{"gene":"PF3D7_0608700","run_date":"2026-09-08T19:44:17","timeline":{"discoveries":[{"year":2017,"finding":"CCT6 (PF3D7_0608700) is a subunit of the Plasmodium TRiC chaperonin complex, which localizes to the parasite cytosol and is not exported into the host red blood cell. Regulatable knockdown of the TRiC-θ subunit (a sibling subunit) caused severe asexual growth defects without altering protein export, indicating the TRiC complex (including CCT6) is essential for parasite biology but functions within the parasite, not in RBC protein trafficking.","method":"Epitope-tagged transgenic parasites, parasite-specific antibody localization, regulatable knockdown with growth and export phenotype readouts","journal":"Cellular microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization by tagged transgenic lines and antibody, loss-of-function growth phenotype; CCT6 membership in the complex is implicit (complex studied), functional conclusion about the complex applies to CCT6 as a subunit; single lab","pmids":["28067475"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"finding":"CCT6 (PF3D7_0608700) is a subunit of the native Plasmodium falciparum CCT/TRiC chaperonin complex. Multiple sequence alignment revealed that the conserved ATP hydrolysis motif GDGTT present in most CCT subunits is replaced by GDGSS in CCT6, representing a conservative substitution; the flanking catalytic aspartic acid residues are otherwise conserved, suggesting CCT6 retains ATP-hydrolysis capability but may contribute to heterogeneity in the sequential ATP hydrolysis mechanism of the complex.","method":"Multiple sequence alignment of all PfCCT subunits with identification of conserved ATP-hydrolysis motifs","journal":"FASEB journal : official publication of the Federation of American Societies for Experimental Biology","confidence":"Low","confidence_rationale":"Tier 4 / Weak — computational/sequence analysis only, no in vitro biochemical validation of CCT6 ATPase activity","pmids":["26443825"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2022,"finding":"CCT6 (PF3D7_0608700) is a subunit of the PfCCT complex purified from P. falciparum trophozoites via FLAG-tagged CCT8. The complex co-purifies with actin, tubulin, WD40-domain proteins, and several initiation factors including eIF2α, establishing that CCT6-containing PfCCT functions as a molecular chaperone for these substrates in the parasite cytosol.","method":"Affinity purification (FLAG-SLI tagging of CCT8) followed by proteomic analysis of the PfCCT complex from synchronized trophozoite-stage parasites","journal":"Frontiers in molecular biosciences","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — affinity purification with mass spectrometry from native parasite extract; CCT6 membership in the purified complex established; single lab, no independent replication reported","pmids":["36567946"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2019,"finding":"CCT6 (PF3D7_0608700) was detected as a component of the TRiC/CCT complex that co-immunoprecipitates with the CAF1/CCR4/NOT complex subunit PyCCR4-1 in P. yoelii schizonts, suggesting the TRiC complex (including CCT6) associates with translational regulatory machinery; this interaction was observed at a less stringent SAINT score threshold (0.1–0.35), consistent with a role in inhibiting stress granule formation.","method":"GFP-tagged PyCCR4-1 co-immunoprecipitation followed by mass spectrometry (SAINT scoring) from synchronized P. yoelii schizonts","journal":"PLoS pathogens","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single co-IP/MS experiment, sub-threshold SAINT score for CCT6 specifically, no functional follow-up on CCT6 itself","pmids":["30703164"],"is_preprint":false,"attribution":[{"species":"Plasmodium yoelii","strain":""}]},{"year":2015,"finding":"The PfTRiC chaperonin complex (of which CCT6/PF3D7_0608700 is a subunit) binds to and assists in the export of Maurer's cleft resident proteins (e.g. PfSBP1) as soluble forms in the red blood cell cytoplasm; the N-terminal domain of PfSBP1 was identified as the domain of interaction with PfTRiC.","method":"Co-immunoprecipitation, domain-mapping experiments, and localization studies in P. falciparum-infected erythrocytes","journal":"Traffic (Copenhagen, Denmark)","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab co-IP and domain mapping; CCT6 is one subunit of the complex and its individual contribution is not distinguished; contradicted by Spillman et al. 2017 regarding TRiC export","pmids":["25615740"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"CCT6 (PF3D7_0608700) is a subunit of the cytosolic TRiC/CCT chaperonin complex in Plasmodium falciparum; the complex folds actin, tubulin, WD40-domain proteins, and interacts with eIF2α, is essential for asexual parasite growth, localizes within the parasite (not exported to the host RBC), and CCT6 itself carries a variant ATP-hydrolysis motif (GDGSS instead of GDGTT) whose functional significance has not been directly tested."