P00957

PR
Gene name
alaS (lovB, b2697, JW2667)
Protein name
Alanine--tRNA ligase
Names
Alanyl-tRNA synthetase, AlaRS
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b2697
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)

398-468 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

9 structures for P00957

Entry ID Method Resolution Chain Position Source
3HXU X-ray 210 A A 2-442 PDB
3HXV X-ray 193 A A 2-442 PDB
3HXW X-ray 193 A A 2-442 PDB
3HXX X-ray 211 A A 2-442 PDB
3HXY X-ray 227 A A 2-442 PDB
3HXZ X-ray 199 A A/B/C/D 2-442 PDB
3HY0 X-ray 190 A A/B 2-442 PDB
3HY1 X-ray 279 A A/B 2-442 PDB
AF-P00957-F1 Predicted AlphaFoldDB

No variants for P00957

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P00957

No associated diseases with P00957

4 regional properties for P00957

Type Name Position InterPro Accession
domain DHHA1 domain 732 - 871 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 653 - 696 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 7 - 556 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 3 - 709 IPR018165

Functions

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

2 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

9 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.
DNA-binding transcription repressor activity A DNA-binding transcription factor activity that represses or decreases the transcription of specific gene sets.
identical protein binding Binding to an identical protein or proteins.
Ser-tRNA(Ala) hydrolase activity Catalysis of the hydrolysis of misacylated Ser-tRNA(Ala).
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.
negative regulation of DNA-templated transcription Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription.
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
P40825 ALA1 Alanine--tRNA ligase, mitochondrial Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
10 20 30 40 50 60
MSKSTAEIRQ AFLDFFHSKG HQVVASSSLV PHNDPTLLFT NAGMNQFKDV FLGLDKRNYS
70 80 90 100 110 120
RATTSQRCVR AGGKHNDLEN VGYTARHHTF FEMLGNFSFG DYFKHDAIQF AWELLTSEKW
130 140 150 160 170 180
FALPKERLWV TVYESDDEAY EIWEKEVGIP RERIIRIGDN KGAPYASDNF WQMGDTGPCG
190 200 210 220 230 240
PCTEIFYDHG DHIWGGPPGS PEEDGDRYIE IWNIVFMQFN RQADGTMEPL PKPSVDTGMG
250 260 270 280 290 300
LERIAAVLQH VNSNYDIDLF RTLIQAVAKV TGATDLSNKS LRVIADHIRS CAFLIADGVM
310 320 330 340 350 360
PSNENRGYVL RRIIRRAVRH GNMLGAKETF FYKLVGPLID VMGSAGEDLK RQQAQVEQVL
370 380 390 400 410 420
KTEEEQFART LERGLALLDE ELAKLSGDTL DGETAFRLYD TYGFPVDLTA DVCRERNIKV
430 440 450 460 470 480
DEAGFEAAME EQRRRAREAS GFGADYNAMI RVDSASEFKG YDHLELNGKV TALFVDGKAV
490 500 510 520 530 540
DAINAGQEAV VVLDQTPFYA ESGGQVGDKG ELKGANFSFA VEDTQKYGQA IGHIGKLAAG
550 560 570 580 590 600
SLKVGDAVQA DVDEARRARI RLNHSATHLM HAALRQVLGT HVSQKGSLVN DKVLRFDFSH
610 620 630 640 650 660
NEAMKPEEIR AVEDLVNTQI RRNLPIETNI MDLEAAKAKG AMALFGEKYD ERVRVLSMGD
670 680 690 700 710 720
FSTELCGGTH ASRTGDIGLF RIISESGTAA GVRRIEAVTG EGAIATVHAD SDRLSEVAHL
730 740 750 760 770 780
LKGDSNNLAD KVRSVLERTR QLEKELQQLK EQAAAQESAN LSSKAIDVNG VKLLVSELSG
790 800 810 820 830 840
VEPKMLRTMV DDLKNQLGST IIVLATVVEG KVSLIAGVSK DVTDRVKAGE LIGMVAQQVG
850 860 870
GKGGGRPDMA QAGGTDAAAL PAALASVKGW VSAKLQ