A7Z750

PR
Gene name
aspS
Protein name
Aspartate--tRNA(Asp/Asn) ligase
Names
Aspartyl-tRNA synthetase, AspRS, Non-discriminating aspartyl-tRNA synthetase, ND-AspRS
Species
Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42) (Bacillus amyloliquefaciens subsp. plantarum)
KEGG Pathway
bay:RBAM_024660
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)

538-592 (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 A7Z750

Entry ID Method Resolution Chain Position Source
AF-A7Z750-F1 Predicted AlphaFoldDB

No variants for A7Z750

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A7Z750

No associated diseases with A7Z750

6 regional properties for A7Z750

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 123 - 560 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 20 - 105 IPR004365
domain Aminoacyl-tRNA synthetase, class II 144 - 558 IPR006195
domain GAD domain 314 - 408 IPR029351
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 4 - 140 IPR047089
domain Aspartate-tRNA ligase, type 1, core domain 144 - 562 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
MFGRTYYCGE ITEKAIGETV KLKGWVQKRR DLGGLIFIDL RDRSGIVQVV FNPDVSKEAL
70 80 90 100 110 120
AAAEAIRNEY VLDIEGTVSA REEGTVNPNL KTGKIEIKAE AVTVLSTAKT PPFPISDQAA
130 140 150 160 170 180
DVSEDVRLKH RYLDLRRPAM FQTLQMRHQV TKSIRHFLDE NGFLDIETPI LTKSSPEGAR
190 200 210 220 230 240
DYLVPSRVHE GEFYALPQSP QIFKQLLMVS GFERYYQVAR CFRDEDLRAD RQPEFTQIDI
250 260 270 280 290 300
EMSFMSQEDI MALAEEMMAK VMLETKGVEV PLPLPRMTYE EAMNSYGSDK PDTRFGMLLT
310 320 330 340 350 360
DVSDIVKDTE FKVFSSAVAN GGVVKAINVK GAAGDYSRKD IDALGVFAGN YGAKGLAWVK
370 380 390 400 410 420
VEADGVKGPI AKFFDEEKQA KLAEALEASE GDLLLFGADK FEVVAQSLGA LRLKLGKERG
430 440 450 460 470 480
LIDESLFNFL WVVDWPLLEH DEEEGRFYAA HHPFTMPVRE DLDLIETAPE DMKAQAYDLV
490 500 510 520 530 540
LNGYELGGGS IRIFEKDVQE KMFGLLGFTK EEAEEEFGYL LEAFEYGAPP HGGIALGLDR
550 560 570 580 590
LVMLLAGRTN LRDTIAFPKT ASASCLLTEA PGEVSDAQLE ELHLSVKRKV KQ