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 Q9KDE6

Entry ID Method Resolution Chain Position Source
AF-Q9KDE6-F1 Predicted AlphaFoldDB

No variants for Q9KDE6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9KDE6

No associated diseases with Q9KDE6

1 regional properties for Q9KDE6

Type Name Position InterPro Accession
domain Amidohydrolase-related 50 - 431 IPR006680

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
MKYLTSAQVR QMFLDFFKEK GHDVEPSASL VPHDDPSLLW INSGVATLKK YFDGRVIPEN
70 80 90 100 110 120
PRITNAQKSI RTNDIENVGK TARHHTFFEM LGNFSIGDYF KEEAIEWAWE FLTSEKWIGF
130 140 150 160 170 180
DKEKLSVTVH PEDDEAYSYW KEKIGIPEER IIRLEGNFWD IGEGPSGPNT EIFYDRGPEY
190 200 210 220 230 240
GDQPNDPELY PGGENDRYLE VWNLVFSQFN HNPDGSYTPL PKKNIDTGMG LERMVSVIQN
250 260 270 280 290 300
VPTNFETDLF MPIIRATEKI SGTEYGSHHE ADVSFKVIAD HIRTVTFAIG DGALPSNEGR
310 320 330 340 350 360
GYVLRRLLRR AVRYAKQIGI DRPFMYELVP VVGDIMVDFY PEVKEKAAFI QKVVKTEEER
370 380 390 400 410 420
FHETLNEGLS ILEKVIDKAK SEGASTISGS DVFRLYDTYG FPVDLTEEYV EEQGLQVDLD
430 440 450 460 470 480
GFEAEMERQR ERARTARQQA GSMQVQDEVL GQITVDSTFI GYKQLSTETT IETIVLDKTV
490 500 510 520 530 540
ADYVGAGQEA KVILKETPFY AESGGQVADK GIIRGANGFA VVSDVQKAPN GQHLHTVIVK
550 560 570 580 590 600
EGTLQVNDQV QAIVEETERS GIVKNHTATH LLHRALKDVL GEHVNQAGSL VSEERLRFDF
610 620 630 640 650 660
SHFGQVTDEE KEKIERIVNE KIWQAIKVNI STKTLDEAKA IGAMALFGEK YGDIVRVVEV
670 680 690 700 710 720
GDYSIELCGG CHVTNTSEIG LFKIVSESGI GAGVRRIEAV TGKEAFLFMA KQLDLLKETA
730 740 750 760 770 780
ATVKAKNVKD VPVRVEALQQ QIRELQRENE SLNAKLGNME AGSLVNEVQK IEGVPVLAKA
790 800 810 820 830 840
ISGADMDGLR SIVDKLKQEI PSVVIVLGTA SEGKVNIVAG VTKDLINKGY HAGKLVKEVA
850 860 870
TRCGGGGGGR PDMAQAGGKQ PEKLQDALSF VYEYVKSIS