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 Q835J8

Entry ID Method Resolution Chain Position Source
AF-Q835J8-F1 Predicted AlphaFoldDB

No variants for Q835J8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q835J8

No associated diseases with Q835J8

4 regional properties for Q835J8

Type Name Position InterPro Accession
domain DHHA1 domain 738 - 877 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 657 - 700 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 8 - 559 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 4 - 713 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
MKELTSSQVR QMYLDFFKSK GHSVEPSASL VPVNDPTLLW INSGVATLKK YFDGSVVPEN
70 80 90 100 110 120
PRITNAQKSI RTNDIENVGK TARHHTMFEM LGNFSIGDYF KNEAIHWAWE FLTGAEWLAF
130 140 150 160 170 180
DPEKLYVTVY PKDTEAKRIW RDEVGLSEDH IIDVEDNFWD IGAGPSGPDT EIFYDRGEEF
190 200 210 220 230 240
LDIPEDDPEN YPGGENERYL EIWNLVFSEF NHTPEDTYEP LPHKNIDTGM GLERVVSIIQ
250 260 270 280 290 300
DAPTNFETDL FMPIIHAVEA LGTNVKYGDA PQTDVSFKVI ADHIRALSFA IGDGALPSNE
310 320 330 340 350 360
GRGYVLRRLL RRAVMHGKKL GINEAFLYKL VPVVGEIMVS YYPEVLQQKD FIEKVVRTEE
370 380 390 400 410 420
ERFHETINEG LSMLNEVIKE VKDAKGDTLD GKIIFKLYDT FGFPVELTEE VAEDEGLKVD
430 440 450 460 470 480
HAGFETEMEA QRERARSARS KETSMGVQSA LLTDIKVESK FVGYTELTHD SELFVIIQGD
490 500 510 520 530 540
ALVNEASAGT AELIFAETPF YAEMGGQIAD RGYVKNTAGE VVANVVDVKK APNGQFLHKV
550 560 570 580 590 600
EVLAPLAEGQ IYQLQVDERM RTRILKNHTA THLLHRALKD VLGEHANQAG SLVAPGHLRF
610 620 630 640 650 660
DFTHFGQVTS EELARMEAIV NEKIWEAIPV VTIETDIDTA KNMGAMALFG EKYGKEVRVV
670 680 690 700 710 720
NIGDYSIELC GGTHVANTED IGIFKIVSES GIGAGVRRIE AVTSKEAYQL LQEEERQLKE
730 740 750 760 770 780
IATLVKSPQL KEVVTKTEQL QQQLRDLQKE NEQLAGKLAN QQAGDIFKDV KDINGVRYIA
790 800 810 820 830 840
AQVNVKDMNQ LRQLADQWKQ KELSDVLVLA TAQDEKVSLL AAMTKDMNGK GLKAGDLIKA
850 860 870
IAPKVGGGGG GRPDMAQAGG KNPAGIADAL AEVENWLANA