},"narrative":{"mechanistic_narrative":"CCT6 (PF3D7_0608700) is a subunit of the cytosolic TRiC/CCT chaperonin complex of Plasmodium falciparum, characterized in the available corpus only through its membership in that complex rather than through any activity attributable to CCT6 alone [PMID:28067475, PMID:36567946]. The CCT6-containing PfCCT complex, purified from trophozoite-stage parasites, co-purifies with actin, tubulin, WD40-domain proteins, and translation initiation factors including eIF2α, consistent with a role in folding these cytosolic substrates [PMID:36567946]. The complex resides in the parasite cytosol and is not exported into the host red blood cell, and regulatable knockdown of a sibling TRiC subunit causes severe asexual growth defects without altering protein export, establishing that the complex is essential for parasite growth and functions within the parasite [PMID:28067475]. Sequence alignment shows that CCT6 carries a conservative substitution in the conserved ATP-hydrolysis motif (GDGSS in place of GDGTT) while retaining the flanking catalytic aspartates, a feature that may contribute to heterogeneity in the complex's sequential ATP-hydrolysis cycle [PMID:26443825]. Beyond its role as a complex subunit, no CCT6-specific molecular function, substrate, or loss-of-function phenotype has been directly characterized in the available corpus; findings regarding TRiC substrate binding and any association with translational regulatory machinery apply to the complex, not to CCT6 individually [PMID:30703164, PMID:25615740].","teleology":[{"year":2015,"claim":"Establishing that CCT6 is an authentic subunit of the native parasite chaperonin and noting its divergent catalytic motif framed CCT6 as a potentially specialized component of the sequential ATPase cycle.","evidence":"Multiple sequence alignment of all PfCCT subunits identifying the GDGSS-for-GDGTT substitution in CCT6","pmids":["26443825"],"confidence":"Low","gaps":["Sequence analysis only; no in vitro biochemical validation of CCT6 ATPase activity","Functional consequence of the GDGSS motif untested","Contribution of CCT6 to complex assembly not addressed"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"claim":"An early proposal implicated the PfTRiC complex in chaperoning exported Maurer's cleft proteins, raising the possibility that the chaperonin acts in host-cell protein trafficking.","evidence":"Co-immunoprecipitation and N-terminal domain mapping of PfSBP1 with PfTRiC in infected erythrocytes","pmids":["25615740"],"confidence":"Low","gaps":["CCT6's individual contribution not distinguished from the complex","Subsequently contradicted regarding TRiC export role","No functional demonstration of CCT6 in export"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"claim":"Determining the localization and essentiality of the TRiC complex resolved where it acts, showing it functions inside the parasite cytosol and is required for asexual growth rather than for host-cell protein export.","evidence":"Epitope-tagged transgenic lines, parasite-specific antibody localization, and regulatable knockdown of a sibling TRiC subunit with growth and export readouts","pmids":["28067475"],"confidence":"Medium","gaps":["Phenotype demonstrated by knockdown of a sibling subunit, not CCT6 itself","CCT6 membership inferred from complex studies","Single lab"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2019,"claim":"Detection of the TRiC complex among interactors of the CCR4/NOT deadenylase machinery hinted at a link between the chaperonin and translational/stress-granule regulation.","evidence":"GFP-tagged PyCCR4-1 co-immunoprecipitation with mass spectrometry and SAINT scoring in P. yoelii schizonts","pmids":["30703164"],"confidence":"Low","gaps":["CCT6 detected only at a sub-threshold SAINT score","No functional follow-up on CCT6","Interaction shown in P. yoelii, not P. falciparum"],"attribution":[{"species":"Plasmodium yoelii","strain":""}]},{"year":2022,"claim":"Native purification of the intact complex defined its substrate repertoire, identifying actin, tubulin, WD40-domain proteins, and initiation factors including eIF2α as PfCCT clients.","evidence":"FLAG-SLI affinity purification via CCT8 followed by proteomics from synchronized trophozoites","pmids":["36567946"],"confidence":"Medium","gaps":["Substrates attributed to the complex, not to CCT6 specifically","No direct folding assay for any client","Single lab, no independent replication"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"Whether CCT6 has any function, substrate specificity, or catalytic contribution distinct from its role as a complex subunit remains unknown.","evidence":"","pmids":[],"confidence":"Low","gaps":["No CCT6-specific knockdown or knockout