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 P75521

Entry ID Method Resolution Chain Position Source
AF-P75521-F1 Predicted AlphaFoldDB

No variants for P75521

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P75521

No associated diseases with P75521

3 regional properties for P75521

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 118 - 449 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 22 - 100 IPR004365
domain Aminoacyl-tRNA synthetase, class II 136 - 445 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
MSATAISDLF EKPAQFKNKK IKLTGWLKNK RTSANIIFLE VNDGSTLLNL QAVVKQDQPE
70 80 90 100 110 120
LFALAESISL ASAVSVSGTV ALTPKSKQPL ELVVKQINVL STARADYPLQ KKEHSLEFFR
130 140 150 160 170 180
NNAYLRVRAR TYFAIMKVRS LLSQAIFDYF FKNDFVLVHS PILTSNDCEG AGETFELKQG
190 200 210 220 230 240
KEFFNKTTYL TVSGQFGAEC YAQAFKKVFT FGPTFRAEKS HTSRHLSEFW MIEPEVAFAN
250 260 270 280 290 300
LKDLIKLIES TVKTVIKQVM QKAKQELDFL EKQFDVKLME RLKQITSTKN FHVLEYTKAL
310 320 330 340 350 360
EILKTAQASG QANFEVQDFN FGLDLKTEHE RFLCEQHFHN QPVFVINYPK DFKAFYMKQN
370 380 390 400 410 420
ADGRTVGAVD LLFPQIGEIC GGSEREGNLE KLVERCQAMQ IDTQTLNWYL DMRKWGYFAS
430 440 450
AGFGLGFDRL LAYICGLENI RDAIPFPRAH GSINY