{"gene":"TG_233200","gene_symbol":"URM1","run_date":"2026-09-08T12:58:24","timeline":{"discoveries":[{"year":2022,"finding":"TgURM1 localizes to the tachyzoite cytoplasm and functions as a ubiquitin-like modifier (urmylation); mutations of its C-terminal glycine-glycine motif block the urmylation process, establishing this motif as essential for conjugation activity.","method":"Subcellular localization (imaging), site-directed mutagenesis of C-terminal GG motif, urmylation assay","journal":"Microbiology spectrum","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct mutagenesis of functional motif plus localization, single lab with two orthogonal methods","pmids":["35323018"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"finding":"Urmylation (TgURM1 conjugation to target proteins) is significantly induced by oxidative stress conditions in T. gondii.","method":"Urmylation assay under oxidative stress, western blot","journal":"Microbiology spectrum","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — biochemical conjugation assay combined with oxidative stress treatment, single lab","pmids":["35323018"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"finding":"TgAHP1 (alkyl hydroperoxide reductase) was identified as a substrate/binding partner of TgURM1 under oxidative stress conditions, establishing TgAHP1 as an urmylation target involved in the oxidative stress response.","method":"Proximity-based protein labeling (BioID/TurboID) combined with proteomics, interaction confirmed under oxidative stress","journal":"Microbiology spectrum","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — proximity labeling + proteomics, single lab, oxidative-stress-dependent interaction","pmids":["35323018"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"finding":"TgURM1 knockout results in significant reduction of parasite invasion, replication, and virulence in mice, and the knockout strain is intolerant to oxidative stress, establishing TgURM1 as required for oxidative stress response and parasite fitness.","method":"Genetic knockout (CRISPR/Cas9), invasion/replication assays, mouse virulence model, oxidative stress tolerance assay","journal":"Microbiology spectrum","confidence":"High","confidence_rationale":"Tier 2 / Strong — CRISPR knockout with multiple orthogonal phenotypic readouts (invasion, replication, virulence, stress tolerance) in a single rigorous study","pmids":["35323018"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"finding":"TgUba1 is the ubiquitin-like activating enzyme (E1-like protein) for TgUrm1; it localizes to the cytoplasm, contains an E1-like activating domain (AD) essential for interaction with TgUrm1, and its deletion significantly reduces TgUrm1 conjugate formation under oxidative stress.","method":"Domain mapping, co-interaction assay (AD domain deletion), CRISPR/Cas9 knockout, urmylation assay under oxidative stress","journal":"International journal of molecular sciences","confidence":"High","confidence_rationale":"Tier 2 / Strong — domain-level interaction mapping, CRISPR knockout, and functional urmylation assay in a single study with multiple orthogonal methods","pmids":["36142209"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"finding":"TgUba1 knockout attenuates parasite proliferation and virulence but does not affect invasion or egress, placing TgUba1 (and by extension TgUrm1 activation) specifically in the proliferation/survival pathway.","method":"CRISPR/Cas9 knockout, proliferation assay, invasion/egress assays, mouse virulence model","journal":"International journal of molecular sciences","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — CRISPR knockout with multiple phenotypic readouts, single lab","pmids":["36142209"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"finding":"Deletion of TgUrm1 in the type II Pru strain (PruΔUrm1) significantly reduces in vitro invasion and proliferation, confirming that TgUrm1 is required for these parasite processes in a type II genetic background.","method":"CRISPR/Cas9 knockout, in vitro invasion assay, proliferation assay","journal":"Vaccine","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — CRISPR knockout with two orthogonal cellular assays, single lab, replicates findings in a second strain","pmids":["39705796"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":"Pru"}]}],"current_model":"TgURM1 is a cytoplasmic ubiquitin-like modifier (UBL) in Toxoplasma gondii whose conjugation activity (urmylation) requires its C-terminal GG motif and is activated by the E1-like enzyme TgUba1 (via its AD domain); urmylation is strongly induced by oxidative stress and targets TgAHP1 (alkyl hydroperoxide reductase), thereby mediating antioxidant defense, while TgURM1 loss impairs parasite invasion, replication, and virulence."