"accession"	"counters"	"description"	"gene"	"go_terms"	"id"	"ida_accession"	"in_alphafold"	"in_bfvd"	"is_fragment"	"length"	"name"	"protein_evidence"	"proteome"	"sequence"	"source_database"	"source_organism"
"Q58717"	"{'domain_architectures': 2, 'entries': 18, 'isoforms': 0, 'proteomes': 1, 'sets': 4, 'structures': 2, 'taxa': 1, 'dbEntries': {'ssf': 2, 'pfam': 3, 'profile': 2, 'cathgene3d': 2, 'cdd': 1, 'smart': 1, 'interpro': 7}, 'proteome': 1, 'taxonomy': 1, 'similar_proteins': 2}"	"[""A DNA-guided ssDNA endonuclease that may play a role in defense against invading genetic elements. Uses short ssDNA sequences as guides (gDNA) to bind complementary target strands, resulting in slicing of the target DNA (tDNA) (PubMed:24442234, PubMed:27741323, PubMed:28319081, PubMed:28319084). Endonucleolytically cleaves tDNA (the gDNA indicates where to cleave); two major and two minor products are seen which correspond to cleavage sites between nucleotides 9/10, 10/11, 13/14, and 14/15 downstream of the target residue base-paired with the 5'-end of the gDNA (PubMed:24442234, PubMed:27741323, PubMed:28319081, PubMed:28319084). Efficient guide-dependent tDNA cleavage requires a minimal length of 15 bp and is maximal at 19 bp (PubMed:28319081). Prefers gDNA with 5'-phosphorylated purines and 3'-pyrimidines; changing these bases alters the cleavage activity and patterns (PubMed:28319084). Also has guide-independent activity on tDNA called 'chopping' (PubMed:28319081). Probably a first round of guide-independent activity on an invading plasmid or virus would generate guide DNAs for subsequent, more efficient, guide-dependent degradation of invading nucleic acids (PubMed:28319081). Has no activity on substrate with a mismatch at positions 10 and 11, on ssDNA or RNA, nor on DNA:RNA hybrids (PubMed:24442234). Digests longer (750 bp) dsDNA as well as circular plasmid and naked genomic DNA, but not chromatin, in a guide DNA-independent manner (PubMed:28319081). Addition of endogenous histone A3 protects DNA from cleavage, while cleavage is insensitive to methylation (PubMed:28319081). When plasmid encoding active or mutated protein (Ala-541) is transformed into Sulfolobus acidocaldarius about 25-fold fewer transformants are found with active protein; reduced levels of plasmid are found in wild-type transformed cells. While S.acidocaldarius grows at a similar temperature to M.jannaschii (70 to 80 degrees Celsius) it has very different histone-like proteins, which presumably do not protect against MjAgo (PubMed:28319081). Binds ssDNA, dsDNA and DNA-RNA hybrids; binding is most efficient with dsDNA (PubMed:24442234)""]"	"ago"	"[{'identifier': 'GO:0005515', 'name': 'protein binding', 'category': {'code': 'F', 'name': 'molecular_function'}}, {'identifier': 'GO:0003723', 'name': 'RNA binding', 'category': {'code': 'F', 'name': 'molecular_function'}}, {'identifier': 'GO:0003676', 'name': 'nucleic acid binding', 'category': {'code': 'F', 'name': 'molecular_function'}}]"	"AGO_METJA"	"12d4d8dd2c08327c003123dfd7b16d57c6a8ac58"	True	False	False	713	"Protein argonaute"	1	"UP000000805"	"MVLNKVTYKINAYKIKEEFIPKEVHFYRIKSFVNEAFNFYRFVNFYGGMIINKKDKSFVLPYKVDNKVLKYKDGNNEIPIDIEYIKSLKLEYVKPEIAEKLVRGYLKSVHKIEPELSRIIKNIRKHKVVENIKVESYCEYEVKKHDGDYYLILNFRHTASITKHLWDFVNRDKALLEEYVGKKIIFKPNPKVRYTISLVDAPNPQKIEEIMSHIIKYYKWSEDMVKSTFGEIDYNQPIMYCEEILEPFAPQFCNLVFYMDELDSYILKELQSYWRLSNENKGKIINEIAKKLRFIDNTPKELEFMKFNNTPLLVKDVNKNPTKIYSTNTLFTWIYNQNAKIYLPYDVPEIIRNKNLLTYILIDEEIKDELKAIKDKVNKMFRNYNKIANKTELPKFNYANRWKYFSTDDIRGIIKEIKSEFNDEICFALIIGKEKYKDNDYYEILKKQLFDLKIISQNILWENWRKDDKGYMTNNLLIQIMGKLGIKYFILDSKTPYDYIMGLDTGLGIFGNHRVGGCTVVYDSEGKIRRIQPIETPAPGERLHLPYVIEYLENKANIDMENKNILFLRDGFIQNSERNDLKEISKELNSNIEVISIRKNNKYKVFTSDYRIGSVFGNDGIFLPHKTPFGSNPVKLSTWLRFNCGNEEGLKINESIMQLLYDLTKMNYSALYGEGRYLRIPAPIHYADKFVKALGKNWKIDEELLKHGFLYFI"	"reviewed"	"{'taxId': '243232', 'scientificName': 'Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)', 'fullName': 'Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)'}"