phenotype","GDGSS motif function untested biochemically","No structural model of CCT6 within the parasite complex"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["TRiC/CCT chaperonin complex (PfCCT)"],"partners":["ACTIN","TUBULIN","WD40-DOMAIN PROTEINS","EIF2Α","CCT8 (SIBLING SUBUNIT)","PYCCR4-1 (P. YOELII, SUB-THRESHOLD)","PFSBP1 (COMPLEX-LEVEL, CONTESTED)"],"other_free_text":["CCT6 carries a variant ATP-hydrolysis motif (GDGSS instead of GDGTT) with conserved flanking catalytic aspartates; functional significance untested.","All functional evidence is at the level of the intact PfCCT/TRiC complex; no CCT6-specific loss-of-function or activity has been established.","The TRiC complex is essential for asexual growth and functions within the parasite cytosol, not in host RBC protein export."]}},"prefetch_data":{},"corpus_meta":[{"pmid":"28067475","id":"PMC_28067475","title":"The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol.","date":"2017","source":"Cellular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/28067475","citation_count":51,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"25615740","id":"PMC_25615740","title":"New Export Pathway in Plasmodium falciparum-Infected Erythrocytes: Role of the Parasite Group II Chaperonin, PfTRiC.","date":"2015","source":"Traffic (Copenhagen, Denmark)","url":"https://pubmed.ncbi.nlm.nih.gov/25615740","citation_count":15,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"36567946","id":"","title":"The malaria parasite chaperonin containing TCP-1 (CCT) complex: Data integration with other CCT proteomes.","date":"2022","source":"Frontiers in molecular biosciences","url":"https://pubmed.ncbi.nlm.nih.gov/36567946","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["CCT6"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"30703164","id":"","title":"Plasmodium male gametocyte development and transmission are critically regulated by the two putative deadenylases of the CAF1/CCR4/NOT complex.","date":"2019","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/30703164","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["CCT6"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"26443825","id":"","title":"Plasmodium actin is incompletely folded by heterologous protein-folding machinery and likely requires the native Plasmodium chaperonin complex to enter a mature functional state.","date":"2015","source":"FASEB journal : official publication of the Federation of American Societies for Experimental Biology","url":"https://pubmed.ncbi.nlm.nih.gov/26443825","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["CCT6"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":7152,"output_tokens":1709,"usd":0.023546,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6765,"output_tokens":2580,"usd":0.049162,"stage2_stop_reason":"end_turn"},"total_usd":0.072708,"stage1_batch_id":"msgbatch_01SRp5hyRc82zNjddxyCCXGk","stage2_batch_id":"msgbatch_01K3BTmBazRo3pRrMvyaPMTY","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2017,\n      \"finding\": \"CCT6 (PF3D7_0608700) is a subunit of the Plasmodium TRiC chaperonin complex, which localizes to the parasite cytosol and is not exported into the host red blood cell. Regulatable knockdown of the TRiC-θ subunit (a sibling subunit) caused severe asexual growth defects without altering protein export, indicating the TRiC complex (including CCT6) is essential for parasite biology but functions within the parasite, not in RBC protein trafficking.\",\n      \"method\": \"Epitope-tagged transgenic parasites, parasite-specific antibody localization, regulatable knockdown with growth and export phenotype readouts\",\n      \"journal\": \"Cellular microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization by tagged transgenic lines and antibody, loss-of-function growth phenotype; CCT6 membership in the complex is implicit (complex studied), functional conclusion about the complex applies to CCT6 as a subunit; single lab\",\n      \"pmids\": [\"28067475\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"CCT6 (PF3D7_0608700) is a subunit of the native Plasmodium falciparum CCT/TRiC chaperonin complex. Multiple sequence alignment revealed that the conserved ATP hydrolysis motif GDGTT present in most CCT subunits is replaced by GDGSS in CCT6, representing a conservative substitution; the flanking catalytic aspartic acid residues are otherwise conserved, suggesting CCT6 retains ATP-hydrolysis capability but may contribute to heterogeneity in the sequential ATP hydrolysis mechanism of the complex.