},"narrative":{"mechanistic_narrative":"TgURM1 is a cytoplasmic ubiquitin-like modifier in Toxoplasma gondii that mediates antioxidant defense through protein conjugation (urmylation), a process essential for parasite fitness and virulence [PMID:35323018]. Its C-terminal glycine-glycine motif is required for conjugation to target proteins, and urmylation is strongly induced by oxidative stress [PMID:35323018]. Activation depends on the E1-like enzyme TgUba1, whose activating (AD) domain is required for interaction with TgURM1 and for conjugate formation under oxidative stress [PMID:36142209]. Under oxidative stress TgURM1 conjugates the alkyl hydroperoxide reductase TgAHP1, linking urmylation to the parasite's oxidative stress response [PMID:35323018]. Loss of TgURM1 impairs invasion, replication, oxidative stress tolerance, and virulence, with reduced invasion and proliferation confirmed in the type II Pru strain [PMID:35323018, PMID:39705796]. No further mechanistic detail on the urmylation cascade beyond these findings has been characterized in the available corpus.","teleology":[{"year":2022,"claim":"Establishing that TgURM1 is a functional ubiquitin-like modifier defined where its conjugation activity resides and where it acts in the parasite.","evidence":"Cytoplasmic imaging plus site-directed mutagenesis of the C-terminal GG motif with an urmylation assay in T. gondii tachyzoites","pmids":["35323018"],"confidence":"Medium","gaps":["Does not identify the ligase or downstream deconjugating machinery","GG-motif requirement shown by mutagenesis but conjugation chemistry not structurally resolved"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"claim":"Linking urmylation to oxidative stress and identifying TgAHP1 as a target answered what physiological trigger drives conjugation and which substrate connects it to redox defense.","evidence":"Urmylation/western blot assays under oxidative stress and proximity labeling (BioID/TurboID) proteomics in T. gondii","pmids":["35323018"],"confidence":"Medium","gaps":["TgAHP1 identified by proximity labeling without reciprocal validation of the modification site","Functional consequence of TgAHP1 urmylation on its reductase activity not measured"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"claim":"Knockout of TgURM1 established that urmylation is required for parasite fitness rather than dispensable, tying the pathway to invasion, replication, stress tolerance, and virulence.","evidence":"CRISPR/Cas9 knockout with invasion, replication, oxidative stress tolerance assays and a mouse virulence model","pmids":["35323018"],"confidence":"High","gaps":["Does not resolve which downstream targets mediate each phenotype","Strain background of the initial knockout not specified in attribution"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"claim":"Identifying TgUba1 as the E1-like activating enzyme filled in the upstream activation step of the urmylation cascade.","evidence":"Domain mapping and AD-domain deletion interaction assay, CRISPR/Cas9 knockout, and urmylation assay under oxidative stress in T. gondii","pmids":["36142209"],"confidence":"High","gaps":["Downstream carrier/ligase equivalents not identified","Direct thioester intermediate chemistry not demonstrated"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"claim":"Phenotyping the TgUba1 knockout distinguished which parasite processes depend on urmylation activation, placing it in proliferation/survival rather than invasion or egress.","evidence":"CRISPR/Cas9 knockout with proliferation, invasion, egress assays and a mouse virulence model","pmids":["36142209"],"confidence":"Medium","gaps":["Discrepancy with TgURM1 knockout invasion defect not reconciled","Single lab, single strain background"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"claim":"Deleting TgURM1 in a second, type II genetic background tested whether the fitness requirement generalizes beyond the original strain.","evidence":"CRISPR/Cas9 knockout in the Pru strain with in vitro invasion and proliferation assays","pmids":["39705796"],"confidence":"Medium","gaps":["Oxidative stress and in vivo virulence not re-tested in this background","Substrate-level mechanism in Pru not examined"],"attribution":[{"species":"Toxoplasma gondii","strain":"Pru"}]},{"year":null,"claim":"The full urmylation enzymatic cascade downstream of TgUba1 and the broader substrate repertoire beyond TgAHP1 remain undefined.