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 A1SST6

Entry ID Method Resolution Chain Position Source
AF-A1SST6-F1 Predicted AlphaFoldDB

No variants for A1SST6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1SST6

No associated diseases with A1SST6

6 regional properties for A1SST6

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 117 - 556 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 19 - 97 IPR004365
domain Aminoacyl-tRNA synthetase, class II 141 - 554 IPR006195
domain GAD domain 307 - 405 IPR029351
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 2 - 134 IPR047089
domain Aspartate-tRNA ligase, type 1, core domain 138 - 558 IPR047090

Functions

Description
EC Number 6.1.1.23 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
aspartate-tRNA ligase activity Catalysis of the reaction: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).
aspartate-tRNA(Asn) ligase activity Catalysis of the reaction: tRNA(Asx) + L-aspartate + ATP = aspartyl-tRNA(Asx) + diphosphate + AMP.
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
aspartyl-tRNA aminoacylation The process of coupling aspartate to aspartyl-tRNA, catalyzed by aspartyl-tRNA synthetase. The aspartyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of an aspartic acid 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
MRTMYCGEVT EAVLGQEIQL VGWINKQRDL GGVIFLDMRD RAGIVQVFFD ADTPIATALA
70 80 90 100 110 120
TTVRNEFCIQ IKGLVRARPE GQVNKDMTTG GIEILGLELE ILNRSEPLPL DSNQQNSEEQ
130 140 150 160 170 180
RLRYRYLDLR RPEMAKRMQF RAKVSSFVRR FLDDQDFLDV ETPILTKATP EGARDYLVPS
190 200 210 220 230 240
RTHKGKFFAL PQSPQLFKQL LMMSGMDRYY QIVKCFRDED LRADRQPEFT QIDIETSFMN
250 260 270 280 290 300
ADQVMEISEE MIVKLFKEML NVDLGNFPKM TYAEALRRFG SDKPDLRIDF ELYDVADLMK
310 320 330 340 350 360
DVEFNVFSGP ANDPDSRVAV ICVPGGAKLS RKNIDEYGKF VTIYGAKGLA WMKVNEVAKG
370 380 390 400 410 420
LEGVQSPVAK FLNEEIVTEL LIRTGAKDGD IILFGADKSN IVSEAIGALR LKVAQDLGLV
430 440 450 460 470 480
KDQWKPLWVI DFPMFEPLDD GGLTPLHHPF TAPIGLTVEE LEANPVGAIS NAYDMVLNGC
490 500 510 520 530 540
ELGGGSVRIH KQDMQAAIFR ILKISDEEAE DKFGFLLEAL KYGAPPHAGL AFGLDRLVML
550 560 570 580 590
MTGTSSIRDV IAFPKTASAA CPLTNAPSFA NPAVLAELNV AVVADPKKVI SE