Q5WHP3

PR
Gene name
aspS
Protein name
Aspartate--tRNA ligase
Names
Aspartyl-tRNA synthetase, AspRS
Species
Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii)
KEGG Pathway
bcl:ABC1577
EC number
6.1.1.12: 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)

1-43 (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 Q5WHP3

Entry ID Method Resolution Chain Position Source
AF-Q5WHP3-F1 Predicted AlphaFoldDB

No variants for Q5WHP3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5WHP3

No associated diseases with Q5WHP3

5 regional properties for Q5WHP3

Type Name Position InterPro Accession
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain 152 - 375 IPR000194
domain ATP synthase, alpha subunit, C-terminal 382 - 511 IPR000793
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain 29 - 95 IPR004100
active_site ATPase, alpha/beta subunit, nucleotide-binding domain, active site 366 - 375 IPR020003
domain ATP synthase, F1 complex, alpha subunit nucleotide-binding domain 97 - 378 IPR033732

Functions

Description
EC Number 6.1.1.12 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.

3 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).
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
MKRTHHCGQL DKTLAGQQVQ LKGWVQRRRD LGQVIFLDLR DRSGIVQVVC SPEVSEEALK
70 80 90 100 110 120
AADRVRNEYL VAVSGIVVER NEQAVNDKLA TGAIEVHVRE LEILNVSKSL PFQIEADTDA
130 140 150 160 170 180
AEDVRLKYRY LDLRRPDMQE AFAMRHKIMK SVRDFLDADG YLEIETPMLT KSTPEGARDY
190 200 210 220 230 240
LVPSRVHHGQ FYALPQSPQI FKQLLMVSGF EKYFQIVRCF RDEDLRADRQ PEFTQIDIET
250 260 270 280 290 300
SFLDTEDILA MTEAMMEKLL KETHGLELKR PFSRMTYEEA MNRYGSDKPD TRFGMELIEL
310 320 330 340 350 360
SDVLKDTEFK VFKGALEAGG IIKGLTLKGG ADKLSRKDID ALADFVKPYG AKGLAWLKVD
370 380 390 400 410 420
DEGIKGPIAK FFNEAQTAAL LAAMDAEAGD LLFFGADKKQ VVFHALGALR LKFGKEFQLI
430 440 450 460 470 480
DENAFHFLWV TDFPLVEYDE QAKRFVALHH PFTRPKAEDL DLMETHPEQV RAEAYDLVLN
490 500 510 520 530 540
GFELGGGSQR IYERELQEKM FKLLGFSSEA AKEEFGFLLE AFDYGTPPHG GIALGLDRIV
550 560 570 580
MLLARKSNLR EVIAFPKTAS ASDLLTEAPN KVSVEQLIDL NLSIISKRS