O29342

PR
Gene name
aspS
Protein name
Aspartate--tRNA(Asp/Asn) ligase
Names
Aspartyl-tRNA synthetase, AspRS, Non-discriminating aspartyl-tRNA synthetase, ND-AspRS
Species
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
KEGG Pathway
afu:AF_0920
EC number
6.1.1.23: Ligases forming aminoacyl-tRNA and related compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

31-110 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for O29342

Entry ID Method Resolution Chain Position Source
AF-O29342-F1 Predicted AlphaFoldDB

No variants for O29342

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O29342

No associated diseases with O29342

3 regional properties for O29342

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 116 - 424 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 17 - 96 IPR004365
domain Aminoacyl-tRNA synthetase, class II 100 - 430 IPR006195

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.

5 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.
magnesium ion binding Binding to a magnesium (Mg) ion.
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
MRVYTADVKP EMEGQKVTLY GWVHEVRDLG GLVFILLRDR EGIVQITLPR KFVSKQVFKL
70 80 90 100 110 120
AKKIRRESVI AVTGEVRREE KAPGGVEIIP ESIEVLNEAD APLPLEVTEK VPAELDTRLD
130 140 150 160 170 180
HRFMDLRRPR VQAIFRIRHQ VMQSVREFLS EEGFIEVHTP KIVSTATEGG TELFPISYFE
190 200 210 220 230 240
KEAFLNQSPQ LYKQVLMAAG FEKVFEIGPI FRAEEHNTTR HLNEAISIDI EMSFTDHNGV
250 260 270 280 290 300
MDVLERLVQR VYEDVAEKCE RYLGWLEVSL EIPELPFPRI TYDEAREIAA RKGEEIPWGE
310 320 330 340 350 360
DLSTNALKLV GEEMGGLYFI TDWPTESKPF YAMPYEDRPE ISKSFDLMHG WLELSSGAQR
370 380 390 400 410 420
IHLYDMLVES IKAKGMEPES FGFYLEAFRY GMPPHAGWGL GAERLIMSML GLKNVREAVL
FPRDRHRLVP