P21889

PR
Gene name
aspS
Protein name
Aspartate--tRNA ligase
Names
Aspartyl-tRNA synthetase, AspRS
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b1866
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)

533-590 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

4 structures for P21889

Entry ID Method Resolution Chain Position Source
1C0A X-ray 240 A A 1-585 PDB
1EQR X-ray 270 A A/B/C 1-590 PDB
1IL2 X-ray 260 A A/B 1-590 PDB
AF-P21889-F1 Predicted AlphaFoldDB

No variants for P21889

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P21889

No associated diseases with P21889

6 regional properties for P21889

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 118 - 558 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 18 - 102 IPR004365
domain Aminoacyl-tRNA synthetase, class II 138 - 555 IPR006195
domain GAD domain 307 - 406 IPR029351
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 2 - 134 IPR047089
domain Aspartate-tRNA ligase, type 1, core domain 138 - 558 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
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

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.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
A6QPU5 DARS2 Aspartate--tRNA ligase, mitochondrial Bos taurus (Bovine) PR
Q8BIP0 Dars2 Aspartate--tRNA ligase, mitochondrial Mus musculus (Mouse) PR
10 20 30 40 50 60
MRTEYCGQLR LSHVGQQVTL CGWVNRRRDL GSLIFIDMRD REGIVQVFFD PDRADALKLA
70 80 90 100 110 120
SELRNEFCIQ VTGTVRARDE KNINRDMATG EIEVLASSLT IINRADVLPL DSNHVNTEEA
130 140 150 160 170 180
RLKYRYLDLR RPEMAQRLKT RAKITSLVRR FMDDHGFLDI ETPMLTKATP EGARDYLVPS
190 200 210 220 230 240
RVHKGKFYAL PQSPQLFKQL LMMSGFDRYY QIVKCFRDED LRADRQPEFT QIDVETSFMT
250 260 270 280 290 300
APQVREVMEA LVRHLWLEVK GVDLGDFPVM TFAEAERRYG SDKPDLRNPM ELTDVADLLK
310 320 330 340 350 360
SVEFAVFAGP ANDPKGRVAA LRVPGGASLT RKQIDEYGNF VKIYGAKGLA YIKVNERAKG
370 380 390 400 410 420
LEGINSPVAK FLNAEIIEDI LDRTAAQDGD MIFFGADNKK IVADAMGALR LKVGKDLGLT
430 440 450 460 470 480
DESKWAPLWV IDFPMFEDDG EGGLTAMHHP FTSPKDMTAA ELKAAPENAV ANAYDMVING
490 500 510 520 530 540
YEVGGGSVRI HNGDMQQTVF GILGINEEEQ REKFGFLLDA LKYGTPPHAG LAFGLDRLTM
550 560 570 580
LLTGTDNIRD VIAFPKTTAA ACLMTEAPSF ANPTALAELS IQVVKKAENN