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No E2/E3-equivalent carrier or ligase identified","Substrate repertoire beyond TgAHP1 uncharacterized","Structural basis of GG-motif conjugation not determined"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":["TGUBA1 (E1-LIKE ACTIVATING ENZYME, AD DOMAIN REQUIRED FOR INTERACTION)","TGAHP1 (ALKYL HYDROPEROXIDE REDUCTASE, URMYLATION SUBSTRATE UNDER OXIDATIVE STRESS)"],"other_free_text":["C-terminal glycine-glycine motif is essential for conjugation activity [#0]","Urmylation is oxidative-stress inducible [#1]","TgURM1 loss impairs invasion, replication, oxidative stress tolerance, and virulence [#3]; requirement confirmed in type II Pru strain [#6]"]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"35323018","id":"PMC_35323018","title":"Involvement of Urm1, a Ubiquitin-Like Protein, in the Regulation of Oxidative Stress Response of Toxoplasma gondii.","date":"2022","source":"Microbiology spectrum","url":"https://pubmed.ncbi.nlm.nih.gov/35323018","citation_count":13,"is_preprint":false},{"pmid":"36142209","id":"PMC_36142209","title":"Uba1: A Potential Ubiquitin-like Activator Protein of Urm1 in Toxoplasma gondii.","date":"2022","source":"International journal of molecular sciences","url":"https://pubmed.ncbi.nlm.nih.gov/36142209","citation_count":4,"is_preprint":false},{"pmid":"39705796","id":"PMC_39705796","title":"Evaluation of the toxoplasma Urm1 gene deletion mutant (PruΔUrm1) as a promising vaccine candidate against toxoplasmosis in mice.","date":"2024","source":"Vaccine","url":"https://pubmed.ncbi.nlm.nih.gov/39705796","citation_count":3,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":4157,"output_tokens":1693,"usd":0.018933,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6916,"output_tokens":2632,"usd":0.05019,"stage2_stop_reason":"end_turn"},"total_usd":0.069123,"stage1_batch_id":"msgbatch_01TEPNZ4MCzJ7xtsNwosiDRk","stage2_batch_id":"msgbatch_01FQShM7n1sfCr4pWTDShmki","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2022,\n      \"finding\": \"TgURM1 localizes to the tachyzoite cytoplasm and functions as a ubiquitin-like modifier (urmylation); mutations of its C-terminal glycine-glycine motif block the urmylation process, establishing this motif as essential for conjugation activity.\",\n      \"method\": \"Subcellular localization (imaging), site-directed mutagenesis of C-terminal GG motif, urmylation assay\",\n      \"journal\": \"Microbiology spectrum\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct mutagenesis of functional motif plus localization, single lab with two orthogonal methods\",\n      \"pmids\": [\"35323018\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"Urmylation (TgURM1 conjugation to target proteins) is significantly induced by oxidative stress conditions in T. gondii.\",\n      \"method\": \"Urmylation assay under oxidative stress, western blot\",\n      \"journal\": \"Microbiology spectrum\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — biochemical conjugation assay combined with oxidative stress treatment, single lab\",\n      \"pmids\": [\"35323018\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"TgAHP1 (alkyl hydroperoxide reductase) was identified as a substrate/binding partner of TgURM1 under oxidative stress conditions, establishing TgAHP1 as an urmylation target involved in the oxidative stress response.\",\n      \"method\": \"Proximity-based protein labeling (BioID/TurboID) combined with proteomics, interaction confirmed under oxidative stress\",\n      \"journal\": \"Microbiology spectrum\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — proximity labeling + proteomics, single lab, oxidative-stress-dependent interaction\",\n      \"pmids\": [\"35323018\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"TgURM1 knockout results in significant reduction of parasite invasion, replication, and virulence in mice, and the knockout strain is intolerant to oxidative stress, establishing TgURM1 as required for oxidative stress response and parasite fitness.