{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY6JWG2","uniProtkbId":"A0ABY6JWG2_9ARAC","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Cordylochernes scorpioides","taxonId":51811,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UYV60324.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001235939"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Chelicerata","Arachnida","Pseudoscorpiones","Cheliferoidea","Chernetidae","Cordylochernes"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00039862"}],"value":"Alanine--glyoxylate aminotransferase 2, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044055"}],"value":"2.6.1.18"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00039130"}],"value":"2.6.1.40"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013049"}],"value":"2.6.1.44"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00041662"}],"value":"(R)-3-amino-2-methylpropionate--pyruvate transaminase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00042611"}],"value":"Beta-ALAAT II"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00042669"}],"value":"Beta-alanine-pyruvate aminotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044258"}],"value":"D-3-aminoisobutyrate-pyruvate aminotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00041845"}],"value":"D-AIBAT"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044257"}],"value":"D-beta-aminoisobutyrate-pyruvate aminotransferase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UYV60324.1"}],"value":"LAZ67_1000824"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00058068"}],"value":"Multifunctional aminotransferase with a broad substrate specificity. 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The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA also has nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025615"}],"value":"Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00055265"}],"value":"Nucleocapsid protein p11 (NC) forms the nucleocore that coats the retro-elements dimeric RNA. Binds these RNAs through its zinc fingers. Promotes primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty3 RNA and initiation of reverse transcription"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025590"}],"value":"Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. 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The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002180"}],"value":"The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22508"},{"database":"Rhea","id":"RHEA-COMP:17339"},{"database":"Rhea","id":"RHEA-COMP:17340"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61560"},{"database":"ChEBI","id":"CHEBI:173112"}],"ecNumber":"2.7.7.49","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22508"},{"database":"Rhea","id":"RHEA-COMP:17339"},{"database":"Rhea","id":"RHEA-COMP:17340"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61560"},{"database":"ChEBI","id":"CHEBI:173112"}],"ecNumber":"2.7.7.7","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Endonucleolytic cleavage to 5'-phosphomonoester.","ecNumber":"3.1.26.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000077"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. 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retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00055265"}],"value":"Nucleocapsid protein p11 (NC) forms the nucleocore that coats the retro-elements dimeric RNA. Binds these RNAs through its zinc fingers. Promotes primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty3 RNA and initiation of reverse transcription"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025590"}],"value":"Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002180"}],"value":"The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22508"},{"database":"Rhea","id":"RHEA-COMP:17339"},{"database":"Rhea","id":"RHEA-COMP:17340"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61560"},{"database":"ChEBI","id":"CHEBI:173112"}],"ecNumber":"2.7.7.49","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22508"},{"database":"Rhea","id":"RHEA-COMP:17339"},{"database":"Rhea","id":"RHEA-COMP:17340"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61560"},{"database":"ChEBI","id":"CHEBI:173112"}],"ecNumber":"2.7.7.7","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Endonucleolytic cleavage to 5'-phosphomonoester.","ecNumber":"3.1.26.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000077"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.","ecNumber":"3.4.23.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10094"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00063849"}],"value":"The protease is a homodimer, whose active site consists of two apposed aspartic acid residues"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00457"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":2058,"modifier":"EXACT"}},"description":"Pepsin 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Once in the nucleus, integrase performs the integration of the dsDNA into the host genome"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00055265"}],"value":"Nucleocapsid protein p11 (NC) forms the nucleocore that coats the retro-elements dimeric RNA. Binds these RNAs through its zinc fingers. Promotes primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty3 RNA and initiation of reverse transcription"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025590"}],"value":"Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. 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