Q83BE5

PR
Gene name
aspS
Protein name
Aspartate--tRNA(Asp/Asn) ligase
Names
Aspartyl-tRNA synthetase, AspRS, Non-discriminating aspartyl-tRNA synthetase, ND-AspRS
Species
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
KEGG Pathway
cbu:CBU_1565
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)

537-590 (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 Q83BE5

Entry ID Method Resolution Chain Position Source
AF-Q83BE5-F1 Predicted AlphaFoldDB

No variants for Q83BE5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q83BE5

No associated diseases with Q83BE5

5 regional properties for Q83BE5

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 - 104 IPR004365
domain Aminoacyl-tRNA synthetase, class II 142 - 559 IPR006195
domain GAD domain 314 - 405 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
MRTHYADKVD SSLIDQTITL CGWVHRRRDH GGLIFIDLRD REGLVQVVCN PTESTVFKVA
70 80 90 100 110 120
ESLRNEYVIK VTGKVHKRPE GTVNPHIPSG EVEIAASDIT LLNKSKPLPF NIDEYQEVSE
130 140 150 160 170 180
EVRLKFRYLD LRRPEVAQRL KMRSYIIREI RRFLDERGFL DIETPMLTKS TPEGARDYLV
190 200 210 220 230 240
PSRTHPGQFF ALPQSPQIFK EILMVAGFDR YYQIVRCFRD EDLRADRQPE FTQLDLEMSF
250 260 270 280 290 300
VEEKDIQQLM ETMIRHLFST FLNVPLPDPF PRITYDEAIK TYGTDRPDLR NPLTLVDVTD
310 320 330 340 350 360
LMKSVEFKVF KEPANNPHGR IAVLRLPKGA ELSRKAIDDY TQFVGIYGAK GLAYIKVENI
370 380 390 400 410 420
DNGTGGLHSP ILKFLPENVI AEILKRTQAQ SGDILFFGAD KAKIVNESLG ALRDRLCADL
430 440 450 460 470 480
NLYEGQWKPV WVVDFPMFDR EDVGDWQALH HPFTALQETD PEKVIANPGD VLSRAYDMVL
490 500 510 520 530 540
NGSEIGGGSI RINDIGMQYA VLKVLGISKE MAEAQFGHLL MALQFGSPPL GGIAFGLDRL
550 560 570 580
VAIMTGASSI RDVIAFPKTQ TAQCPLTNAP AQVETLQLET LGLKVSKHRK