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

2 structures for Q92R45

Entry ID Method Resolution Chain Position Source
2Q62 X-ray 180 A A/B/C/D/E/F/G/H 1-241 PDB
AF-Q92R45-F1 Predicted AlphaFoldDB

No variants for Q92R45

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q92R45

No associated diseases with Q92R45

1 regional properties for Q92R45

Type Name Position InterPro Accession
domain NADPH-dependent FMN reductase-like 35 - 179 IPR005025

Functions

Description
EC Number
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

2 GO annotations of molecular function

Name Definition
FMN binding Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
FMN reductase (NADPH) activity Catalysis of the reaction: FMNH2 + NADP+ = FMN + NADPH + 2 H+.

2 GO annotations of biological process

Name Definition
protein homotetramerization The formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits.
response to metal ion Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a metal ion stimulus.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSDDDSSHDL PAANLQQLRL PDSASLRPAF STHRPRILIL YGSLRTVSYS RLLAEEARRL
70 80 90 100 110 120
LEFFGAEVKV FDPSGLPLPD AAPVSHPKVQ ELRELSIWSE GQVWVSPERH GAMTGIMKAQ
130 140 150 160 170 180
IDWIPLSTGS IRPTQGKTLA VMQVSGGSQS FNAVNQMRIL GRWMRMITIP NQSSVAKAFQ
190 200 210 220 230 240
EFDANGRMKP SSYYDRVVDV MEELVKFTLL TRDCSAYLTD RYSERKESAA ELEHRVTLKS
V