEVL FRARVHNTRQ QGATLAFLTL RQQASLIQGL VKANKEGTIS 150
    KNMVKWAGSL NLESIVLVRG IVKKVDEPIK SATVQNLEIH ITKIYTISET 200
    PEALPILLED ASRSEAEAEA AGLPVVNLDT RLDYRVIDLR TVTNQAIFRI 250
    QAGVCELFRE YLATKKFTEV HTPKLLGAPS EGGSSVFEVT YFKGKAYLAQ 300
    SPQFNKQQLI VADFERVYEI GPVFRAENSN THRHMTEFTG LDMEMAFEEH 350
    YHEVLDTLSE LFVFIFSELP KRFAHEIELV RKQYPVEEFK LPKDGKMVRL 400
    TYKEGIEMLR AAGKEIGDFE DLSTENEKFL GKLVRDKYDT DFYILDKFPL 450
    EIRPFYTMPD PANPKYSNSY DFFMRGEEIL SGAQRIHDHA LLQERMKAHG 500
    LSPEDPGLKD YCDGFSYGCP PHAGGGIGLE RVVMFYLDLK NIRRASLFPR 550
    DPKRLRP 557
    Length:557
    Mass (Da):63,516
    Last modified:January 23, 2007 - v3
    Checksum:i6656279B3E9011A5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    BK006945 Genomic DNA. Translation: DAA09302.1.
    PIRiA23508. SYBYDC.
    RefSeqiNP_013083.1. NM_001181838.1.

    Genome annotation databases

    EnsemblFungiiYLL018C; YLL018C; YLL018C.
    GeneIDi850643.
    KEGGisce:YLL018C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    BK006945 Genomic DNA. Translation: DAA09302.1 .
    PIRi A23508. SYBYDC.
    RefSeqi NP_013083.1. NM_001181838.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 71-557 [» ]
    ProteinModelPortali P04802.
    SMRi P04802. Positions 68-557.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31235. 55 interactions.
    DIPi DIP-4093N.
    IntActi P04802. 15 interactions.
    MINTi MINT-510718.
    STRINGi 4932.YLL018C.

    Proteomic databases

    MaxQBi P04802.
    PaxDbi P04802.
    PRIDEi P04802.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLL018C ; YLL018C ; YLL018C .
    GeneIDi 850643.
    KEGGi sce:YLL018C.

    Organism-specific databases

    SGDi S000003941. DPS1.

    Phylogenomic databases

    eggNOGi COG0017.
    GeneTreei ENSGT00550000074880.
    HOGENOMi HOG000226032.
    KOi K01876.
    OMAi FCVGPVF.
    OrthoDBi EOG7PK972.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32123-MONOMER.
    SABIO-RK P04802.

    Miscellaneous databases

    EvolutionaryTracei P04802.
    NextBioi 966579.
    PROi P04802.

    Gene expression databases

    Genevestigatori P04802.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    InterProi IPR004364. aa-tRNA-synt_II.
    IPR018150. aa-tRNA-synt_II-like.
    IPR006195. aa-tRNA-synth_II.
    IPR004523. Asp-tRNA_synthase.
    IPR002312. Asp/Asn-tRNA-synth_IIb.
    IPR012340. NA-bd_OB-fold.
    IPR004365. NA-bd_OB_tRNA.
    [Graphical view ]
    PANTHERi PTHR22594. PTHR22594. 1 hit.
    PTHR22594:SF10. PTHR22594:SF10. 1 hit.
    Pfami PF00152. tRNA-synt_2. 1 hit.
    PF01336. tRNA_anti-codon. 1 hit.
    [Graphical view ]
    PRINTSi PR01042. TRNASYNTHASP.
    SUPFAMi SSF50249. SSF50249. 1 hit.
    TIGRFAMsi TIGR00458. aspS_nondisc. 1 hit.
    PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence polymorphisms in the yeast gene encoding aspartyl tRNA synthase."
      Reid G.A.
      Nucleic Acids Res. 16:1212-1212(1988) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
      , 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.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "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] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-557.
    7. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
      Strain: ATCC 90840 / EAY235 / FY23.
    8. "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] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, MUTAGENESIS.
    9. "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] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PRO-273.
    10. "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.
    11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-14; SER-301 AND SER-502, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-502, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), MUTAGENESIS.

    Entry informationi

    Entry nameiSYDC_YEAST
    AccessioniPrimary (citable) accession number: P04802
    Secondary accession number(s): D6VXY6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 163 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 5750 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3