P40825

PR
Gene name
ALA1
Protein name
Alanine--tRNA ligase, mitochondrial
Names
Alanyl-tRNA synthetase, AlaRS
Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
KEGG Pathway
sce:YOR335C
EC number
6.1.1.7: Ligases forming aminoacyl-tRNA and related compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-58 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P40825

Entry ID Method Resolution Chain Position Source
AF-P40825-F1 Predicted AlphaFoldDB

No variants for P40825

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P40825

No associated diseases with P40825

2 regional properties for P40825

Type Name Position InterPro Accession
domain Aldehyde dehydrogenase domain 1 - 212 IPR015590
conserved_site Aldehyde dehydrogenase, cysteine active site 23 - 34 IPR016160

Functions

Description
EC Number 6.1.1.7 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • [Isoform Cytoplasmic]: Cytoplasm
  • ;
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

6 GO annotations of molecular function

Name Definition
alanine-tRNA ligase activity Catalysis of the reaction: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).
amino acid binding Binding to an amino acid, organic acids containing one or more amino substituents.
aminoacyl-tRNA editing activity The hydrolysis of an incorrectly aminoacylated tRNA.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
tRNA binding Binding to a transfer RNA.
zinc ion binding Binding to a zinc ion (Zn).

3 GO annotations of biological process

Name Definition
alanyl-tRNA aminoacylation The process of coupling alanine to alanyl-tRNA, catalyzed by alanyl-tRNA synthetase. The alanyl-tRNA synthetase is a class-II synthetases. The activated amino acid is transferred to the 3'-OH group of an alanine accetping tRNA.
mitochondrial alanyl-tRNA aminoacylation The process of coupling alanine to alanyl-tRNA in a mitochondrion, catalyzed by alanyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA.
tRNA modification The covalent alteration of one or more nucleotides within a tRNA molecule to produce a tRNA molecule with a sequence that differs from that coded genetically.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P00957 alaS Alanine--tRNA ligase Escherichia coli (strain K12) PR
10 20 30 40 50 60
MTSTTGLRNL TLSFKKQLTT STRTIMTIGD KQKWTATNVR NTFLDYFKSK EHKFVKSSPV
70 80 90 100 110 120
VPFDDPTLLF ANAGMNQYKP IFLGTVDPAS DFYTLKRAYN SQKCIRAGGK HNDLEDVGKD
130 140 150 160 170 180
SYHHTFFEML GNWSFGDYFK KEAITYSWTL LTEVYGIPKD RLYVTYFEGD EKLGLEPDTE
190 200 210 220 230 240
ARELWKNVGV PDDHILPGNA KDNFWEMGDQ GPCGPCSEIH YDRIGGRNAA SLVNMDDPDV
250 260 270 280 290 300
LEVWNLVFIQ FNREQDGSLK PLPAKHIDTG MGFERLVSVL QDVRSNYDTD VFTPLFERIQ
310 320 330 340 350 360
EITSVRPYSG NFGENDKDGI DTAYRVLADH VRTLTFALAD GGVPNNEGRG YVLRRILRRG
370 380 390 400 410 420
ARYARKYMNY PIGNFFSTLA PTLISQVQDI FPELAKDPAF LFEILDEEEA SFAKTLDRGE
430 440 450 460 470 480
RLFEKYASAA SKTESKTLDG KQVWRLYDTY GFPVDLTELM AEEQGLKIDG PGFEKAKQES
490 500 510 520 530 540
YEASKRGGKK DQSDLIKLNV HELSELNDAK VPKTNDEFKY GSANVEGTIL KLHDGTNFVD
550 560 570 580 590 600
EITEPGKKYG IILDKTCFYA EQGGQEYDTG KIVIDDAAEF NVENVQLYNG FVFHTGSLEE
610 620 630 640 650 660
GKLSVGDKII ASFDELRRFP IKNNHTGTHI LNFALKETLG NDVDQKGSLV APEKLRFDFS
670 680 690 700 710 720
HKKAVSNEEL KKVEDICNEQ IKENLQVFYK EIPLDLAKSI DGVRAVFGET YPDPVRVVSV
730 740 750 760 770 780
GKPIEELLAN PANEEWTKYS IEFCGGTHVN KTGDIKYFVI LEESGIAKGI RRIVAVTGTE
790 800 810 820 830 840
AFEAQRLAEQ FAADLDAADK LPFSPIKEKK LKELGVKLGQ LSISVITKNE LKQKFNKIEK
850 860 870 880 890 900
AVKDEVKSRA KKENKQTLDE VKTFFETNEN APYLVKFIDI SPNAKAITEA INYMKSNDSV
910 920 930 940 950 960
KDKSIYLLAG NDPEGRVAHG CYISNAALAK GIDGSALAKK VSSIIGGKAG GKGNVFQGMG
970 980
DKPAAIKDAV DDLESLFKEK LSI