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 Q2IEC3

Entry ID Method Resolution Chain Position Source
AF-Q2IEC3-F1 Predicted AlphaFoldDB

No variants for Q2IEC3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2IEC3

No associated diseases with Q2IEC3

5 regional properties for Q2IEC3

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 149 - 485 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 58 - 130 IPR004365
domain Aminoacyl-tRNA synthetase, class II 172 - 483 IPR006195
domain Lysyl-tRNA synthetase, class II, C-terminal 167 - 486 IPR018149
domain Lysine-tRNA ligase, class II, N-terminal 57 - 159 IPR044136

Functions

Description
EC Number 1.13.11.11 With incorporation of two atoms of oxygen
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

3 GO annotations of molecular function

Name Definition
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
metal ion binding Binding to a metal ion.
tryptophan 2,3-dioxygenase activity Catalysis of the reaction: L-tryptophan + O2 = N-formyl-L-kynurenine.

1 GO annotations of biological process

Name Definition
tryptophan catabolic process to kynurenine The chemical reactions and pathways resulting in the breakdown of tryptophan into other compounds, including kynurenine.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTDPSAHSAA LTYGSYLALD ELLAAQRPRS EEHDELLFIV VHQVYELWFK QVVHELTWLQ
70 80 90 100 110 120
ERLHRGEGGH ALATLKRVLT ILKTVVAQVD VIETMTPRQF TAFRSRLEAA SGFQSAQFRV
130 140 150 160 170 180
LEAMLGRRDD RMLAPYPPDG PGYARIAAAM AAPSLFDSLL RYLATQGFET PVVPEPRPAG
190 200 210 220 230 240
WRQPSEAVQR VLLEVYRADG EAALVCERFV DLDEGVQEWR YRHVKMVERT IGDKPGTGGS
250 260
AGARYLRSTL FTPAFPDLWA VRGAL