Q8Y270

PR
Gene name
aspS
Protein name
Aspartate--tRNA(Asp/Asn) ligase
Names
Aspartyl-tRNA synthetase, AspRS, Non-discriminating aspartyl-tRNA synthetase, ND-AspRS
Species
Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum)
KEGG Pathway
rso:RSc0466
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)

541-605 (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 Q8Y270

Entry ID Method Resolution Chain Position Source
AF-Q8Y270-F1 Predicted AlphaFoldDB

No variants for Q8Y270

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8Y270

No associated diseases with Q8Y270

6 regional properties for Q8Y270

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 121 - 554 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 19 - 103 IPR004365
domain Aminoacyl-tRNA synthetase, class II 144 - 552 IPR006195
domain GAD domain 313 - 398 IPR029351
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 3 - 134 IPR047089
domain Aspartate-tRNA ligase, type 1, core domain 141 - 556 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
MRTQYCGQVT EQLLGQSVTL SGWAHRRRDH GGVIFIDLRD REGLVQVVCD PDRPEMFKVA
70 80 90 100 110 120
EGVRNEFCLQ VKGIVRARPE GTTNPNLASG KIEVLCHELT VLNASVTPPF QLDDDNLSET
130 140 150 160 170 180
TRLTHRVLDL RRPQMQYNLR LRYKVAMEVR KYLDDKGFID IETPMLTKST PEGARDYLVP
190 200 210 220 230 240
SRVNAGQFFA LPQSPQLFKQ MLMVSGFDRY YQITKCFRDE DLRADRQPEF TQIDCETSFL
250 260 270 280 290 300
SEQEIRDLFE EMIRTVFQNT MSVALDAKFP VMEFREAMAR FGSDKPDLRV KLEFTELTDA
310 320 330 340 350 360
MKDVDFKVFS GPANAEGGRV VALRVPGGAA LSRGDIDAYT KFVEIYGAKG LAWIKVNEVA
370 380 390 400 410 420
KGRDGLQSPI VKNLHDAAIA EILKRSGAQD GDILFFGADR AKVVNDAMGA LRLKVGHSDF
430 440 450 460 470 480
AKSTGLFEDA WKPLWVVDFP MFEYDEEDAR WVAMHHPFTS PKDEHLEYLE TDPGKCIAKA
490 500 510 520 530 540
YDMVLNGWEI GGGSVRIYRE EVQSKVFRAL KIGDEEARAK FGFLLDALQY GAPPHGGIAF
550 560 570 580 590 600
GLDRVVTMMA GADSIRDVIA FPKTQRAQDL LTQAPSPVDE KQLRELHIRL RAAEAKVAAP
AAATA