\",\n      \"method\": \"Multiple sequence alignment of all PfCCT subunits with identification of conserved ATP-hydrolysis motifs\",\n      \"journal\": \"FASEB journal : official publication of the Federation of American Societies for Experimental Biology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 4 / Weak — computational/sequence analysis only, no in vitro biochemical validation of CCT6 ATPase activity\",\n      \"pmids\": [\"26443825\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"CCT6 (PF3D7_0608700) is a subunit of the PfCCT complex purified from P. falciparum trophozoites via FLAG-tagged CCT8. The complex co-purifies with actin, tubulin, WD40-domain proteins, and several initiation factors including eIF2α, establishing that CCT6-containing PfCCT functions as a molecular chaperone for these substrates in the parasite cytosol.\",\n      \"method\": \"Affinity purification (FLAG-SLI tagging of CCT8) followed by proteomic analysis of the PfCCT complex from synchronized trophozoite-stage parasites\",\n      \"journal\": \"Frontiers in molecular biosciences\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — affinity purification with mass spectrometry from native parasite extract; CCT6 membership in the purified complex established; single lab, no independent replication reported\",\n      \"pmids\": [\"36567946\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"CCT6 (PF3D7_0608700) was detected as a component of the TRiC/CCT complex that co-immunoprecipitates with the CAF1/CCR4/NOT complex subunit PyCCR4-1 in P. yoelii schizonts, suggesting the TRiC complex (including CCT6) associates with translational regulatory machinery; this interaction was observed at a less stringent SAINT score threshold (0.1–0.35), consistent with a role in inhibiting stress granule formation.\",\n      \"method\": \"GFP-tagged PyCCR4-1 co-immunoprecipitation followed by mass spectrometry (SAINT scoring) from synchronized P. yoelii schizonts\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single co-IP/MS experiment, sub-threshold SAINT score for CCT6 specifically, no functional follow-up on CCT6 itself\",\n      \"pmids\": [\"30703164\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium yoelii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"The PfTRiC chaperonin complex (of which CCT6/PF3D7_0608700 is a subunit) binds to and assists in the export of Maurer's cleft resident proteins (e.g. PfSBP1) as soluble forms in the red blood cell cytoplasm; the N-terminal domain of PfSBP1 was identified as the domain of interaction with PfTRiC.\",\n      \"method\": \"Co-immunoprecipitation, domain-mapping experiments, and localization studies in P. falciparum-infected erythrocytes\",\n      \"journal\": \"Traffic (Copenhagen, Denmark)\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab co-IP and domain mapping; CCT6 is one subunit of the complex and its individual contribution is not distinguished; contradicted by Spillman et al. 2017 regarding TRiC export\",\n      \"pmids\": [\"25615740\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"CCT6 (PF3D7_0608700) is a subunit of the cytosolic TRiC/CCT chaperonin complex in Plasmodium falciparum; the complex folds actin, tubulin, WD40-domain proteins, and interacts with eIF2α, is essential for asexual parasite growth, localizes within the parasite (not exported to the host RBC), and CCT6 itself carries a variant ATP-hydrolysis motif (GDGSS instead of GDGTT) whose functional significance has not been directly tested.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"CCT6 (PF3D7_0608700) is a subunit of the cytosolic TRiC/CCT chaperonin complex of Plasmodium falciparum, characterized in the available corpus only through its membership in that complex rather than through any activity attributable to CCT6 alone [#0, #2]. The CCT6-containing PfCCT complex, purified from trophozoite-stage parasites, co-purifies with actin, tubulin, WD40-domain proteins, and translation initiation factors including eIF2\\u03b1, consistent with a role in folding these cytosolic substrates [#2]. The complex resides in the parasite cytosol and is not exported into the host red blood cell, and regulatable knockdown of a sibling TRiC subunit causes severe asexual growth defects without altering protein export, establishing that the complex is essential for parasite growth and functions within the parasite [#0]. Sequence alignment shows that CCT6 carries a conservative substitution in the conserved ATP-hydrolysis motif (GDGSS in place of GDGTT) while retaining the flanking catalytic aspartates, a feature that may contribute to heterogeneity in the complex's sequential ATP-hydrolysis cycle [#1]. Beyond its role as a complex subunit, no CCT6-specific molecular function, substrate, or loss-of-function phenotype has been directly characterized in the available corpus; findings regarding TRiC substrate binding and any association with translational regulatory machinery apply to the complex, not to CCT6 individually [#3, #4].\",\n  \"teleology\": [\n    {\n      \"year\": 2015,\n      \"claim\": \"Establishing that CCT6 is an authentic subunit of the native parasite chaperonin and noting its divergent catalytic motif framed CCT6 as a potentially specialized component of the sequential ATPase cycle.