Q9PHM7

PR
Gene name
aspS
Protein name
Aspartate--tRNA(Asp/Asn) ligase
Names
Aspartyl-tRNA synthetase, AspRS, Non-discriminating aspartyl-tRNA synthetase, ND-AspRS
Species
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
KEGG Pathway
cje:Cj0640c
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)

413-492 (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 Q9PHM7

Entry ID Method Resolution Chain Position Source
AF-Q9PHM7-F1 Predicted AlphaFoldDB

No variants for Q9PHM7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9PHM7

No associated diseases with Q9PHM7

6 regional properties for Q9PHM7

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 119 - 553 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 18 - 102 IPR004365
domain Aminoacyl-tRNA synthetase, class II 149 - 550 IPR006195
domain GAD domain 313 - 405 IPR029351
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 2 - 136 IPR047089
domain Aspartate-tRNA ligase, type 1, core domain 142 - 554 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
MRSHYNTDLG ISHVGQSVKL CGWVNSYRDH GGVIFIDLRD RSGIIQLVCD PNDSKEAHEI
70 80 90 100 110 120
ASNARNEFVL ITEGTIRPRG EGLVNPKLKT GEIEVVVSKL TIENESAVPP FAIADESVNE
130 140 150 160 170 180
ELRLKYRFLD LRNPKLYENF ALRSKACIAA RNSLANMGFL EVETPILTKA TPEGARDYLV
190 200 210 220 230 240
PSRVHQGEFY ALPQSPQLFK QLLMCSGFDR YFQIAKCFRD EDLRADRQPE FTQIDVEMSF
250 260 270 280 290 300
CEQKDVIKVA ETFLKDIFKA CGKEIQTPFR QMQYKDAMEN YGSDKPDLRF DLKFIDVIDI
310 320 330 340 350 360
FTKSNNEIFA NIAKDTKKNR IKAIRVPKGD TIFSKRQMQR FEEFVRKFGA QGLAFIQVKK
370 380 390 400 410 420
DGLKGPLCKF FSEEDLNELS KRCELEVGDV VFFGAGAKKT VLDYMGRFRI FLANELKLID
430 440 450 460 470 480
PNALEFLWVV DFPMFEQNDD GSYSAMHHPF TMPKNIDETD LEEISSIAYD VVLNGVELGG
490 500 510 520 530 540
GSIRIHKNDI QQKVFKLLNI DEEQQKEKFG FLLDALSFGA PPHGGIAIGL DRLIMLVTGA
550 560 570 580
NSIREVIAFP KTQRAQCLMT DAPSPASNEA MRELGIKLRE NIK