Q2JMA8

PR
Gene name
aspS
Protein name
Aspartate--tRNA(Asp/Asn) ligase
Names
Aspartyl-tRNA synthetase, AspRS, Non-discriminating aspartyl-tRNA synthetase, ND-AspRS
Species
Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime)
KEGG Pathway
cyb:CYB_1161
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)

545-601 (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 Q2JMA8

Entry ID Method Resolution Chain Position Source
AF-Q2JMA8-F1 Predicted AlphaFoldDB

No variants for Q2JMA8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2JMA8

No associated diseases with Q2JMA8

6 regional properties for Q2JMA8

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 132 - 571 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 26 - 111 IPR004365
domain Aminoacyl-tRNA synthetase, class II 152 - 568 IPR006195
domain GAD domain 323 - 422 IPR029351
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 10 - 148 IPR047089
domain Aspartate-tRNA ligase, type 1, core domain 152 - 572 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
MPAAIHRPAR TLYCGEVRPA HIGQTVTLYG WIDRRRDHGG VIFLDLRDRS GIVQLVADPQ
70 80 90 100 110 120
KTPQSYPLAG EVRNEYVVRV TGTVQQRPPD SFNPRLATGE VEIYAEQLEV LSPVGKQLPF
130 140 150 160 170 180
SVSGEEAEEV REEIRLRYRY LDLRRERMSR NLQLRHRVIQ AIRRFLEDEE GFVEVETPIL
190 200 210 220 230 240
TRSTPEGARD YLVPSRVNPG EWFALPQSPQ LFKQLLMVAG VDRYYQIARC FRDEDLRADR
250 260 270 280 290 300
QPEFTQLDME MSFMDQEGIL ELNERLICHI FKTVKGIHLP RPFPRLTYAE AMARYGSDKP
310 320 330 340 350 360
DTRFGMELVD VSEVFQGSRF KVFAKVLAEG GLIKILPVPG GDEKISNTRI KPGGDLFKLV
370 380 390 400 410 420
TQYGAGGLAF IRVRPDSLDT IGALKESLSP EQEKRLLDLT QAKPGDLLLF GAGPAAVVNE
430 440 450 460 470 480
SLGRLRLHLG QELGLIPENA LNLLWITDFP MFEFNAEENR LEALHHPFTA PHPDDLADLK
490 500 510 520 530 540
TARAQAYDLV WNGVEVGGGS LRIYQREIQE QVFQAIGLTP EQARDKFGFL LEAFEYGTPP
550 560 570 580 590 600
HGGIAYGLDR LVMLLAGEDS IRDVIAFPKT QQARCLLTGA PSSVEAKQLK ELHVASTYQP
G