A0A1M5A5Z8 · AGO_MARH1
- ProteinProtein argonaute
- Geneago
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids640 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
A highly versatile argonaute that uses 5'-phospho- and 5'-OH- guide RNA (gRNA) or DNA (gDNA) to cleave target RNA or ssDNA (tDNA) in all possible combinations; has no detectable activity in the absence of guide. Uses short guide sequences (18-21 nucleotides (nt) on average) to bind complementary target nucleic acids resulting in target cleavage in a site-specific manner. Using 5'-phospho-gRNA or 5'-OH-gRNA the cleavage site is 10 nt downstream of the target residue base-paired with the 5'-end of the gRNA, using 5'-phospho-gDNA the cleavage site is 11 nucleotides (nt) downstream, while with 5'-OH-gDNA the cleavage site is 9 nt downstream.
Miscellaneous
Unlike most prokaryotic argonautes, this is encoded in a CRISPR-cas locus.
Cofactor
Note: Mn2+ supports cleavage of all guide:target combinations, Mg2+ only supports gRNA-directed cleavage (PubMed:36288702).
Cleavage probaby requires 2 divalent metal cations (By similarity).
Cleavage probaby requires 2 divalent metal cations (By similarity).
Temperature Dependence
Optimum temperature for all combinations of guide:target is 60-65 degrees Celsius, the RNA product is more stable at 60 than 65 degrees Celsius.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 445 | |||||
Sequence: D | ||||||
Binding site | 445 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 445 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 481 | |||||
Sequence: E | ||||||
Active site | 515 | |||||
Sequence: D | ||||||
Binding site | 515 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 623 | |||||
Sequence: N | ||||||
Binding site | 623 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | DNA binding | |
Molecular Function | DNA endonuclease activity | |
Molecular Function | metal ion binding | |
Molecular Function | RNA binding | |
Molecular Function | RNA endonuclease activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein argonaute
- EC number
- Short namesMhAgo
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Thermotogota > Thermotogae > Petrotogales > Petrotogaceae > Marinitoga
Accessions
- Primary accessionA0A1M5A5Z8
Proteomes
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 445 | No longer cleaves target; when associated with A-515. | ||||
Sequence: D → A | ||||||
Mutagenesis | 515 | No longer cleaves target; when associated with A-445. | ||||
Sequence: D → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000457786 | 1-640 | Protein argonaute | |||
Sequence: MYLNLYEIKIPYRVKRLYYFNKENDPKEFARNLSRVNNIRFNDSKDLVWLEIPDIDFKITPQQAEKYKIEKNEIIGEKEDSDLFVKTIYRYIKKKFIDNNFYYKRGNNYISINDKFPLDSNTNVNAHLTYKIKLYKINERYYISVLPKFTFLSDKPALESPIKSTYLFNIKSGKTFPYISGLNGVLKIDLGENGIKEVLFPENYYFNFTSKEAEKFGFSKEIHNIYKEKIFSGYKKIKQSLYFLEDIININNYNLTMDKKIYVNIEYEFKKGISRNIKDVFKYSFYKNDQKIKIAFFFSSKKQIYEIQRSLKMLFQNKNSIFYQTIYEMGFSKVIFLREPKTNSSAFMYNPETFEISNKDFFENLEGNIMAIIILDKFLGNIDSLIQKFPENLILQPILKEKLEKIQPYIIKSYVYKMGNFIPECQPYVIRNLKDKNKTLYIGIDLSHDNYLKKSNLAISAVNNFGDIIYLNKYKNLELNEKMNLDIVEKEYIQILNEYYERNKNYPENIIVLRDGRYLEDIEIIKNILNIENIKYSLIEVNKSVNINSCEDLKEWIIKLSDNNFIYYPKTYFNQKGVEIKIIENNTDYNNEKILEQVYSLTRVVHPTPYVNYRLPYPLQVVNKVALTELEWKLYIPYMK |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-100 | N-terminal domain | ||||
Sequence: MYLNLYEIKIPYRVKRLYYFNKENDPKEFARNLSRVNNIRFNDSKDLVWLEIPDIDFKITPQQAEKYKIEKNEIIGEKEDSDLFVKTIYRYIKKKFIDNN | ||||||
Region | 101-153 | Linker L1 | ||||
Sequence: FYYKRGNNYISINDKFPLDSNTNVNAHLTYKIKLYKINERYYISVLPKFTFLS | ||||||
Region | 154-209 | PAZ domain | ||||
Sequence: DKPALESPIKSTYLFNIKSGKTFPYISGLNGVLKIDLGENGIKEVLFPENYYFNFT | ||||||
Region | 210-291 | Linker L2 | ||||
Sequence: SKEAEKFGFSKEIHNIYKEKIFSGYKKIKQSLYFLEDIININNYNLTMDKKIYVNIEYEFKKGISRNIKDVFKYSFYKNDQK | ||||||
Region | 292-423 | Mid domain | ||||
Sequence: IKIAFFFSSKKQIYEIQRSLKMLFQNKNSIFYQTIYEMGFSKVIFLREPKTNSSAFMYNPETFEISNKDFFENLEGNIMAIIILDKFLGNIDSLIQKFPENLILQPILKEKLEKIQPYIIKSYVYKMGNFIP | ||||||
Region | 424-640 | PIWI domain | ||||
Sequence: ECQPYVIRNLKDKNKTLYIGIDLSHDNYLKKSNLAISAVNNFGDIIYLNKYKNLELNEKMNLDIVEKEYIQILNEYYERNKNYPENIIVLRDGRYLEDIEIIKNILNIENIKYSLIEVNKSVNINSCEDLKEWIIKLSDNNFIYYPKTYFNQKGVEIKIIENNTDYNNEKILEQVYSLTRVVHPTPYVNYRLPYPLQVVNKVALTELEWKLYIPYMK |
Domain
Has 4 domains (N-terminal, PAZ, Mid and PIWI). The N-terminal and PAZ domains are joined by linker L1, the PAZ and Mid domains are joined by linker L2. The domains assemble in 2 lobes; the PAZ lobe consists of the N-terminal, L1, PAZ and L2 domains, while the PIWI lobe has the Mid and PIWI domains. The PIWI domain assumes an RNase H fold and has the catalytic residues. gDNA lies between the 2 lobes, with its unpaired 5'-end anchored in the Mid lobe.
Sequence similarities
Belongs to the argonaute family. Long pAgo subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length640
- Mass (Da)76,715
- Last updated2017-03-15 v1
- ChecksumE1527C6F01E12279