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 Q7W222

Entry ID Method Resolution Chain Position Source
AF-Q7W222-F1 Predicted AlphaFoldDB

No variants for Q7W222

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7W222

No associated diseases with Q7W222

3 regional properties for Q7W222

Type Name Position InterPro Accession
domain Elp3/MiaA/NifB-like, radical SAM core domain 96 - 305 IPR006638
domain Radical SAM 43 - 329 IPR007197
domain Lipoyl synthase, N-terminal 27 - 85 IPR031691

Functions

Description
EC Number 2.8.1.8 Sulfurtransferases
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.

3 GO annotations of molecular function

Name Definition
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
lipoate synthase activity Catalysis of the reaction: protein N6-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine = protein N6-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosyl.
metal ion binding Binding to a metal ion.

1 GO annotations of biological process

Name Definition
protein lipoylation The lipoylation of peptidyl-lysine to form peptidyl-N6-lipoyl-L-lysine.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSTLVESPVP SNDSQAAAPA AYDPTQKQKS QAKTARIPIK VVAAEKLKKP EWIRVRAAAP
70 80 90 100 110 120
GSRFYDIKRI LREHNLHTVC EEASCPNIGE CFGKGTATFM IMGDKCTRRC PFCDVGHGRP
130 140 150 160 170 180
DPLDTQEPEN LARTIAALKL SYVVITSVDR DDLRDGGAAH FVECIAKVRE YSPDTRIEVL
190 200 210 220 230 240
VPDFRGRLDR ALHILNSGPP DVMNHNLETV PRLYKQARPG SDYAHSLKLL VEFKKLHPEV
250 260 270 280 290 300
PTKSGLMLGL GETDEEILQV MRDMREHNVD MLTIGQYLQP SEHHLPVLRY VHPDTFAMFE
310 320 330
REAYAMGFTH AAVGAMVRSS YHADQQAHAA GVN