CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007415
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alanine--tRNA ligase, mitochondrial 
Protein Synonyms/Alias
 Alanyl-tRNA synthetase; AlaRS 
Gene Name
 ALA1 
Gene Synonyms/Alias
 CDC64; YOR335C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
48NTFLDYFKSKEHKFVacetylation[1]
103KRAYNSQKCIRAGGKubiquitination[2]
110KCIRAGGKHNDLEDVacetylation[1]
265SLKPLPAKHIDTGMGacetylation[1]
425RGERLFEKYASAASKacetylation[1]
475IDGPGFEKAKQESYEacetylation[1]
510LSELNDAKVPKTNDEacetylation[1]
510LSELNDAKVPKTNDEubiquitination[2]
646LGNDVDQKGSLVAPEacetylation[1]
646LGNDVDQKGSLVAPEubiquitination[2]
654GSLVAPEKLRFDFSHubiquitination[2]
698EIPLDLAKSIDGVRAacetylation[1]
698EIPLDLAKSIDGVRAubiquitination[2]
895TEAINYMKSNDSVKDacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 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 (By similarity). 
Sequence Annotation
 METAL 625 625 Zinc (Potential).
 METAL 629 629 Zinc (Potential).
 METAL 744 744 Zinc (Potential).
 METAL 748 748 Zinc (Potential).
 MOD_RES 504 504 Phosphoserine.
 MOD_RES 975 975 Phosphoserine.  
Keyword
 Alternative initiation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Metal-binding; Mitochondrion; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding; Transit peptide; tRNA-binding; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 983 AA 
Protein Sequence
MTSTTGLRNL TLSFKKQLTT STRTIMTIGD KQKWTATNVR NTFLDYFKSK EHKFVKSSPV 60
VPFDDPTLLF ANAGMNQYKP IFLGTVDPAS DFYTLKRAYN SQKCIRAGGK HNDLEDVGKD 120
SYHHTFFEML GNWSFGDYFK KEAITYSWTL LTEVYGIPKD RLYVTYFEGD EKLGLEPDTE 180
ARELWKNVGV PDDHILPGNA KDNFWEMGDQ GPCGPCSEIH YDRIGGRNAA SLVNMDDPDV 240
LEVWNLVFIQ FNREQDGSLK PLPAKHIDTG MGFERLVSVL QDVRSNYDTD VFTPLFERIQ 300
EITSVRPYSG NFGENDKDGI DTAYRVLADH VRTLTFALAD GGVPNNEGRG YVLRRILRRG 360
ARYARKYMNY PIGNFFSTLA PTLISQVQDI FPELAKDPAF LFEILDEEEA SFAKTLDRGE 420
RLFEKYASAA SKTESKTLDG KQVWRLYDTY GFPVDLTELM AEEQGLKIDG PGFEKAKQES 480
YEASKRGGKK DQSDLIKLNV HELSELNDAK VPKTNDEFKY GSANVEGTIL KLHDGTNFVD 540
EITEPGKKYG IILDKTCFYA EQGGQEYDTG KIVIDDAAEF NVENVQLYNG FVFHTGSLEE 600
GKLSVGDKII ASFDELRRFP IKNNHTGTHI LNFALKETLG NDVDQKGSLV APEKLRFDFS 660
HKKAVSNEEL KKVEDICNEQ IKENLQVFYK EIPLDLAKSI DGVRAVFGET YPDPVRVVSV 720
GKPIEELLAN PANEEWTKYS IEFCGGTHVN KTGDIKYFVI LEESGIAKGI RRIVAVTGTE 780
AFEAQRLAEQ FAADLDAADK LPFSPIKEKK LKELGVKLGQ LSISVITKNE LKQKFNKIEK 840
AVKDEVKSRA KKENKQTLDE VKTFFETNEN APYLVKFIDI SPNAKAITEA INYMKSNDSV 900
KDKSIYLLAG NDPEGRVAHG CYISNAALAK GIDGSALAKK VSSIIGGKAG GKGNVFQGMG 960
DKPAAIKDAV DDLESLFKEK LSI 983 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0004813; F:alanine-tRNA ligase activity; IGI:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
 GO:0070143; P:mitochondrial alanyl-tRNA aminoacylation; IC:SGD. 
Interpro
 IPR002318; 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; Pesterase_DHHA1.
 IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
 IPR012947; tRNA_SAD. 
Pfam
 PF02272; DHHA1
 PF01411; tRNA-synt_2c
 PF07973; tRNA_SAD 
SMART
 SM00863; tRNA_SAD 
PROSITE
 PS50860; AA_TRNA_LIGASE_II_ALA 
PRINTS
 PR00980; TRNASYNTHALA.