Q3B3A1

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 luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon luteolum)
KEGG Pathway
plt:Plut_1320
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)

150-227 (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 Q3B3A1

Entry ID Method Resolution Chain Position Source
AF-Q3B3A1-F1 Predicted AlphaFoldDB

No variants for Q3B3A1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q3B3A1

No associated diseases with Q3B3A1

6 regional properties for Q3B3A1

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 133 - 570 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 32 - 111 IPR004365
domain Aminoacyl-tRNA synthetase, class II 157 - 581 IPR006195
domain GAD domain 326 - 419 IPR029351
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 16 - 149 IPR047089
domain Aspartate-tRNA ligase, type 1, core domain 154 - 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
MTKEAGELNA LKNRFRTDYC GQLGLDGEGR EVRLGGWVHR IRDHGGLVFI DLRDHTGICQ
70 80 90 100 110 120
LVVQPEREEL FELAGRLHAE SVITIEGRVV ARSSETINPR LASGSIEVVV SAIGVESHAR
130 140 150 160 170 180
PLPFPVADEV QTSEELRLKY RFIDLRREKI HENIIFRSRI SAAIRRYLEE RDFIEIQTPI
190 200 210 220 230 240
LTSSSPEGAR DFLVPSRLHP GKFYALPQAP QQFKQLLMVA GFPRYFQIAP CFRDEDARAD
250 260 270 280 290 300
RSPGEFYQLD MEMAFIEQDD LFEILEGMFR HLTDTMSKKR ITRFPFPRIS YREVMDSYGT
310 320 330 340 350 360
DKPDLRIPLK IEDVTPMFTD SGFKVFASNT KPGCAVKALV LKGRGTESRL FYDKAEKRAR
370 380 390 400 410 420
ELGSAGLAYI QFREEGPKGP IVKFMTEPEL QAMKDQLTLE TGDVVFFAAG KWEAACKIMG
430 440 450 460 470 480
GMRTYFGDLF TLDPDELSFC WIVDFPMFEY NEDAKKVDFS HNPFSMPQGE MEALETMDPL
490 500 510 520 530 540
DVLAYQYDIV CNGIELSSGA IRNHKPEIMY KAFEIAGYSR EEVDLRFGHM IEAFKLGAPP
550 560 570 580 590 600
HGGIAPGLDR LVMILRDEQN IREVIAFPMN QQAQDLMMAA PSEVTGAQLR ELHIRLDLPE
EEKK