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 Q72KF7

Entry ID Method Resolution Chain Position Source
AF-Q72KF7-F1 Predicted AlphaFoldDB

No variants for Q72KF7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q72KF7

No associated diseases with Q72KF7

1 regional properties for Q72KF7

Type Name Position InterPro Accession
domain NADPH-dependent FMN reductase-like 35 - 179 IPR005025

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
MRVFIDEIAR HVDQEVELRG WLYQRRSKGK IHFLILRDGT GFLQATVVQG EVPEAVFREA
70 80 90 100 110 120
DHLPQETALR VWGRVREDRR APGGFELAVR DLQVVSRPQG EYPIGPKEHG IDFLMDHRHL
130 140 150 160 170 180
WLRHRRPFAV MRIRDELERA IHEFFGERGF LRFDAPILTP SAVEGTTELF EVELFDGEKA
190 200 210 220 230 240
YLSQSGQLYA EAGALAFAKV YTFGPTFRAE RSKTRRHLLE FWMVEPEVAF MTHEENMALQ
250 260 270 280 290 300
EELVSFLVAR VLERRSRELE MLGRDPKALE PAAEGHYARL TYKEAVALVN RIAQEDPEVP
310 320 330 340 350 360
PLPYGEDFGA PHEAALSRRF DRPVFVERYP ARIKAFYMEP DPEDPELVLN DDLLAPEGYG
370 380 390 400 410 420
EIIGGSQRIH DLELLRRKIQ EFGLPEEVYD WYLDLRRFGS VPHSGFGLGL ERTVAWICGL
430
AHVREAIPFP RMYTRMRP