\",\n      \"method\": \"Genetic knockout (CRISPR/Cas9), invasion/replication assays, mouse virulence model, oxidative stress tolerance assay\",\n      \"journal\": \"Microbiology spectrum\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — CRISPR knockout with multiple orthogonal phenotypic readouts (invasion, replication, virulence, stress tolerance) in a single rigorous study\",\n      \"pmids\": [\"35323018\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"TgUba1 is the ubiquitin-like activating enzyme (E1-like protein) for TgUrm1; it localizes to the cytoplasm, contains an E1-like activating domain (AD) essential for interaction with TgUrm1, and its deletion significantly reduces TgUrm1 conjugate formation under oxidative stress.\",\n      \"method\": \"Domain mapping, co-interaction assay (AD domain deletion), CRISPR/Cas9 knockout, urmylation assay under oxidative stress\",\n      \"journal\": \"International journal of molecular sciences\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — domain-level interaction mapping, CRISPR knockout, and functional urmylation assay in a single study with multiple orthogonal methods\",\n      \"pmids\": [\"36142209\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"TgUba1 knockout attenuates parasite proliferation and virulence but does not affect invasion or egress, placing TgUba1 (and by extension TgUrm1 activation) specifically in the proliferation/survival pathway.\",\n      \"method\": \"CRISPR/Cas9 knockout, proliferation assay, invasion/egress assays, mouse virulence model\",\n      \"journal\": \"International journal of molecular sciences\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — CRISPR knockout with multiple phenotypic readouts, single lab\",\n      \"pmids\": [\"36142209\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"Deletion of TgUrm1 in the type II Pru strain (PruΔUrm1) significantly reduces in vitro invasion and proliferation, confirming that TgUrm1 is required for these parasite processes in a type II genetic background.\",\n      \"method\": \"CRISPR/Cas9 knockout, in vitro invasion assay, proliferation assay\",\n      \"journal\": \"Vaccine\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — CRISPR knockout with two orthogonal cellular assays, single lab, replicates findings in a second strain\",\n      \"pmids\": [\"39705796\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"Pru\"}]\n    }\n  ],\n  \"current_model\": \"TgURM1 is a cytoplasmic ubiquitin-like modifier (UBL) in Toxoplasma gondii whose conjugation activity (urmylation) requires its C-terminal GG motif and is activated by the E1-like enzyme TgUba1 (via its AD domain); urmylation is strongly induced by oxidative stress and targets TgAHP1 (alkyl hydroperoxide reductase), thereby mediating antioxidant defense, while TgURM1 loss impairs parasite invasion, replication, and virulence.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"TgURM1 is a cytoplasmic ubiquitin-like modifier in Toxoplasma gondii that mediates antioxidant defense through protein conjugation (urmylation), a process essential for parasite fitness and virulence [#0, #3]. Its C-terminal glycine-glycine motif is required for conjugation to target proteins, and urmylation is strongly induced by oxidative stress [#0, #1]. Activation depends on the E1-like enzyme TgUba1, whose activating (AD) domain is required for interaction with TgURM1 and for conjugate formation under oxidative stress [#4]. Under oxidative stress TgURM1 conjugates the alkyl hydroperoxide reductase TgAHP1, linking urmylation to the parasite's oxidative stress response [#2]. Loss of TgURM1 impairs invasion, replication, oxidative stress tolerance, and virulence, with reduced invasion and proliferation confirmed in the type II Pru strain [#3, #6]. No further mechanistic detail on the urmylation cascade beyond these findings has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2022,\n      \"claim\": \"Establishing that TgURM1 is a functional ubiquitin-like modifier defined where its conjugation activity resides and where it acts in the parasite.\",\n      \"evidence\": \"Cytoplasmic imaging plus site-directed mutagenesis of the C-terminal GG motif with an urmylation assay in T. gondii tachyzoites\",\n      \"pmids\": [\"35323018\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Does not identify the ligase or downstream deconjugating machinery\", \"GG-motif requirement shown by mutagenesis but conjugation chemistry not structurally resolved\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Linking urmylation to oxidative stress and identifying TgAHP1 as a target answered what physiological trigger drives conjugation and which substrate connects it to redox defense.