A0AA36G9A7 · A0AA36G9A7_9BILA
- ProteinRibonuclease
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1020 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic activity
- 6-(alpha-D-glucosaminyl)-(1-octadecanoyl,2-(9Z)-octadecenoyl-sn-glycero-3-phospho)-1D-myo-inositol(in) = 6-(alpha-D-glucosaminyl)-(1-octadecanoyl,2-(9Z)-octadecenoyl-sn-glycero-3-phospho)-1D-myo-inositol(out)
- a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out)
- a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out)
- a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out)
- an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol(in) = an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol(out)
Cofactor
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )
Note: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | signal peptidase complex | |
Molecular Function | metal ion binding | |
Molecular Function | RNA binding | |
Molecular Function | RNA-DNA hybrid ribonuclease activity | |
Biological Process | RNA catabolic process | |
Biological Process | signal peptide processing |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibonuclease
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Mesorhabditinae > Mesorhabditis
Accessions
- Primary accessionA0AA36G9A7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 560-581 | Helical | ||||
Sequence: LYLLGVTFLVSALHLLFDVLSF | ||||||
Transmembrane | 602-617 | Helical | ||||
Sequence: LLWRAFSYTVIFFYLM | ||||||
Transmembrane | 679-698 | Helical | ||||
Sequence: WLALLMLPLCVGGAIYSLAY | ||||||
Transmembrane | 704-725 | Helical | ||||
Sequence: WYSWCIESMANGVYAFGFLFML | ||||||
Transmembrane | 887-906 | Helical | ||||
Sequence: LLISFIAVCFSGFAAAWHYV | ||||||
Transmembrane | 912-933 | Helical | ||||
Sequence: VKPVLIICSAGYFITVGILQLY |
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 30-253 | RNase H type-2 | ||||
Sequence: PCVLGIDEAGRGPVLGPMVYGCAISPVDKDAELRSLGVDDSKALTEAKREEIFDDMNDSGETKQVVAWAIQCLSAQYISSSMLKRNKISLNEISHNSAIQLIRDALAANVNVVEIFVDTVGPKATYQAKLERIFPGISITVSEKADSKYPIVSAASIAAKVTRDRRLRAWEFRETGVNVPEAGFGSDPNTKKFLAGGVDPIFGFSSLIRFSWKTADLIVEKRCA |
Sequence similarities
Belongs to the CLPTM1 family.
Belongs to the RNase HII family.
Belongs to the SPCS2 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusFragment
- Length1,020
- Mass (Da)114,613
- Last updated2024-01-24 v1
- Checksum79D4C05589E52159
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1020 | |||||
Sequence: E |
Keywords
- Technical term