##gff-version 3 I3LM39 UniProtKB Chain 1 495 . . . ID=PRO_0000423063;Note=Cyclic GMP-AMP synthase I3LM39 UniProtKB Region 1 134 . . . Note=DNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Region 1 128 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite I3LM39 UniProtKB Region 57 68 . . . Note=Required for association with the cell membrane;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Region 103 134 . . . Note=Required for activation upon DNA viral infection;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Region 147 190 . . . Note=DNA-binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Region 316 357 . . . Note=Interaction with collided ribosomes;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Region 359 382 . . . Note=DNA-binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Motif 143 148 . . . Note=Nuclear export signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Motif 268 278 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Compositional bias 48 75 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite I3LM39 UniProtKB Binding site 186 186 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Binding site 188 188 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Binding site 200 200 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Binding site 202 202 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Binding site 202 202 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Binding site 294 294 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Binding site 294 294 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Binding site 294 294 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Binding site 337 337 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Binding site 351 358 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Binding site 351 351 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Binding site 358 358 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Binding site 365 365 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Binding site 371 371 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Binding site 372 372 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Binding site 379 379 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Binding site 389 389 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Binding site 410 414 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Site 230 230 . . . Note=Arginine-anchor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Site 294 295 . . . Note=Cleavage%3B by CASP3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Modified residue 7 7 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Modified residue 13 13 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Modified residue 56 56 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Modified residue 57 57 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Modified residue 165 165 . . . Note=PolyADP-ribosyl glutamic acid;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8C6L5 I3LM39 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Modified residue 190 190 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Modified residue 261 261 . . . Note=5-glutamyl polyglutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8C6L5 I3LM39 UniProtKB Modified residue 278 278 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Modified residue 359 359 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Modified residue 369 369 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Modified residue 389 389 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Modified residue 410 410 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Modified residue 481 481 . . . Note=N6-methyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Lipidation 379 379 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Lipidation 380 380 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Lipidation 449 449 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Cross-link 206 206 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8C6L5 I3LM39 UniProtKB Cross-link 260 260 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8C6L5 I3LM39 UniProtKB Cross-link 322 322 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8C6L5 I3LM39 UniProtKB Cross-link 322 322 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8C6L5 I3LM39 UniProtKB Cross-link 359 359 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8C6L5 I3LM39 UniProtKB Cross-link 359 359 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Cross-link 369 369 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8C6L5 I3LM39 UniProtKB Cross-link 386 386 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Cross-link 389 389 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N884 I3LM39 UniProtKB Mutagenesis 200 200 . . . Note=Abolishes enzyme activity and stimulation of interferon production%3B when associated with N-202. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Mutagenesis 202 202 . . . Note=Abolishes enzyme activity and stimulation of interferon production%3B when associated with Q-200. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23722159;Dbxref=PMID:23722159 I3LM39 UniProtKB Helix 139 147 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Helix 150 173 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Turn 177 180 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Beta strand 182 184 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Turn 188 192 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLZ I3LM39 UniProtKB Beta strand 200 208 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Beta strand 213 217 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Beta strand 221 227 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Helix 238 240 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Helix 248 262 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Beta strand 269 271 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Beta strand 281 285 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Beta strand 287 289 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Beta strand 291 301 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Helix 307 309 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Turn 316 319 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Helix 321 328 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Beta strand 332 335 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Beta strand 339 344 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLZ I3LM39 UniProtKB Helix 346 348 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Beta strand 350 353 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Helix 355 363 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Beta strand 366 368 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLZ I3LM39 UniProtKB Turn 369 372 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Helix 381 398 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Turn 399 401 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Turn 404 407 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Helix 410 423 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Helix 427 429 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Helix 432 434 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Helix 435 452 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Turn 468 470 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Helix 473 488 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX I3LM39 UniProtKB Helix 492 494 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JLX