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 A1B495

Entry ID Method Resolution Chain Position Source
AF-A1B495-F1 Predicted AlphaFoldDB

No variants for A1B495

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1B495

No associated diseases with A1B495

2 regional properties for A1B495

Type Name Position InterPro Accession
domain NADH-quinone oxidoreductase, subunit D 140 - 412 IPR001135
conserved_site NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site 63 - 74 IPR014029

Functions

Description
EC Number
Subcellular Localization
  • Cell inner membrane ; Peripheral membrane protein
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
MDGDIRKNSY DDGSMDALTG EQSIRNFNIN FGPQHPAAHG VLRMVLELDG EIVERADPHI
70 80 90 100 110 120
GLLHRGTEKL MESRTYLQNL PYLDRLDYVA PMNQEHAWCL AIERLTGTVI PRRASLIRVL
130 140 150 160 170 180
YSEIGRILNH LMGVTTGAMD VGALTPPLWG FEAREELMIF YERACGARLH AAYFRPGGVH
190 200 210 220 230 240
QDLPPDLLDD IEEWCERFPK LVDDLDTLLT ENRIFKQRLV DIGIVTEADA LDWGYTGVMV
250 260 270 280 290 300
RGSGLAWDLR RSQPYECYDE FDFQIPVGRN GDCYDRYLCR MAEMRESCKI MQQAVQKLRA
310 320 330 340 350 360
EPAGDVLARG KLTPPRRAEM KRDMESLIHH FKLYTEGFKV PAGEVYAAVE APKGEFGVYL
370 380 390 400 410
VADGTNKPWR AKLRAPGFAH LQSIDWMSRG HMLADVPAII ATLDIVFGEV DR