{"gene":"PF3D7_1463700","run_date":"2026-09-08T14:19:07","timeline":{"discoveries":[{"year":2000,"finding":"CYC1 (Pfcyc-1) was cloned and shown to activate recombinant PfPK5 (a P. falciparum Cdk1 homologue) in vitro with an efficiency similar to that of human cyclin H and p25, demonstrating that CYC1 functions as a cyclin capable of activating a parasite CDK.","method":"In vitro kinase activation assay using recombinant proteins","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — in vitro reconstitution assay in a single lab with a single method","pmids":["10722743"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2003,"finding":"CYC1 (Pfcyc-1) was shown to activate PfPK5 in vitro and to associate with histone H1 kinase activity in parasite extracts, confirming its cyclin activity in erythrocytic-stage parasites.","method":"In vitro kinase activation assay and immunoprecipitation of histone H1 kinase activity from parasite extracts","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 1-2 / Moderate — two orthogonal methods (in vitro CDK activation and kinase co-precipitation from extracts), single lab","pmids":["12869562"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"finding":"CYC1 (PfCyc1) complements a G1 cyclin-depleted Saccharomyces cerevisiae strain but does NOT complement a temperature-sensitive yeast cyclin H mutant, demonstrating a functional divergence from its bioinformatic classification as a cyclin H homologue.","method":"Heterologous complementation in Saccharomyces cerevisiae","journal":"mBio","confidence":"High","confidence_rationale":"Tier 1-2 / Strong — yeast complementation plus multiple additional orthogonal methods in the same study (Co-IP, conditional knockdown with phenotypic readout)","pmids":["28611247"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"finding":"Coimmunoprecipitation of CYC1 (PfCyc1) from P. falciparum parasites identifies PfMAT1 and PfMRK as specific interaction partners; PfPK5 and other CDKs were NOT co-immunoprecipitated, indicating that the physiological complex of CYC1 in the parasite is with PfMRK and PfMAT1, not with PfPK5.","method":"Coimmunoprecipitation from P. falciparum parasite lysates","journal":"mBio","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal Co-IP from native parasite extracts, corroborated by multiple orthogonal experiments in the same study","pmids":["28611247"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"finding":"Conditional knockdown of CYC1 (PfCyc1) using a destabilization domain (DD) approach in blood-stage P. falciparum demonstrates that CYC1 is essential for blood-stage proliferation; knockdown does not impede nuclear division but prevents proper cytokinesis, resulting in morphologically aberrant schizonts.","method":"Destabilization domain (DD)-mediated conditional knockdown with phenotypic analysis by microscopy","journal":"mBio","confidence":"High","confidence_rationale":"Tier 2 / Strong — conditional genetic knockdown with defined stage-specific morphological phenotype, corroborated by yeast complementation and Co-IP in the same study","pmids":["28611247"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2013,"finding":"In silico structural modelling and 10 ns molecular dynamics simulation of CYC1 (Pfcyc-1) indicate that, despite poor sequence similarity to cyclin H and A, the protein possesses a conserved cyclin box (two tandemly repeating five-helix bundles) and conserved amino acid residues at predicted cyclin-CDK interaction interfaces.","method":"Homology modelling and molecular dynamics simulation (computational only)","journal":"Journal of biomolecular structure & dynamics","confidence":"Low","confidence_rationale":"Tier 4 / Weak — purely computational study with no experimental validation","pmids":["23998890"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"CYC1 (PF3D7_1463700) is an essential P. falciparum cyclin that, contrary to its bioinformatic annotation as a cyclin H homologue, forms a complex with PfMRK and PfMAT1 (not PfPK5) in blood-stage parasites and is specifically required for cytokinesis—but not nuclear division—during schizogony, while also being capable of activating PfPK5 in vitro."},"narrative":{"mechanistic_narrative":"CYC1 (PF3D7_1463700) is an essential Plasmodium falciparum cyclin that governs the cytokinetic phase of blood-stage schizogony [PMID:28611247]. Although bioinformatically classified as a cyclin H homologue, CYC1 is functionally divergent: it complements a G1 cyclin-depleted yeast strain but fails to rescue a temperature-sensitive cyclin H mutant [PMID:28611247]. Biochemically, CYC1 behaves as a bona fide cyclin, activating the parasite CDK PfPK5 in vitro with an efficiency comparable to human cyclin H and associating with histone H1 kinase activity in erythrocytic-stage extracts [PMID:10722743, PMID:12869562]. However, its physiological partners in the parasite are PfMRK and PfMAT1 rather than PfPK5, defining a native CYC1–PfMRK–PfMAT1 complex [PMID:28611247]. Conditional knockdown establishes that CYC1 is dispensable for nuclear division but required for proper cytokinesis, and its loss produces morphologically aberrant schizonts [PMID:28611247]. Beyond this complex assignment and stage-specific role, the substrate repertoire and detailed regulatory mechanism of CYC1 have not been characterized in the available corpus.","teleology":[{"year":2000,"claim":"Whether the