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 A9CTP8

Entry ID Method Resolution Chain Position Source
AF-A9CTP8-F1 Predicted AlphaFoldDB

No variants for A9CTP8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A9CTP8

No associated diseases with A9CTP8

2 regional properties for A9CTP8

Type Name Position InterPro Accession
domain NADPH-dependent FMN reductase-like 4 - 143 IPR005025
domain Flavodoxin/nitric oxide synthase 4 - 189 IPR008254

Functions

Description
EC Number 6.1.1.22 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.

2 GO annotations of molecular function

Name Definition
asparagine-tRNA ligase activity Catalysis of the reaction: L-asparagine + ATP + tRNA(Asn) = AMP + Asn-tRNA(Asn) + diphosphate + 2 H(+).
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

1 GO annotations of biological process

Name Definition
asparaginyl-tRNA aminoacylation The process of coupling asparagine to asparaginyl-tRNA, catalyzed by asparaginyl-tRNA synthetase. The asparaginyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of an asparagine-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
MKLQDNLKSI KKELERIKVE NWSKENIDKN TYRYIRLFDI DDSLMNQKIC FFGWVKSSRS
70 80 90 100 110 120
SSKISFIELI SQFKIIKCVI PTKVKLTDHT TLKVWGIMKP NNGNDEHQFE IDVQAYEVYG
130 140 150 160 170 180
GYQAPSFPLN IHSDKDTLLD LAHLGLRMPH RILFLQAQNE LLKALRKFYW NNNYTEITPP
190 200 210 220 230 240
TLVQTQVEGG ATLFKLNYYD QPAYLTQSSQ LYLETVAPVV GKAFCIMPSY RAEKSKTSRH
250 260 270 280 290 300
LSEFTHVEAE LVDIQFDELM DQIEQLIRST INEFYKNILP EIKKIDNDFQ PVVLSDKQFK
310 320 330 340 350 360
KITYEDAIHF LIAQNHKKTD NTDYQLGDDI SDASEKFLLE TYGENQPIFL IRFPTDHKPF
370 380 390 400 410 420
YVAKDQYGTQ TCDLLFPGIG EIVGGSMRET NYNNLLDGFK RENIDHEPYS WYLDMAKFGP
430 440 450
SPHGGYGLGF ERLLMCLMKY KSVDQSTLYC RKPSRCTP