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Protein

Alanine--tRNA ligase, mitochondrial

Gene

ALA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.UniRule annotation1 Publication

Catalytic activityi

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

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi625 – 6251ZincUniRule annotation
Metal bindingi629 – 6291ZincUniRule annotation
Metal bindingi744 – 7441ZincUniRule annotation
Metal bindingi748 – 7481ZincUniRule annotation

GO - Molecular functioni

  • alanine-tRNA ligase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • tRNA binding Source: UniProtKB-KW

GO - Biological processi

  • alanyl-tRNA aminoacylation Source: SGD
  • mitochondrial alanyl-tRNA aminoacylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, tRNA-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-33810-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine--tRNA ligase, mitochondrialUniRule annotation (EC:6.1.1.7UniRule annotation)
Alternative name(s):
Alanyl-tRNA synthetaseUniRule annotation
Short name:
AlaRSUniRule annotation
Gene namesi
Name:ALA1UniRule annotation
Synonyms:CDC64
Ordered Locus Names:YOR335C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR335C.
SGDiS000005862. ALA1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424MitochondrionAdd
BLAST
Chaini25 – 983959Alanine--tRNA ligase, mitochondrialPRO_0000075287Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei504 – 5041PhosphoserineCombined sources
Modified residuei975 – 9751PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40825.
PeptideAtlasiP40825.
PRIDEiP40825.

PTM databases

iPTMnetiP40825.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi34718. 80 interactions.
DIPiDIP-6286N.
IntActiP40825. 6 interactions.
MINTiMINT-688621.

Structurei

3D structure databases

ProteinModelPortaliP40825.
SMRiP40825. Positions 29-778.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.UniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiP40825.
KOiK01872.
OMAiFDFNCPR.
OrthoDBiEOG799302.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B.
InterProiIPR002318. Ala-tRNA-lgiase_IIc.
IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR023033. Ala_tRNA_ligase_euk/bac.
IPR003156. DHHA1_dom.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsiTIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform Mitochondrial (identifier: P40825-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTSTTGLRNL TLSFKKQLTT STRTIMTIGD KQKWTATNVR NTFLDYFKSK
60 70 80 90 100
EHKFVKSSPV VPFDDPTLLF ANAGMNQYKP IFLGTVDPAS DFYTLKRAYN
110 120 130 140 150
SQKCIRAGGK HNDLEDVGKD SYHHTFFEML GNWSFGDYFK KEAITYSWTL
160 170 180 190 200
LTEVYGIPKD RLYVTYFEGD EKLGLEPDTE ARELWKNVGV PDDHILPGNA
210 220 230 240 250
KDNFWEMGDQ GPCGPCSEIH YDRIGGRNAA SLVNMDDPDV LEVWNLVFIQ
260 270 280 290 300
FNREQDGSLK PLPAKHIDTG MGFERLVSVL QDVRSNYDTD VFTPLFERIQ
310 320 330 340 350
EITSVRPYSG NFGENDKDGI DTAYRVLADH VRTLTFALAD GGVPNNEGRG
360 370 380 390 400
YVLRRILRRG ARYARKYMNY PIGNFFSTLA PTLISQVQDI FPELAKDPAF
410 420 430 440 450
LFEILDEEEA SFAKTLDRGE RLFEKYASAA SKTESKTLDG KQVWRLYDTY
460 470 480 490 500
GFPVDLTELM AEEQGLKIDG PGFEKAKQES YEASKRGGKK DQSDLIKLNV
510 520 530 540 550
HELSELNDAK VPKTNDEFKY GSANVEGTIL KLHDGTNFVD EITEPGKKYG
560 570 580 590 600
IILDKTCFYA EQGGQEYDTG KIVIDDAAEF NVENVQLYNG FVFHTGSLEE
610 620 630 640 650
GKLSVGDKII ASFDELRRFP IKNNHTGTHI LNFALKETLG NDVDQKGSLV
660 670 680 690 700
APEKLRFDFS HKKAVSNEEL KKVEDICNEQ IKENLQVFYK EIPLDLAKSI
710 720 730 740 750
DGVRAVFGET YPDPVRVVSV GKPIEELLAN PANEEWTKYS IEFCGGTHVN
760 770 780 790 800
KTGDIKYFVI LEESGIAKGI RRIVAVTGTE AFEAQRLAEQ FAADLDAADK
810 820 830 840 850
LPFSPIKEKK LKELGVKLGQ LSISVITKNE LKQKFNKIEK AVKDEVKSRA
860 870 880 890 900
KKENKQTLDE VKTFFETNEN APYLVKFIDI SPNAKAITEA INYMKSNDSV
910 920 930 940 950
KDKSIYLLAG NDPEGRVAHG CYISNAALAK GIDGSALAKK VSSIIGGKAG
960 970 980
GKGNVFQGMG DKPAAIKDAV DDLESLFKEK LSI
Note: Produced by alternative initiation at 2 upstream redundant non-AUG codons in-frame of the first AUG used for isoform Cytoplasmic.
Length:983
Mass (Da):110,059
Last modified:November 30, 2010 - v3
Checksum:iDC0F50DB6409F11F
GO
Isoform Cytoplasmic (identifier: P40825-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: Missing.

