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 Q7NBM9

Entry ID Method Resolution Chain Position Source
AF-Q7NBM9-F1 Predicted AlphaFoldDB

No variants for Q7NBM9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7NBM9

No associated diseases with Q7NBM9

3 regional properties for Q7NBM9

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 117 - 449 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 21 - 100 IPR004365
domain Aminoacyl-tRNA synthetase, class II 136 - 446 IPR006195

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.

3 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.
nucleic acid binding Binding to a nucleic acid.

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
MQLIEIKELL LSHSKREGEQ VVLVGSFKSI RSSGAIGFIA FSDSTALEPV QIVFKKENTP
70 80 90 100 110 120
NFDEISKLPI SSMILVKGVV RNTPEKKQPF EIQASKIVVL KEADPSYPLQ KKAHGSEFLR
130 140 150 160 170 180
ENAHLRVRTN KFYVIMKIRS ELANAFFEFF KNNDFLYVHA PLITSNDSEG AGESFEVISP
190 200 210 220 230 240
NDPNYFGKKA SLTVSGQFAA EAYAQGFKRV FTFGPTFRAE KSHTSKHLSE FWMIEPEVSL
250 260 270 280 290 300
MDLDKLTILI EQCVKHAIYY LFDYAKPELE WCNENLEPGL IDKLNNVINN DFPRVEYREV
310 320 330 340 350 360
IEILKKAVAE GVEFEVKDIH FGMDLKSEHE RYICEKVFKR PVFVINYPKD VKAFYMKLND
370 380 390 400 410 420
DNQTVAATDL LAPGIGEICG GSQREDSYNK LLTRCLELDI DPEFNNLQWY LDLRKYGYYR
430 440 450
SAGFGLGFER LLMYVTGCDN IRDAIPFPRF HGQLDF