\",\n      \"evidence\": \"Urmylation/western blot assays under oxidative stress and proximity labeling (BioID/TurboID) proteomics in T. gondii\",\n      \"pmids\": [\"35323018\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"TgAHP1 identified by proximity labeling without reciprocal validation of the modification site\", \"Functional consequence of TgAHP1 urmylation on its reductase activity not measured\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Knockout of TgURM1 established that urmylation is required for parasite fitness rather than dispensable, tying the pathway to invasion, replication, stress tolerance, and virulence.\",\n      \"evidence\": \"CRISPR/Cas9 knockout with invasion, replication, oxidative stress tolerance assays and a mouse virulence model\",\n      \"pmids\": [\"35323018\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not resolve which downstream targets mediate each phenotype\", \"Strain background of the initial knockout not specified in attribution\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Identifying TgUba1 as the E1-like activating enzyme filled in the upstream activation step of the urmylation cascade.\",\n      \"evidence\": \"Domain mapping and AD-domain deletion interaction assay, CRISPR/Cas9 knockout, and urmylation assay under oxidative stress in T. gondii\",\n      \"pmids\": [\"36142209\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Downstream carrier/ligase equivalents not identified\", \"Direct thioester intermediate chemistry not demonstrated\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Phenotyping the TgUba1 knockout distinguished which parasite processes depend on urmylation activation, placing it in proliferation/survival rather than invasion or egress.\",\n      \"evidence\": \"CRISPR/Cas9 knockout with proliferation, invasion, egress assays and a mouse virulence model\",\n      \"pmids\": [\"36142209\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Discrepancy with TgURM1 knockout invasion defect not reconciled\", \"Single lab, single strain background\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Deleting TgURM1 in a second, type II genetic background tested whether the fitness requirement generalizes beyond the original strain.\",\n      \"evidence\": \"CRISPR/Cas9 knockout in the Pru strain with in vitro invasion and proliferation assays\",\n      \"pmids\": [\"39705796\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Oxidative stress and in vivo virulence not re-tested in this background\", \"Substrate-level mechanism in Pru not examined\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"Pru\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The full urmylation enzymatic cascade downstream of TgUba1 and the broader substrate repertoire beyond TgAHP1 remain undefined.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No E2/E3-equivalent carrier or ligase identified\", \"Substrate repertoire beyond TgAHP1 uncharacterized\", \"Structural basis of GG-motif conjugation not determined\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0031386\", \"supporting_discovery_ids\": [0, 1, 2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0032446\", \"supporting_discovery_ids\": [0, 2, 4], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005737\", \"supporting_discovery_ids\": [0, 4], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006979\", \"supporting_discovery_ids\": [1, 2, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\n      \"TgUba1 (E1-like activating enzyme, AD domain required for interaction)\",\n      \"TgAHP1 (alkyl hydroperoxide reductase, urmylation substrate under oxidative stress)\"\n    ],\n    \"other_free_text\": [\n      \"C-terminal glycine-glycine motif is essential for conjugation activity [#0]\",\n      \"Urmylation is oxidative-stress inducible [#1]\",\n      \"TgURM1 loss impairs invasion, replication, oxidative stress tolerance, and virulence [#3]; requirement confirmed in type II Pru strain [#6]\"\n    ]\n  },\n  \"strain_conflicts\": []\n}","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_233200","name":"URM1","product":"ubiquitin-like protein URM1","uniprot_acc":"A0A125YVW0","chromosome":"TGME49_chrVIII","start_pos":2494730},{"strain":"GT1","gene_id":"TGGT1_233200","name":null,"product":"ubiquitin related modifier protein","uniprot_acc":null,"chromosome":"TGGT1_chrVIII","start_pos":2490651},{"strain":"RH88","gene_id":"TGRH88_077190","name":null,"product":"ubiquitin related modifier protein","uniprot_acc":null,"chromosome":"CM023089","start_pos":7600952},{"strain":"VEG","gene_id":"TGVEG_233200","name":null,"product":"ubiquitin related modifier protein","uniprot_acc":"B6KK06","chromosome":"TGVEG_chrVIII","start_pos":2503375}]}