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 A1SVX3

Entry ID Method Resolution Chain Position Source
AF-A1SVX3-F1 Predicted AlphaFoldDB

No variants for A1SVX3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1SVX3

No associated diseases with A1SVX3

No regional properties for A1SVX3

Type Name Position InterPro Accession
No domain, repeats, and functional sites for A1SVX3

Functions

Description
EC Number
Subcellular Localization
  • Cell outer membrane ; Lipid-anchor
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cell outer membrane A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures.

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

2 GO annotations of biological process

Name Definition
Gram-negative-bacterium-type cell outer membrane assembly The assembly of an outer membrane of the type formed in Gram-negative bacteria. This membrane is enriched in polysaccharide and protein, and the outer leaflet of the membrane contains specific lipopolysaccharide structures.
protein insertion into membrane The process that results in the incorporation of a protein into a biological membrane. Incorporation in this context means having some part or covalently attached group that is inserted into the the hydrophobic region of one or both bilayers.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSKFYKSGRV TTAVIVALSL SACARFDART QANGDFDYVQ TPRGEHYQTA HFTQNEARDI
70 80 90 100 110 120
YDIPALTEQQ KRIGFLSSNV DIRPPTQLIP VIDGVVLEAN NSDKTTVLFN AFNHTENMKD
130 140 150 160 170 180
KVWTLLESYI AANNIEVAAK DSNLTQIETG MFRHQQAYGS FLFRTKVVRE SSYRFTLNQP
190 200 210 220 230 240
QGGQNAALTV EVLSYSEKND NVDLKVNLTA RSKKSIELRL VNDLLKYAYQ LKESSELQVA
250 260 270 280 290 300
NSQPLPIKLG YDDNNQMVWI VDADFIVSWT KLPDLLALLR FEQVDADKNL GYYLVKFKAP
310 320 330 340 350 360
NAKYWPENNL NSFELDNAEY FIQLGELNSG STSITWLDAD KKPLADEKVT EIYFSITSKI
370
RDVLLLNENQ SKAL