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 Q1AVI6

Entry ID Method Resolution Chain Position Source
AF-Q1AVI6-F1 Predicted AlphaFoldDB

No variants for Q1AVI6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q1AVI6

No associated diseases with Q1AVI6

2 regional properties for Q1AVI6

Type Name Position InterPro Accession
domain NADH-quinone oxidoreductase, subunit D 151 - 318 IPR001135-1
domain NADH-quinone oxidoreductase, subunit D 321 - 396 IPR001135-2

Functions

Description
EC Number
Subcellular Localization
  • Cell 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
MLREERRAAE EAITLIRPAT SRLVDPDIRD EFGLETLDMN MGPQHPAMHG LLRLILELDG
70 80 90 100 110 120
ETIVRCDPVM GYLHRCQEKI AENRTYPAVI PLTDRLDYFA NMHNEHGYCL AVEDLLGVEI
130 140 150 160 170 180
PPRAEYIRVL MCELMRIASH LPSIGFLLLE LGAFTPILYA FRERERIQNF FEAVTGARMM
190 200 210 220 230 240
FHYIRIGGVK ADLPPDIPEK IWEYVEGLEK RIKPDFIDLI EGNEIFIERT RGISRLTQEE
250 260 270 280 290 300
AIELGLTGPP LRCTGVAFDV RRDYPYSVYP ELDFEVVTDT AGDVEASYRV RIKEVYESIK
310 320 330 340 350 360
IIRQCLEKMP EGEVMGDVGR RVRPPEGEGF GRVEGPRGEF AVHVVSDGSD TPYRVHYRDP
370 380 390
SFVNMQLLQE KMPGHYLPDI MPIMGLVDPV SGGWDK