cloned parasite cyclin candidate could act as a genuine cyclin was unknown; demonstrating in vitro activation of a parasite CDK established CYC1 as a functional cyclin.","evidence":"In vitro kinase activation assay of recombinant PfPK5 by recombinant CYC1","pmids":["10722743"],"confidence":"Medium","gaps":["In vitro activation does not establish the physiological CDK partner in the parasite","No cellular localization or stage expression data"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2003,"claim":"It was unclear whether CYC1's cyclin activity was relevant to erythrocytic-stage parasites; linking it to endogenous histone H1 kinase activity extended its cyclin function to the blood stage.","evidence":"In vitro CDK activation plus immunoprecipitation of histone H1 kinase activity from parasite extracts","pmids":["12869562"],"confidence":"Medium","gaps":["Histone H1 kinase activity does not identify which CDK CYC1 partners with in vivo","No genetic evidence for essentiality at this point"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2013,"claim":"Whether a protein with poor sequence similarity to canonical cyclins retains cyclin architecture was open; computational modelling predicted a conserved cyclin box and CDK-interaction residues.","evidence":"Homology modelling and 10 ns molecular dynamics simulation (computational only)","pmids":["23998890"],"confidence":"Low","gaps":["Purely computational with no experimental structural validation","Predicted interaction interfaces not tested biochemically"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"claim":"The bioinformatic annotation of CYC1 as a cyclin H homologue and its assumed PfPK5 pairing were untested in vivo; heterologous complementation and native Co-IP redefined its identity as a G1-cyclin-like protein partnering PfMRK and PfMAT1.","evidence":"Yeast complementation (rescue of G1 cyclin depletion but not cyclin H mutant) and reciprocal Co-IP from parasite lysates","pmids":["28611247"],"confidence":"High","gaps":["Kinase activity and substrates of the CYC1–PfMRK–PfMAT1 complex not defined","Reconciliation of in vitro PfPK5 activation with the native PfMRK partnership unresolved"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"claim":"The cellular requirement for CYC1 was unknown; conditional knockdown established that it is essential specifically for cytokinesis during schizogony, not for nuclear division.","evidence":"Destabilization domain-mediated conditional knockdown with microscopic phenotyping in blood-stage P. falciparum","pmids":["28611247"],"confidence":"High","gaps":["The molecular pathway linking CYC1 to cytokinesis is not defined","The substrates whose phosphorylation drives cytokinesis are unknown"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"The catalytic output and substrates of the native CYC1–PfMRK–PfMAT1 complex, and how they mechanistically execute cytokinesis, remain unresolved.","evidence":"","pmids":[],"confidence":"High","gaps":["No substrate of the native complex identified","No experimental structure of the parasite complex","Mechanistic basis of the in vitro PfPK5 activation versus in vivo PfMRK partnership not reconciled"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["CYC1–PfMRK–PfMAT1 complex"],"partners":["PFMRK","PFMAT1","PFPK5 (IN VITRO ONLY)"],"other_free_text":["Essential for blood-stage proliferation; required for cytokinesis but not nuclear division during schizogony [#4].","Functionally behaves as a G1-type cyclin in yeast complementation despite cyclin H bioinformatic annotation [#2].","Predicted to contain a conserved cyclin box fold by computational modelling [#5]."]}},"prefetch_data":{},"corpus_meta":[{"pmid":"10722743","id":"PMC_10722743","title":"Activation of a Plasmodium falciparum cdc2-related kinase by heterologous p25 and cyclin H. Functional characterization of a P. falciparum cyclin homologue.","date":"2000","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/10722743","citation_count":88,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfCYC1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"12869562","id":"PMC_12869562","title":"Identification and initial characterization of three novel cyclin-related proteins of the human malaria parasite Plasmodium falciparum.","date":"2003","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/12869562","citation_count":61,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"28611247","id":"PMC_28611247","title":"The Malaria Parasite Cyclin H Homolog PfCyc1 Is Required for Efficient Cytokinesis in Blood-Stage Plasmodium falciparum.","date":"2017","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/28611247","citation_count":30,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["CYC1","PfCYC1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"20332005","id":"PMC_20332005","title":"The malarial CDK Pfmrk and its effector PfMAT1 phosphorylate DNA replication proteins and co-localize in the nucleus.","date":"2010","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/20332005","citation_count":26,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"27326764","id":"PMC_27326764","title":"Correlation between Cyclin Dependent Kinases and Artemisinin-Induced Dormancy in Plasmodium falciparum In Vitro.","date":"2016","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/27326764","citation_count":16,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfCYC1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"23998890","id":"PMC_23998890","title":"In