Show »
Length:958
Mass (Da):107,277
Checksum:i50FD31C2E2D40F32
GO

Sequence cautioni

The sequence AAC49007.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA89980.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA99658.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence DAA11096.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 74TTGL → NYRI in AAC49007 (PubMed:7761427).Curated
Sequence conflicti16 – 161Missing in AAC49007 (PubMed:7761427).Curated
Sequence conflicti161 – 1611R → S in AAC49007 (PubMed:7761427).Curated
Sequence conflicti490 – 4923KDQ → RTK in AAC49007 (PubMed:7761427).Curated
Sequence conflicti865 – 8662FE → LQ in AAC49007 (PubMed:7761427).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2525Missing in isoform Cytoplasmic. CuratedVSP_040236Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49821 Genomic DNA. Translation: CAA89980.1. Different initiation.
Z75243 Genomic DNA. Translation: CAA99658.1. Different initiation.
U18672 Genomic DNA. Translation: AAC49007.1. Different initiation.
BK006948 Genomic DNA. Translation: DAA11096.1. Different initiation.
PIRiS62065.
RefSeqiNP_014980.3. NM_001183755.3. [P40825-2]

Genome annotation databases

GeneIDi854513.
KEGGisce:YOR335C.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49821 Genomic DNA. Translation: CAA89980.1. Different initiation.
Z75243 Genomic DNA. Translation: CAA99658.1. Different initiation.
U18672 Genomic DNA. Translation: AAC49007.1. Different initiation.
BK006948 Genomic DNA. Translation: DAA11096.1. Different initiation.
PIRiS62065.
RefSeqiNP_014980.3. NM_001183755.3. [P40825-2]

3D structure databases

ProteinModelPortaliP40825.
SMRiP40825. Positions 29-778.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34718. 80 interactions.
DIPiDIP-6286N.
IntActiP40825. 6 interactions.
MINTiMINT-688621.

PTM databases

iPTMnetiP40825.

Proteomic databases

MaxQBiP40825.
PeptideAtlasiP40825.
PRIDEiP40825.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi854513.
KEGGisce:YOR335C.

Organism-specific databases

EuPathDBiFungiDB:YOR335C.
SGDiS000005862. ALA1.

Phylogenomic databases

InParanoidiP40825.
KOiK01872.
OMAiFDFNCPR.
OrthoDBiEOG799302.

Enzyme and pathway databases

BioCyciYEAST:G3O-33810-MONOMER.

Miscellaneous databases

PROiP40825.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B.
InterProiIPR002318. Ala-tRNA-lgiase_IIc.
IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR023033. Ala_tRNA_ligase_euk/bac.
IPR003156. DHHA1_dom.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsiTIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Wide cross-species aminoacyl-tRNA synthetase replacement in vivo: yeast cytoplasmic alanine enzyme replaced by human polymyositis serum antigen."
    Ripmaster T.L., Shiba K., Schimmel P.
    Proc. Natl. Acad. Sci. U.S.A. 92:4932-4936(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-983, FUNCTION.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. "Translation of a yeast mitochondrial tRNA synthetase initiated at redundant non-AUG codons."
    Tang H.L., Yeh L.S., Chen N.K., Ripmaster T., Schimmel P., Wang C.C.
    J. Biol. Chem. 279:49656-49663(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE INITIATION.
  9. "An unusual pattern of protein expression and localization of yeast alanyl-tRNA synthetase isoforms."
    Huang H.Y., Tang H.L., Chao H.Y., Yeh L.S., Wang C.C.
    Mol. Microbiol. 60:189-198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "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-504, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-975, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYA_YEAST
AccessioniPrimary (citable) accession number: P40825
Secondary accession number(s): D6W330
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 30, 2010
Last modified: June 8, 2016
This is version 143 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 33800 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.