Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for A9BJE0

Entry ID Method Resolution Chain Position Source
AF-A9BJE0-F1 Predicted AlphaFoldDB

No variants for A9BJE0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A9BJE0

No associated diseases with A9BJE0

4 regional properties for A9BJE0

Type Name Position InterPro Accession
domain DHHA1 domain 737 - 873 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 655 - 698 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 8 - 557 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 4 - 711 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

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

4 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).
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).

1 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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKYFTSEEIR ENFLYFFEKK GHKKLPSSSL IPNDPQLLFT VAGMVPFKPI FWGKVEPTYT
70 80 90 100 110 120
RITTCQKCLR TNDIENVGRT PRHHTFFEML GNFSFGDYFK KEAIKWAWEF LTEELGLPAE
130 140 150 160 170 180
KLWASVYETD DEAFNIWKDD IKIPENKILR FGKEENWWGP AGQTGPCGPC SEIYFDTGYT
190 200 210 220 230 240
ENCPDQENCT PACDCGRFVE IWNIVFTEYY SDENGNLSPL PRKNIDTGAG FERICAVTQG
250 260 270 280 290 300
KYDNFDSDLF KEIIEEIQRI FGVKFRVNKS KDVSIKVIAD HSRAIAFLIS EGIIPSNEGR
310 320 330 340 350 360
GYVLRRLIRR AVRHGALLEA KGPFLSSILE TVIKKMGKIY PELIEKEALI KDISFMEEEK
370 380 390 400 410 420
FFETMEKGME RLNNIIQNLN NETTLPGKIA FELYDTYGFP LDLTKEILSE KGIEVDEKEF
430 440 450 460 470 480
TELMNKQREM ARSASGKVEY DTEKQIYKEI DKFLTPTEFI GYDKLSSTEE VQLIIKGNSI
490 500 510 520 530 540
VPQAQEGDEI ELFFPKTPFY AERGGQVSDK GVIYNETFEA EVIHVKPIRN EIISHLVKIK
550 560 570 580 590 600
KGSIKNGERV FLKVDEKKRK ATEKNHTATH LLHSALRKVI GEHIRQAGSY VAPERLRFDF
610 620 630 640 650 660
THYEPLTQDQ IKQIEYLINE QIQKAIPVNI YLKSLEEAKS MDVIALFEEK YGEVVRIVEI
670 680 690 700 710 720
DDFSRELCGG THVSNTGEIG LFKILEESSI SSGVRRIEAI TGFESLNYAT ELESIMTNLS
730 740 750 760 770 780
KMLDSSRDQI PDKIEGILKT IKNQEKEIKQ LQFQLATKNI ERLAETPQII EGEKVVVAQL
790 800 810 820 830 840
ENLEKDVHAN TADILLQKLG RGVVILFNKS NNEQVSLVVK VSKDTSKKFH AGNIARKIAS
850 860 870
YLGGGGGGGP TFAQAGGKYA NKVKEVIEHI NDFMEV