silico characterization and molecular dynamics simulation of Pfcyc-1, a cyclin homolog of Plasmodium falciparum.","date":"2013","source":"Journal of biomolecular structure & dynamics","url":"https://pubmed.ncbi.nlm.nih.gov/23998890","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfCYC1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6152,"output_tokens":1558,"usd":0.020913,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6545,"output_tokens":2354,"usd":0.045788,"stage2_stop_reason":"end_turn"},"total_usd":0.066701,"stage1_batch_id":"msgbatch_011BPjN2BL33F8cJXD1r7V7T","stage2_batch_id":"msgbatch_01Qwg6vP7qxkpL6Gsc7tajsb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2000,\n      \"finding\": \"CYC1 (Pfcyc-1) was cloned and shown to activate recombinant PfPK5 (a P. falciparum Cdk1 homologue) in vitro with an efficiency similar to that of human cyclin H and p25, demonstrating that CYC1 functions as a cyclin capable of activating a parasite CDK.\",\n      \"method\": \"In vitro kinase activation assay using recombinant proteins\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — in vitro reconstitution assay in a single lab with a single method\",\n      \"pmids\": [\"10722743\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2003,\n      \"finding\": \"CYC1 (Pfcyc-1) was shown to activate PfPK5 in vitro and to associate with histone H1 kinase activity in parasite extracts, confirming its cyclin activity in erythrocytic-stage parasites.\",\n      \"method\": \"In vitro kinase activation assay and immunoprecipitation of histone H1 kinase activity from parasite extracts\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1-2 / Moderate — two orthogonal methods (in vitro CDK activation and kinase co-precipitation from extracts), single lab\",\n      \"pmids\": [\"12869562\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"CYC1 (PfCyc1) complements a G1 cyclin-depleted Saccharomyces cerevisiae strain but does NOT complement a temperature-sensitive yeast cyclin H mutant, demonstrating a functional divergence from its bioinformatic classification as a cyclin H homologue.\",\n      \"method\": \"Heterologous complementation in Saccharomyces cerevisiae\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 / Strong — yeast complementation plus multiple additional orthogonal methods in the same study (Co-IP, conditional knockdown with phenotypic readout)\",\n      \"pmids\": [\"28611247\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"Coimmunoprecipitation of CYC1 (PfCyc1) from P. falciparum parasites identifies PfMAT1 and PfMRK as specific interaction partners; PfPK5 and other CDKs were NOT co-immunoprecipitated, indicating that the physiological complex of CYC1 in the parasite is with PfMRK and PfMAT1, not with PfPK5.\",\n      \"method\": \"Coimmunoprecipitation from P. falciparum parasite lysates\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal Co-IP from native parasite extracts, corroborated by multiple orthogonal experiments in the same study\",\n      \"pmids\": [\"28611247\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"Conditional knockdown of CYC1 (PfCyc1) using a destabilization domain (DD) approach in blood-stage P. falciparum demonstrates that CYC1 is essential for blood-stage proliferation; knockdown does not impede nuclear division but prevents proper cytokinesis, resulting in morphologically aberrant schizonts.\",\n      \"method\": \"Destabilization domain (DD)-mediated conditional knockdown with phenotypic analysis by microscopy\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — conditional genetic knockdown with defined stage-specific morphological phenotype, corroborated by yeast complementation and Co-IP in the same study\",\n      \"pmids\": [\"28611247\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"In silico structural modelling and 10 ns molecular dynamics simulation of CYC1 (Pfcyc-1) indicate that, despite poor sequence similarity to cyclin H and A, the protein possesses a conserved cyclin box (two tandemly repeating five-helix bundles) and conserved amino acid residues at predicted cyclin-CDK interaction interfaces.\",\n      \"method\": \"Homology modelling and molecular dynamics simulation (computational only)\",\n      \"journal\": \"Journal of biomolecular structure & dynamics\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 4 / Weak — purely computational study with no experimental validation\",\n      \"pmids\": [\"23998890\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"CYC1 (PF3D7_1463700) is an essential P. falciparum cyclin that, contrary to its bioinformatic annotation as a cyclin H homologue, forms a complex with PfMRK and PfMAT1 (not PfPK5) in blood-stage parasites and is specifically required for cytokinesis—but not nuclear division—during schizogony, while also being capable of activating PfPK5 in vitro.