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 Q0AIE4

Entry ID Method Resolution Chain Position Source
AF-Q0AIE4-F1 Predicted AlphaFoldDB

No variants for Q0AIE4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q0AIE4

No associated diseases with Q0AIE4

6 regional properties for Q0AIE4

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 119 - 560 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 19 - 102 IPR004365
domain Aminoacyl-tRNA synthetase, class II 139 - 557 IPR006195
domain GAD domain 309 - 408 IPR029351
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 2 - 135 IPR047089
domain Aspartate-tRNA ligase, type 1, core domain 139 - 561 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
MRTDYCGAIN TRHLGRTITL CGWVHRRRDH GGVIFIDLRD REGIVQIVCD PDNVAAFPIA
70 80 90 100 110 120
EKIRNEFVLE ITGLVRHRPE GTVNRGIPSG EIEVLVSTIE ILNPSLTPPF QMDDDNLSEA
130 140 150 160 170 180
IRLEYRYLDL RRPAMQHNIR LRHKVTMATR VFLDQHGFID VETPMLTKST PEGARDYLVP
190 200 210 220 230 240
SRVNVGCFFA LPQSPQLFKQ LLMVSGFDRY YQITRCFRDE DLRADRQPEF TQIDIETSFL
250 260 270 280 290 300
QENDIMDLME DMIRRLFADV INVSLPDPFP RISYADAMFR YGSDKPDLRV PLELTELTDL
310 320 330 340 350 360
MQDVPFQVFR DAAQKPGGRV AALRVPGGGE LSRKEIDEYT RFVGIYGAKG LAYIKINDLT
370 380 390 400 410 420
KGMEGLQSPI LKFLPEPVVQ SMLERTQAQN GDLVFFGADK VKTVNDALGA LRVKIGHERG
430 440 450 460 470 480
LATNLWQPLW VVDFPMFEWD EEEKRWQALH HPFTAPSQGH EDFLATDPGK ALSRAYDMVL
490 500 510 520 530 540
NGMEIGGGSI RIHRQDVQSK VFQALNIADD EAKLKFGFLL DALQYGAPPH GGIAFGLDRI
550 560 570 580 590
VAMMTGTDSI RDVIAFPKTQ RAQCLLTQAP STVEEKQLRE LHIRLRKTDI TTD