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Reviewed, UniProtKB/Swiss-Prot P40825 (SYAC_YEAST)

Last modified November 25, 2008. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alanyl-tRNA synthetase, cytoplasmic
    EC=6.1.1.7
Alternative name(s):
    Alanine--tRNA ligase
      Short name=AlaRS
Gene names
Name: ALA1
Ordered Locus Names: YOR335C
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length958 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).

Subcellular location

Cytoplasm.

Miscellaneous

Present with 33800 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords

   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMPhosphoprotein
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processalanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion

Inferred from direct assay. Source: SGD

   Molecular functionATP binding

Inferred from electronic annotation. Source: InterPro

alanine-tRNA ligase activity

Inferred from electronic annotation. Source: InterPro

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RSP5P399401EBI-18648,EBI-16219
SSM4P403181EBI-18648,EBI-18208

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 958958Alanyl-tRNA synthetase, cytoplasmic
PRO_0000075287

Amino acid modifications

Modified residue4791Phosphoserine
Modified residue9501Phosphoserine

Experimental info

Sequence conflict1361R → S in AAC49007. Ref.1
Sequence conflict465 – 4673KDQ → RTK in AAC49007. Ref.1
Sequence conflict840 – 8412FE → LQ in AAC49007. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P40825-1 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 50FD31C2E2D40F32

FASTA958107,277
        10         20         30         40         50         60 
MTIGDKQKWT ATNVRNTFLD YFKSKEHKFV KSSPVVPFDD PTLLFANAGM NQYKPIFLGT 

        70         80         90        100        110        120 
VDPASDFYTL KRAYNSQKCI RAGGKHNDLE DVGKDSYHHT FFEMLGNWSF GDYFKKEAIT 

       130        140        150        160        170        180 
YSWTLLTEVY GIPKDRLYVT YFEGDEKLGL EPDTEARELW KNVGVPDDHI LPGNAKDNFW 

       190        200        210        220        230        240 
EMGDQGPCGP CSEIHYDRIG GRNAASLVNM DDPDVLEVWN LVFIQFNREQ DGSLKPLPAK 

       250        260        270        280        290        300 
HIDTGMGFER LVSVLQDVRS NYDTDVFTPL FERIQEITSV RPYSGNFGEN DKDGIDTAYR 

       310        320        330        340        350        360 
VLADHVRTLT FALADGGVPN NEGRGYVLRR ILRRGARYAR KYMNYPIGNF FSTLAPTLIS 

       370        380        390        400        410        420 
QVQDIFPELA KDPAFLFEIL DEEEASFAKT LDRGERLFEK YASAASKTES KTLDGKQVWR 

       430        440        450        460        470        480 
LYDTYGFPVD LTELMAEEQG LKIDGPGFEK AKQESYEASK RGGKKDQSDL IKLNVHELSE 

       490        500        510        520        530        540 
LNDAKVPKTN DEFKYGSANV EGTILKLHDG TNFVDEITEP GKKYGIILDK TCFYAEQGGQ 

       550        560        570        580        590        600 
EYDTGKIVID DAAEFNVENV QLYNGFVFHT GSLEEGKLSV GDKIIASFDE LRRFPIKNNH 

       610        620        630        640        650        660 
TGTHILNFAL KETLGNDVDQ KGSLVAPEKL RFDFSHKKAV SNEELKKVED ICNEQIKENL 

       670        680        690        700        710        720 
QVFYKEIPLD LAKSIDGVRA VFGETYPDPV RVVSVGKPIE ELLANPANEE WTKYSIEFCG 

       730        740        750        760        770        780 
GTHVNKTGDI KYFVILEESG IAKGIRRIVA VTGTEAFEAQ RLAEQFAADL DAADKLPFSP 

       790        800        810        820        830        840 
IKEKKLKELG VKLGQLSISV ITKNELKQKF NKIEKAVKDE VKSRAKKENK QTLDEVKTFF 

       850        860        870        880        890        900 
ETNENAPYLV KFIDISPNAK AITEAINYMK SNDSVKDKSI YLLAGNDPEG RVAHGCYISN 

       910        920        930        940        950 
AALAKGIDGS ALAKKVSSII GGKAGGKGNV FQGMGDKPAA IKDAVDDLES LFKEKLSI 

« Hide

References

« Hide 'large scale' references
[1]Ripmaster T.L., Schimmel P.
Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence of 29 kb around the PDR10 locus on the right arm of Saccharomyces cerevisiae chromosome XV: similarity to part of chromosome I."
Parle-McDermott A.G., Hand N.J., Goulding S.E., Wolfe K.H.
Yeast 12:999-1004(1996) [PubMed: 8896263] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed: 9169874] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[4]"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].
[5]"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-950, MASS SPECTROMETRY.
[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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479 AND SER-950, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

U18672 Genomic DNA. Translation: AAC49007.1.
Z49821 Genomic DNA. Translation: CAA89980.1.
Z75243 Genomic DNA. Translation: CAA99658.1.
PIRS62065.
RefSeqNP_014980.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:6286N.
IntActP40825.

Proteomic databases

PeptideAtlasP40825.

Genome annotation databases

EnsemblYOR335C. Saccharomyces cerevisiae. [Contig view]
GeneID854513.
GenomeReviewsGene locus YOR335C in contig Y13140_GR.
KEGGsce:YOR335C.
NMPDRfig|4932.3.peg.6096.

Organism-specific databases

CYGDYOR335c.
SGDS000005862. ALA1.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP40825.

Gene expression databases

ArrayExpressP40825.
GermOnlineYOR335C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR002318. Ala-tRNA-synth_IIc.
IPR003156. Pesterase_DHHA1.
IPR012947. tRNA_SAD.
[Graphical view]
PfamPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR00980. TRNASYNTHALA.
TIGRFAMsTIGR00344. alaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubP40825.
NextBio976870.

Entry information

Entry nameSYAC_YEAST
AccessionPrimary (citable) accession number: P40825
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 1, 1996
Last modified: November 25, 2008
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents