Q3JVY8

PR
Gene name
aspS
Protein name
Aspartate--tRNA(Asp/Asn) ligase
Names
Aspartyl-tRNA synthetase, AspRS, Non-discriminating aspartyl-tRNA synthetase, ND-AspRS
Species
Burkholderia pseudomallei (strain 1710b)
KEGG Pathway
bpm:BURPS1710b_0852
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)

84-155 (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 Q3JVY8

Entry ID Method Resolution Chain Position Source
AF-Q3JVY8-F1 Predicted AlphaFoldDB

No variants for Q3JVY8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q3JVY8

No associated diseases with Q3JVY8

5 regional properties for Q3JVY8

Type Name Position InterPro Accession
active_site Thiolase, active site 374 - 387 IPR020610
conserved_site Thiolase, conserved site 339 - 355 IPR020613
active_site Thiolase, acyl-enzyme intermediate active site 84 - 102 IPR020615
domain Thiolase, N-terminal 4 - 262 IPR020616
domain Thiolase, C-terminal 271 - 390 IPR020617

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
MRTEYCGLVT EHLLGQTVSL CGWVHRRRDH GGVIFIDLRD REGLVQVVCD PDRAEMFAAA
70 80 90 100 110 120
EGVRNEFCIQ VKGLVRGRPE GTINAGLKSG RIEVLCHELN VLNASVTPPF QLDDDNLSET
130 140 150 160 170 180
TRLTHRVLDL RRPQMQHNLR LRYRVAIEAR KYLDEQGFID IETPMLTKST PEGARDYLVP
190 200 210 220 230 240
SRVNAGQFFA LPQSPQLFKQ LLMVANFDRY YQITKCFRDE DLRADRQPEF TQIDCETSFL
250 260 270 280 290 300
GEQEIRDLFE DMIRHIFKTT IGVELDATFP VMPYSEAMAR FGSDKPDLRV KLEFTELTDA
310 320 330 340 350 360
MKDVDFKVFS TPANTKDGRV AALRVPKGGE LTRGDIDGYT EFVRIYGAKG LAWIKVNERA
370 380 390 400 410 420
KGRDGLQSPI VKNLHDASIA AILERTGAQD GDIIFFAADR AKVVNDSLGA LRLKIGHSEF
430 440 450 460 470 480
GKANGLVEAG WKPLWVVDFP MFEYDDEEAR YVAAHHPFTS PKDEHLEYLE TDPGRCLAKA
490 500 510 520 530 540
YDMVLNGWEI GGGSVRIHRE EVQSKVFRAL KIGPEEAQAK FGFLLDALQY GAPPHGGIAF
550 560 570 580 590
GLDRIVTMMA GADSIRDVIA FPKTQRAQCL LTQAPSPVDE RQLRELHIRL RQPEQPKA