Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P04803

Entry ID Method Resolution Chain Position Source
AF-P04803-F1 Predicted AlphaFoldDB

2 variants for P04803

Variant ID(s) Position Change Description Diseaes Association Provenance
s04-1004076 26 L>R No SGRP
s04-1004476 159 D>E No SGRP

No associated diseases with P04803

1 regional properties for P04803

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 43 - 52 IPR001412

Functions

Description
EC Number 6.1.1.2 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.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
tryptophan-tRNA ligase activity Catalysis of the reaction: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophanyl-tRNA(Trp).

2 GO annotations of biological process

Name Definition
mitochondrial tryptophanyl-tRNA aminoacylation The process of coupling tryptophan to tryptophanyl-tRNA in a mitochondrion, catalyzed by tryptophanyl-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.
tryptophanyl-tRNA aminoacylation The process of coupling tryptophan to tryptophanyl-tRNA, catalyzed by tryptophanyl-tRNA synthetase. The tryptophanyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a tryptophan-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSNKQAVLKL ISKRWISTVQ RADFKLNSEA LHSNATVFSM IQPTGCFHLG NYLGATRVWT
70 80 90 100 110 120
DLCELKQPGQ ELIFGVADLH AITVPKPDGE MFRKFRHEAV ASILAVGVDP EKASVIYQSA
130 140 150 160 170 180
IPQHSELHWL LSTLASMGLL NRMTQWKSKS NIKQSTNGDY LVNDSDVGKV RLGLFSYPVL
190 200 210 220 230 240
QAADILLYKS THVPVGDDQS QHLELTRHLA EKFNKMYKKN FFPKPVTMLA QTKKVLSLST
250 260 270 280 290 300
PEKKMSKSDP NHDSVIFLND EPKAIQKKIR KALTDSISDR FYYDPVERPG VSNLINIVSG
310 320 330 340 350 360
IQRKSIEDVV EDVSRFNNYR DFKDYVSEVI IEELKGPRTE FEKYINEPTY LHSVVESGMR
370
KAREKAAKNL ADIHKIMGF