Q88VQ8

PR
Gene name
aspS
Protein name
Aspartate--tRNA ligase
Names
Aspartyl-tRNA synthetase, AspRS
Species
Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (Lactobacillus plantarum)
KEGG Pathway
lpl:lp_1980
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)

531-598 (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 Q88VQ8

Entry ID Method Resolution Chain Position Source
AF-Q88VQ8-F1 Predicted AlphaFoldDB

No variants for Q88VQ8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q88VQ8

No associated diseases with Q88VQ8

6 regional properties for Q88VQ8

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 122 - 561 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 19 - 103 IPR004365
domain Aminoacyl-tRNA synthetase, class II 141 - 559 IPR006195
domain GAD domain 312 - 407 IPR029351
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 3 - 138 IPR047089
domain Aspartate-tRNA ligase, type 1, core domain 142 - 563 IPR047090

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
MKRTTYAGLI NEDYLGQTVT LQGWVQKRRD LGSLIFIDLR DREGIVQLVF SQEFSADALA
70 80 90 100 110 120
VADQLRGEYV IEVQGTVVNR NADAVNDRMK TGKVEVEIHD AKILNKAKTP PFYIQDDINV
130 140 150 160 170 180
SDELRLKYRY LDLRRPEMQR GLKIRNGITQ AVHSYFDANG FYDIETPFLT KSTPEGARDY
190 200 210 220 230 240
LVPSRVYQGH FYALPQSPQL FKQLLMGAGF DRYYQIARCF RDEDLRGDRQ PEFTQIDMET
250 260 270 280 290 300
SFLTAEEIQS YTEGLIKQVM KDVKGVDIKT PFTRMTWQEA MDRFGSEKPD VRFGMELKDM
310 320 330 340 350 360
GVAVSNAGFK VFDNALANGG LVKAIAVPGG ADQYSRKQID AYTEYVKRFG AKGLAWMKVT
370 380 390 400 410 420
DDGFSGPVAK FFKNDGDFEA ITSAAAAKPG DLLLFAADSF KVVSDTLGYL RTAIAKELDL
430 440 450 460 470 480
IDQDQYAYLW VVDWPLFEYD EGIERWVPAH HPFTMPNEED VHYLNDGEDP HKAHAQSYDI
490 500 510 520 530 540
ILNGYELGGG SIRIHTRELQ EKMFKALDFT KERAQEQFGF LLDALDMGFP PHGGLAIGLD
550 560 570 580 590
RFAMLLSGND NIREVIAFPK NSKASEPMTN APSRVSDQQL ADLDLNITNP VTDDEPTE