\",\n      \"evidence\": \"Multiple sequence alignment of all PfCCT subunits identifying the GDGSS-for-GDGTT substitution in CCT6\",\n      \"pmids\": [\"26443825\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Sequence analysis only; no in vitro biochemical validation of CCT6 ATPase activity\", \"Functional consequence of the GDGSS motif untested\", \"Contribution of CCT6 to complex assembly not addressed\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"An early proposal implicated the PfTRiC complex in chaperoning exported Maurer's cleft proteins, raising the possibility that the chaperonin acts in host-cell protein trafficking.\",\n      \"evidence\": \"Co-immunoprecipitation and N-terminal domain mapping of PfSBP1 with PfTRiC in infected erythrocytes\",\n      \"pmids\": [\"25615740\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"CCT6's individual contribution not distinguished from the complex\", \"Subsequently contradicted regarding TRiC export role\", \"No functional demonstration of CCT6 in export\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Determining the localization and essentiality of the TRiC complex resolved where it acts, showing it functions inside the parasite cytosol and is required for asexual growth rather than for host-cell protein export.\",\n      \"evidence\": \"Epitope-tagged transgenic lines, parasite-specific antibody localization, and regulatable knockdown of a sibling TRiC subunit with growth and export readouts\",\n      \"pmids\": [\"28067475\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Phenotype demonstrated by knockdown of a sibling subunit, not CCT6 itself\", \"CCT6 membership inferred from complex studies\", \"Single lab\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Detection of the TRiC complex among interactors of the CCR4/NOT deadenylase machinery hinted at a link between the chaperonin and translational/stress-granule regulation.\",\n      \"evidence\": \"GFP-tagged PyCCR4-1 co-immunoprecipitation with mass spectrometry and SAINT scoring in P. yoelii schizonts\",\n      \"pmids\": [\"30703164\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"CCT6 detected only at a sub-threshold SAINT score\", \"No functional follow-up on CCT6\", \"Interaction shown in P. yoelii, not P. falciparum\"],\n      \"attribution\": [{\"species\": \"Plasmodium yoelii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Native purification of the intact complex defined its substrate repertoire, identifying actin, tubulin, WD40-domain proteins, and initiation factors including eIF2\\u03b1 as PfCCT clients.\",\n      \"evidence\": \"FLAG-SLI affinity purification via CCT8 followed by proteomics from synchronized trophozoites\",\n      \"pmids\": [\"36567946\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Substrates attributed to the complex, not to CCT6 specifically\", \"No direct folding assay for any client\", \"Single lab, no independent replication\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Whether CCT6 has any function, substrate specificity, or catalytic contribution distinct from its role as a complex subunit remains unknown.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No CCT6-specific knockdown or knockout phenotype\", \"GDGSS motif function untested biochemically\", \"No structural model of CCT6 within the parasite complex\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0140662\", \"supporting_discovery_ids\": [0, 2]},\n      {\"term_id\": \"GO:0016887\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [0, 2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006457\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"complexes\": [\"TRiC/CCT chaperonin complex (PfCCT)\"],\n    \"partners\": [\"actin\", \"tubulin\", \"WD40-domain proteins\", \"eIF2\\u03b1\", \"CCT8 (sibling subunit)\", \"PyCCR4-1 (P. yoelii, sub-threshold)\", \"PfSBP1 (complex-level, contested)\"],\n    \"other_free_text\": [\n      \"CCT6 carries a variant ATP-hydrolysis motif (GDGSS instead of GDGTT) with conserved flanking catalytic aspartates; functional significance untested.\",\n      \"All functional evidence is at the level of the intact PfCCT/TRiC complex; no CCT6-specific loss-of-function or activity has been established.\",\n      \"The TRiC complex is essential for asexual growth and functions within the parasite cytosol, not in host RBC protein export.\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0608700","name":null,"product":"T-complex protein 1 subunit zeta","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0107300","name":null,"product":"T-complex protein 1 subunit zeta, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1141500","name":null,"product":"T-complex protein 1 subunit zeta, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"CCT6","evaluation":null}