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 Q2S5J0

Entry ID Method Resolution Chain Position Source
AF-Q2S5J0-F1 Predicted AlphaFoldDB

No variants for Q2S5J0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2S5J0

No associated diseases with Q2S5J0

2 regional properties for Q2S5J0

Type Name Position InterPro Accession
domain NADH-quinone oxidoreductase, subunit D 180 - 451 IPR001135
conserved_site NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site 103 - 114 IPR014029

Functions

Description
EC Number
Subcellular Localization
  • Cell inner membrane ; Peripheral membrane protein ; Cytoplasmic side
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

3 GO annotations of molecular function

Name Definition
NAD binding Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
NADH dehydrogenase (quinone) activity Catalysis of the reaction: NADH + H+ + a quinone = NAD+ + a quinol.
quinone binding Binding to a quinone, any member of a class of diketones derivable from aromatic compounds by conversion of two CH groups into CO groups with any necessary rearrangement of double bonds.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPQTQKPDFP GNDLGDQFRF WPKHNEKIYE RLENKHAWLE EKRAAAQGDG KPPATQRSEV
70 80 90 100 110 120
DPLENEMILN IGPQHPATHG VLRCVVKMDG ETIEKSVLDI GYLHRGIEKL AEHKTYQEFM
130 140 150 160 170 180
PYTDRMDYLS PYSNNVAWCL AVEKLADIEV PERAQWIRMI MSELARISSH CLWLGVGMMD
190 200 210 220 230 240
AGAVSGFVWT FQEREEIYSI MDEVAGARFT VSHSRIGGVA NDFSPRAIEM IRDFVDTFPD
250 260 270 280 290 300
RIAGWEGLLN KNRIWVERNK GVGRVTKEEA LELGLTGPNL RGSGVPYDVR RFEPYLKYDE
310 320 330 340 350 360
VDFTIPVREE GDCLARYFLR LDEMKQSVRI IEQCLDRMTE GPIRSDDAKE AYPSKEEVYY
370 380 390 400 410 420
SMEGMIHDFM YTDVGTVPPK GAHSYHAIEG PKGELGFYLT SDGTGRPWRV RINAPSFTNL
430 440 450
QAMEHMLEGE MVADTVVIIG SLDPVMGEAD K