Q55C99

PR
Gene name
maspS (DDB_G0270152)
Protein name
Aspartate--tRNA ligase, mitochondrial
Names
Aspartyl-tRNA synthetase, AspRS
Species
Dictyostelium discoideum (Slime mold)
KEGG Pathway
ddi:DDB_G0270152
EC number
6.1.1.12: 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)

1-89 (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 Q55C99

Entry ID Method Resolution Chain Position Source
AF-Q55C99-F1 Predicted AlphaFoldDB

No variants for Q55C99

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q55C99

No associated diseases with Q55C99

5 regional properties for Q55C99

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 210 - 665 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 92 - 192 IPR004365
domain Aminoacyl-tRNA synthetase, class II 231 - 663 IPR006195
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 76 - 227 IPR047089
domain Aspartate-tRNA ligase, type 1, core domain 231 - 666 IPR047090

Functions

Description
EC Number 6.1.1.12 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

3 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).
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
MNRVILKDSK IFLNVLNKPI IKNKNCLSLL NITTSSTTSI IKNQQINQFN KRNFTNTINN
70 80 90 100 110 120
NKNENINNKI LNIIERSHSC GEITSKDIGK EVIIYGWINS LRNLGDNVFL VIRDGHGKVQ
130 140 150 160 170 180
CYVDLKQQCI LKSSVPNIDI NERNSIEENI KLFKLESIVS IKGKVIARPE RMVNKNMSTG
190 200 210 220 230 240
EIEISVDQLQ LLNNCVDLPF TVEHDSTAVS EELRLKYRYV DLRRDKVQSN IRLRSKVAMA
250 260 270 280 290 300
ARNYLINQQF IEVETPTLFR PTPEGAREYL VPTRHQGQFY SLPQSPQQYK QLLMVGGIDR
310 320 330 340 350 360
YFQLARCYRD EDLRSDRQPE FTQIDMELSF VNTQMIYRII EGLVKTLWKE AGFNIDYEFP
370 380 390 400 410 420
FYTYEQVLST YGIDKPDTRY DMKLVDITDC FNKDETNINL FKNALSQASN NFKESKPVIK
430 440 450 460 470 480
CIKLDQVLPT LKSKHLDQIT TESNSIITVQ IKSNNEWKSL ISKSISEQEK TLITERMNLK
490 500 510 520 530 540
EGDVLLISVG PRFQVESTLG KTRIYCANLL KELNLLKLDP QQFNFLWVVD FPLFTPSDYM
550 560 570 580 590 600
NEQSALLSTH HPFTAPHPED IDLLLNPLST PSDYSKIRGQ HYDIVINGVE LGGGSIRIHN
610 620 630 640 650 660
SDVQLRVLEK VLKLEPHMVQ RFNHLLTALS MGCPPHGGIA LGFDRLCSLL VNSNSIRDVI
670 680 690
AFPKTSGGKE LMTSSPATVT KSELDELFLI QK