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 A7N9U8

Entry ID Method Resolution Chain Position Source
AF-A7N9U8-F1 Predicted AlphaFoldDB

No variants for A7N9U8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A7N9U8

No associated diseases with A7N9U8

3 regional properties for A7N9U8

Type Name Position InterPro Accession
domain Ribosomal protein S4/S9, N-terminal 3 - 95 IPR001912
domain RNA-binding S4 domain 96 - 160 IPR002942
conserved_site Ribosomal protein S4, conserved site 94 - 118 IPR018079

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
small ribosomal subunit The smaller of the two subunits of a ribosome.

2 GO annotations of molecular function

Name Definition
rRNA binding Binding to a ribosomal RNA.
structural constituent of ribosome The action of a molecule that contributes to the structural integrity of the ribosome.

1 GO annotations of biological process

Name Definition
translation The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MARYLGPKCK LSRREGTDLF LKSGVKANDE KCKMNTAPGQ HGARRARLSD YGLQLREKQK
70 80 90 100 110 120
VRRMYGILEG QFKKYYVEAS RRKGNTGATL LELLESRLDN VVYRMGFAAT RAEARQLVVH
130 140 150 160 170 180
KGIMVNGHTC NVPSAQVKAG DVVAVREKAK KQLRIQNAVE LAKHRKELSW IDVNTDSLEG
190 200
TMKSSPDRSE LSADINEQLI IELYSK