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 A5FX11

Entry ID Method Resolution Chain Position Source
AF-A5FX11-F1 Predicted AlphaFoldDB

No variants for A5FX11

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A5FX11

No associated diseases with A5FX11

2 regional properties for A5FX11

Type Name Position InterPro Accession
domain NADH-quinone oxidoreductase, subunit D 136 - 406 IPR001135
conserved_site NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site 59 - 70 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
MSGGMQNGTQ ETERRVIDIN DRHTVNVGPQ HPATHGVLRL IMELEGETVT RADPHIGLLH
70 80 90 100 110 120
RGTEKLIEYK SYLQAVPYFD RLDYVSPMCC EHAFALATER LLGVKVPERA QWIRVLFAEI
130 140 150 160 170 180
TRILNHLLNA VHLALDIGAQ SPSLWGYEER EKLLTFHEAV SGARFHANYF RPGGVSKDMP
190 200 210 220 230 240
TGLAEQIWEW SEKFPKFLDD LQSLLNENRI FRQRLVDIGV ISAEDALAMG FSGPNLRASG
250 260 270 280 290 300
IAWDLRRAQP YDKYDEVDFD IPVGRHGDSF DRYLVRIREM AESLKIIRQA LKAMPEGPIK
310 320 330 340 350 360
VQDHKITPPK RAEMKRSMEA LIHHFKLYTE GYHVPAGTTY TAVEAPKGEF GVYLVADGSN
370 380 390 400
RPYRCKIRAT GFSHLQAMNL MSKGHLLADA IAVLGSIDIV FGEVDR