A9BP37

PR
Gene name
aspS
Protein name
Aspartate--tRNA(Asp/Asn) ligase
Names
Aspartyl-tRNA synthetase, AspRS, Non-discriminating aspartyl-tRNA synthetase, ND-AspRS
Species
Delftia acidovorans (strain DSM 14801 / SPH-1)
KEGG Pathway
dac:Daci_5453
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)

543-600 (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 A9BP37

Entry ID Method Resolution Chain Position Source
AF-A9BP37-F1 Predicted AlphaFoldDB

No variants for A9BP37

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A9BP37

No associated diseases with A9BP37

6 regional properties for A9BP37

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 121 - 566 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 20 - 103 IPR004365
domain Aminoacyl-tRNA synthetase, class II 151 - 563 IPR006195
domain GAD domain 314 - 408 IPR029351
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 4 - 137 IPR047089
domain Aspartate-tRNA ligase, type 1, core domain 141 - 567 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
MAMRSHYCGL VTEALMGETV TLCGWVNRRR DHGGVIFIDL RDREGYVQVV CDPDRAEMFK
70 80 90 100 110 120
TAEGLRNEFC VQVKGLVRAR PEGTTNDKLK SGQIEVLCHE LNVLNASVTP PFQLDDENLS
130 140 150 160 170 180
ETVRLTNRVL DLRRPYMQRN MMLRYRTAIQ VRNFLDKEGF IDIETPMLGK STPEGARDYL
190 200 210 220 230 240
VPSRVHDGEF FALPQSPQLY KQMLMVAGYD RYYQITKCFR DEDLRADRQP EFTQIDCETS
250 260 270 280 290 300
FLDEEEIRAI FQRMITEVFK TQLDVDLGEF PMMTYQDAAF RFGSDKPDLR VKLEFTELTE
310 320 330 340 350 360
IMKDVDFKVF STPATTKGGR VVALRVPGGS QISRGEIDQY TEFVKIYGAK GLAWIKVNEV
370 380 390 400 410 420
AKGRDGLQSP IVKNLHDAAI AEILKRTGAQ DGDLIFFGAD KEKIVNDSIG ALRLKVGHSE
430 440 450 460 470 480
FGKANGLFEN RWAPLWVVDF PMFEHDEEND RWAAVHHPFT SPKDGHEELM VTDPANCLAK
490 500 510 520 530 540
AYDMVLNGWE LGGGSVRIHR ADVQSKVFDA LKISPEDARA KFGYLLDALQ YGAPPHGGLA
550 560 570 580 590
FGLDRLITLM TGADSIRDVI AFPKTQRAQD LLTQAPSPVD EKQLRELHIR LRNPLAATQG