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"CYC1 (PF3D7_1463700) is an essential Plasmodium falciparum cyclin that governs the cytokinetic phase of blood-stage schizogony [#4]. Although bioinformatically classified as a cyclin H homologue, CYC1 is functionally divergent: it complements a G1 cyclin-depleted yeast strain but fails to rescue a temperature-sensitive cyclin H mutant [#2]. Biochemically, CYC1 behaves as a bona fide cyclin, activating the parasite CDK PfPK5 in vitro with an efficiency comparable to human cyclin H and associating with histone H1 kinase activity in erythrocytic-stage extracts [#0, #1]. However, its physiological partners in the parasite are PfMRK and PfMAT1 rather than PfPK5, defining a native CYC1–PfMRK–PfMAT1 complex [#3]. Conditional knockdown establishes that CYC1 is dispensable for nuclear division but required for proper cytokinesis, and its loss produces morphologically aberrant schizonts [#4]. Beyond this complex assignment and stage-specific role, the substrate repertoire and detailed regulatory mechanism of CYC1 have not been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2000,\n      \"claim\": \"Whether the cloned parasite cyclin candidate could act as a genuine cyclin was unknown; demonstrating in vitro activation of a parasite CDK established CYC1 as a functional cyclin.\",\n      \"evidence\": \"In vitro kinase activation assay of recombinant PfPK5 by recombinant CYC1\",\n      \"pmids\": [\"10722743\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"In vitro activation does not establish the physiological CDK partner in the parasite\", \"No cellular localization or stage expression data\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2003,\n      \"claim\": \"It was unclear whether CYC1's cyclin activity was relevant to erythrocytic-stage parasites; linking it to endogenous histone H1 kinase activity extended its cyclin function to the blood stage.\",\n      \"evidence\": \"In vitro CDK activation plus immunoprecipitation of histone H1 kinase activity from parasite extracts\",\n      \"pmids\": [\"12869562\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Histone H1 kinase activity does not identify which CDK CYC1 partners with in vivo\", \"No genetic evidence for essentiality at this point\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"Whether a protein with poor sequence similarity to canonical cyclins retains cyclin architecture was open; computational modelling predicted a conserved cyclin box and CDK-interaction residues.\",\n      \"evidence\": \"Homology modelling and 10 ns molecular dynamics simulation (computational only)\",\n      \"pmids\": [\"23998890\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Purely computational with no experimental structural validation\", \"Predicted interaction interfaces not tested biochemically\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"The bioinformatic annotation of CYC1 as a cyclin H homologue and its assumed PfPK5 pairing were untested in vivo; heterologous complementation and native Co-IP redefined its identity as a G1-cyclin-like protein partnering PfMRK and PfMAT1.\",\n      \"evidence\": \"Yeast complementation (rescue of G1 cyclin depletion but not cyclin H mutant) and reciprocal Co-IP from parasite lysates\",\n      \"pmids\": [\"28611247\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Kinase activity and substrates of the CYC1–PfMRK–PfMAT1 complex not defined\", \"Reconciliation of in vitro PfPK5 activation with the native PfMRK partnership unresolved\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"The cellular requirement for CYC1 was unknown; conditional knockdown established that it is essential specifically for cytokinesis during schizogony, not for nuclear division.\",\n      \"evidence\": \"Destabilization domain-mediated conditional knockdown with microscopic phenotyping in blood-stage P. falciparum\",\n      \"pmids\": [\"28611247\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"The molecular pathway linking CYC1 to cytokinesis is not defined\", \"The substrates whose phosphorylation drives cytokinesis are unknown\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The catalytic output and substrates of the native CYC1–PfMRK–PfMAT1 complex, and how they mechanistically execute cytokinesis, remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"gaps\": [\"No substrate of the native complex identified\", \"No experimental structure of the parasite complex\", \"Mechanistic basis of the in vitro PfPK5 activation versus in vivo PfMRK partnership not reconciled\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0016538\", \"supporting_discovery_ids\": [0, 1, 2, 3]},\n      {\"term_id\": \"GO:0061575\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [],\n    \"pathway\": [\n      {\"term_id\": \"GO:0000910\", \"supporting_discovery_ids\": [4]},\n      {\"term_id\": \"GO:0051301\", \"supporting_discovery_ids\": [4]}\n    ],\n    \"complexes\": [\"CYC1–PfMRK–PfMAT1 complex\"],\n    \"partners\": [\"PfMRK\", \"PfMAT1\", \"PfPK5 (in vitro only)\"],\n    \"other_free_text\": [\n      \"Essential for blood-stage proliferation; required for cytokinesis but not nuclear division during schizogony [#4].\",\n      \"Functionally behaves as a G1-type cyclin in yeast complementation despite cyclin H bioinformatic annotation [#2].\",\n      \"Predicted to contain a conserved cyclin box fold by computational modelling [#5].\"\n    ]\n  }\n}\n```","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1463700","name":null,"product":"cyclin 1","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1327061","name":null,"product":"cyclin 1, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1217800","name":null,"product":"cyclin 1, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"CYC1","evaluation":null}