B9KME7

PR
Gene name
aspS
Protein name
Aspartate--tRNA(Asp/Asn) ligase
Names
Aspartyl-tRNA synthetase, AspRS, Non-discriminating aspartyl-tRNA synthetase, ND-AspRS
Species
Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter sphaeroides)
KEGG Pathway
rsk:RSKD131_2178
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)

143-215 (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 B9KME7

Entry ID Method Resolution Chain Position Source
AF-B9KME7-F1 Predicted AlphaFoldDB

No variants for B9KME7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B9KME7

No associated diseases with B9KME7

5 regional properties for B9KME7

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 21 - 103 IPR004365
domain Aminoacyl-tRNA synthetase, class II 144 - 559 IPR006195
domain GAD domain 314 - 407 IPR029351
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 5 - 138 IPR047089

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
MHAYRSHTCT ELNAAHVGQE VRLSGWVHRV RDHGGVLFLD LRDHYGITQV IADADSPAFA
70 80 90 100 110 120
ELETVRAEWV IRIEGRVKAR DASLVNPKLA TGEIEVYATG MSVLGAADEL PLPVFGETDY
130 140 150 160 170 180
PEETRLTYRF LDLRREKLHQ NMMLRSNVVR SLRNRMWGAG FNEFQTPIIT ASSPEGARDF
190 200 210 220 230 240
LVPSRLHPGK FYALPQAPQQ FKQLIMVAGF DRYFQIAPCF RDEDPRADRS PTDFYQLDIE
250 260 270 280 290 300
MSFVEQEDVF AAVQPVIQGL FEEFGHGKRV EADWPRIAYR DAMLWYGSDK PDLRNPIKMQ
310 320 330 340 350 360
VVSEHFAGSG FAIFAKLLEN EGTEIRAIPA PTGGSRKFCD RMNAFAQSQG LPGMGYIFWR
370 380 390 400 410 420
KGDDGAMEAA GPLAKNIGPE RTEAIRQQLG LGEGDAAFFL GGKPETFEAV AGRARTEIGR
430 440 450 460 470 480
ELGLTEENCF KFAWIVDFPM YEKDDEGKID FSHNPFSMPQ GGMEALEGDP LKVHAYQYDL
490 500 510 520 530 540
ACNGYELISG GIRNHKPEIM FKAFELAGYP KEEVEKRFGG MVKAFRYGAP PHGGCAAGID
550 560 570 580 590
RIVMLLADEA NIREVIMFPM NQRAEDLLMG APSEPTNEQL RELRLRVVPK D