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

3 structures for Q9FNG3

Entry ID Method Resolution Chain Position Source
1VK0 X-ray 210 A A/B/C/D/E/F 2-206 PDB
2Q3S X-ray 210 A A/B/C/D/E/F 2-206 PDB
AF-Q9FNG3-F1 Predicted AlphaFoldDB

17 variants for Q9FNG3

Variant ID(s) Position Change Description Diseaes Association Provenance
tmp_5_1968470_G_A 7 P>L No 1000Genomes
ENSVATH10610423 14 G>A No 1000Genomes
ENSVATH06931368 26 S>L No 1000Genomes
tmp_5_1968329_T_A 54 Y>F No 1000Genomes
tmp_5_1968321_C_A 57 V>L No 1000Genomes
tmp_5_1968314_A_C 59 F>C No 1000Genomes
ENSVATH06931364 61 E>A No 1000Genomes
ENSVATH10610421 79 S>N No 1000Genomes
tmp_5_1968201_G_T 97 L>I No 1000Genomes
ENSVATH13941409 99 D>V No 1000Genomes
ENSVATH06931362 101 Y>F No 1000Genomes
tmp_5_1968181_G_T 103 F>L No 1000Genomes
ENSVATH06931361 112 V>I No 1000Genomes
ENSVATH06931360 121 D>N No 1000Genomes
ENSVATH00608976 124 R>I No 1000Genomes
tmp_5_1967963_T_C 176 K>R No 1000Genomes
ENSVATH06931352 197 V>I No 1000Genomes

No associated diseases with Q9FNG3

No regional properties for Q9FNG3

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q9FNG3

Functions

Description
EC Number 3.1.13.1 Exoribonucleases producing 5'-phosphomonoesters
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
plant-type vacuole A closed structure that is completely surrounded by a unit membrane, contains liquid, and retains the same shape regardless of cell cycle phase. An example of this structure is found in Arabidopsis thaliana.

6 GO annotations of molecular function

Name Definition
3'-5' exonuclease activity Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end.
exoribonuclease II activity Catalysis of the reaction: RNA + H2O = 5'-phosphomononucleotides. Cleaves RNA in the 3' to 5' direction.
nucleic acid binding Binding to a nucleic acid.
protein self-association Binding to a domain within the same polypeptide.
RISC complex binding Binding to a RISC complex.
single-stranded DNA 3'-5' exodeoxyribonuclease activity Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of a single-stranded DNA molecule.

2 GO annotations of biological process

Name Definition
gene silencing by RNA A process in which an RNA molecule reduces expression of target genes. This can occur pre-transcriptionally by assembly of heterochromatin and prevention of transcription or co- or post-transcriptionally by targeting RNAs for degradation or by interfering with splicing or translation. This process starts once the inhibitory RNA molecule has been transcribed, and includes processing of the RNA such as cleavage, modifications, transport from the nucleus to the cytoplasm, loading onto the RISC complex, and the effect on transcription or translation.
positive regulation of miRNA metabolic process Any process that activates or increases the frequency, rate or extent of miRNA metabolic process.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MASFDGPKFK MTDGSYVQTK TIDVGSSTDI SPYLSLIRED SILNGNRAVI FDVYWDVGFP
70 80 90 100 110 120
ETETKTKTSG WSLSSVKLST RNLCLFLRLP KPFHDNLKDL YRFFASKFVT FVGVQIEEDL
130 140 150 160 170 180
DLLRENHGLV IRNAINVGKL AAEARGTLVL EFLGTRELAH RVLWSDLGQL DSIEAKWEKA
190 200
GPEEQLEAAA IEGWLIVNVW DQLSDE