Q3AS30

PR
Gene name
aspS
Protein name
Aspartate--tRNA(Asp/Asn) ligase
Names
Aspartyl-tRNA synthetase, AspRS, Non-discriminating aspartyl-tRNA synthetase, ND-AspRS
Species
Chlorobium chlorochromatii (strain CaD3)
KEGG Pathway
cch:Cag_0932
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)

152-223 (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 Q3AS30

Entry ID Method Resolution Chain Position Source
AF-Q3AS30-F1 Predicted AlphaFoldDB

No variants for Q3AS30

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q3AS30

No associated diseases with Q3AS30

6 regional properties for Q3AS30

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 132 - 569 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 31 - 110 IPR004365
domain Aminoacyl-tRNA synthetase, class II 156 - 567 IPR006195
domain GAD domain 332 - 418 IPR029351
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 15 - 149 IPR047089
domain Aspartate-tRNA ligase, type 1, core domain 153 - 571 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
MSNPVEQQVV CNRFRSHSCG LLNATFEQQH VRLAGWVHRK RDHGGLIFID LRDHTGICQL
70 80 90 100 110 120
VIQPEQQALF AEAEHLHNES VISVEGTVIL RAENAINPRL SSGEIEVVIS CMSIESNAHP
130 140 150 160 170 180
LPFSVADELP TSEELRLKYR FLDLRREKLH ENIIFRSRLT AAVRRYLEEK NFTEIQTPIL
190 200 210 220 230 240
TSSSPEGARD FLVPSRLHPG KFYALPQAPQ QFKQLLMVAG FPRYFQIAPC FRDEDARADR
250 260 270 280 290 300
SPGEFYQLDM EMAFIEQENL FEILEGMLEH ITSTMSKKRI TQVPFPRISY RDVMNRFGTD
310 320 330 340 350 360
KPDLRIPLEI QDVTSLFVDS GFKVFAKNTV PGCCVKALVV KGRGNESRLF YDKAEKRAKE
370 380 390 400 410 420
LGSAGLAYIQ FKDEGAKGPL VKFLSEDDMN ALKQHLNLEQ GDVVFFGAGK WEVTCKIMGG
430 440 450 460 470 480
MRNYFADLFT LDKDELSFCW IVDFPMYEYN EEAKKIDFSH NPFSMPQGEM EALETKDALD
490 500 510 520 530 540
ILAYQYDIVC NGIELSSGAI RNHKPEIMYK AFAIAGYSRE EVDQRFGHMI EAFKLGAPPH
550 560 570 580 590 600
GGIAPGLDRL VMILCDEQNI REVIAFPMNQ QAQDLMMSAP SEVTLAQLRE LHLKVELPKK
EEKKG