A6QPU5

PR
Gene name
DARS2
Protein name
Aspartate--tRNA ligase, mitochondrial
Names
Aspartyl-tRNA synthetase, AspRS
Species
Bos taurus (Bovine)
KEGG Pathway
bta:538772
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)

1-75 (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 A6QPU5

Entry ID Method Resolution Chain Position Source
AF-A6QPU5-F1 Predicted AlphaFoldDB

No variants for A6QPU5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A6QPU5

No associated diseases with A6QPU5

6 regional properties for A6QPU5

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 164 - 603 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 63 - 146 IPR004365
domain Aminoacyl-tRNA synthetase, class II 184 - 602 IPR006195
domain GAD domain 354 - 449 IPR029351
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 47 - 180 IPR047089
domain Aspartate-tRNA ligase, type 1, core domain 184 - 606 IPR047090

Functions

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

3 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.
organelle membrane A membrane that is one of the two lipid bilayers of an organelle envelope or the outermost membrane of single membrane bound organelle.

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.

2 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.
mitochondrial asparaginyl-tRNA aminoacylation The process of coupling asparagine to asparaginyl-tRNA in a mitochondrion, catalyzed by asparaginyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P21889 aspS Aspartate--tRNA ligase Escherichia coli (strain K12) PR
Q8BIP0 Dars2 Aspartate--tRNA ligase, mitochondrial Mus musculus (Mouse) PR
10 20 30 40 50 60
MFCWLSRLCG ELSTPTRRTT QLIWSSAARS MVLSSQRIPE LSSFVARTNT CGELRSSHLG
70 80 90 100 110 120
QEVTLCGWIQ FRRQNIFLVL RDFHGLVQVV IPQDESAASV KKILCEAPME SVVQVSGTVI
130 140 150 160 170 180
SRPPGQKNPK MPTGEIEIKV KTAKLLNSCK KLPFEIKDFM KKTETLRLQY RYLDLRSVQM
190 200 210 220 230 240
QYNLRLRSQM VMKMREYLCN LHGFVDVETP TLFKRTPGGA KEFVIPSREP GKFYSLPQSP
250 260 270 280 290 300
QQFKQLLMVG GLDRYFQVAR CYRDEGSRPD RQPEFTQIDI EMSFVDQTGV QSLIEGLLQY
310 320 330 340 350 360
SWPSDKDPLV VPFPSMPFAE ALASYGTDKP DTRFGMKIVD ISDMFRNTEV GFLQDALSKP
370 380 390 400 410 420
QGTVKAICIR KGAKYLKRKD IESIRKFAAD HFNEEVLPIF LKTNENWNSP VAKFIMEEQG
430 440 450 460 470 480
LGLVKLLETQ EEDVVLLTAG EHKKACSLMG KLRLECADLL EARGVVLRDP ALFSFLWVVD
490 500 510 520 530 540
FPLFLPKEEN PQELESAHHP FTAPHPSDIH LLYTEPHKVR SQHYDLVLNG NEIGGGSIRI
550 560 570 580 590 600
HNSELQHCVL DTVLKEDVKL LSHLLQALDY GAPPHGGIAL GLDRLMCLVT GAPSIRDVIA
610 620 630 640 650
FPKSFRGHDL MSNAPDSIPP EELKPYHIQV SWPMDAETEK SSSNHPCRSE S