##gff-version 3 Q8VSC3 UniProtKB Chain 1 545 . . . ID=PRO_0000395755;Note=E3 ubiquitin-protein ligase ipaH9.8 Q8VSC3 UniProtKB Repeat 57 77 . . . Note=LRR 1 Q8VSC3 UniProtKB Repeat 78 99 . . . Note=LRR 2 Q8VSC3 UniProtKB Repeat 100 117 . . . Note=LRR 3 Q8VSC3 UniProtKB Repeat 118 139 . . . Note=LRR 4 Q8VSC3 UniProtKB Repeat 140 157 . . . Note=LRR 5 Q8VSC3 UniProtKB Repeat 158 179 . . . Note=LRR 6 Q8VSC3 UniProtKB Repeat 182 203 . . . Note=LRR 7 Q8VSC3 UniProtKB Repeat 205 228 . . . Note=LRR 8 Q8VSC3 UniProtKB Domain 261 471 . . . Note=NEL;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q8VSC3 UniProtKB Region 1 242 . . . Note=Interaction with target proteins;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0CE12 Q8VSC3 UniProtKB Region 243 250 . . . Note=Linker;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0CE12 Q8VSC3 UniProtKB Region 251 545 . . . Note=E3 ubiquitin-protein ligase catalytic domain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0CE12 Q8VSC3 UniProtKB Active site 337 337 . . . Note=Glycyl thioester intermediate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24248594,ECO:0000269|PubMed:29144452;Dbxref=PMID:24248594,PMID:29144452 Q8VSC3 UniProtKB Site 166 166 . . . Note=Sensor for substrate-binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33303953;Dbxref=PMID:33303953 Q8VSC3 UniProtKB Site 187 187 . . . Note=Sensor for substrate-binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33303953;Dbxref=PMID:33303953 Q8VSC3 UniProtKB Natural variant 222 222 . . . Note=In plasmid pWR100%2C plasmid pWR501%2C plasmid pSF5 and plasmid pINV_F6_M1382. P->Q Q8VSC3 UniProtKB Natural variant 474 474 . . . Note=In plasmid pINV_F6_M1382. Q->L Q8VSC3 UniProtKB Natural variant 536 536 . . . Note=In plasmid pWR100 and plasmid pWR501. P->F Q8VSC3 UniProtKB Natural variant 536 536 . . . Note=In plasmid pSF5. P->S Q8VSC3 UniProtKB Mutagenesis 50 50 . . . Note=Abolished ability to bind and ubiquitinate host GBP1%3B when associated with A-62 and A-83. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 Q8VSC3 UniProtKB Mutagenesis 62 62 . . . Note=Abolished ability to bind and ubiquitinate host GBP1%3B when associated with A-50 and A-83. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 Q8VSC3 UniProtKB Mutagenesis 83 83 . . . Note=Abolished ability to bind and ubiquitinate host GBP1%3B when associated with A-50 and A-62. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 Q8VSC3 UniProtKB Mutagenesis 86 88 . . . Note=Decreased ability to ubiquitinate host GBP1. YNQ->ANA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31216343;Dbxref=PMID:31216343 Q8VSC3 UniProtKB Mutagenesis 126 126 . . . Note=Decreased ability to ubiquitinate host GBP1%3B when associated with A-146. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31216343;Dbxref=PMID:31216343 Q8VSC3 UniProtKB Mutagenesis 146 146 . . . Note=Decreased ability to ubiquitinate host GBP1%3B when associated with A-126 or A-190. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31216343;Dbxref=PMID:31216343 Q8VSC3 UniProtKB Mutagenesis 163 163 . . . Note=Abolishes proteasomal degradation of host proteins%3B when associated with A-187 and A-210. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24248594;Dbxref=PMID:24248594 Q8VSC3 UniProtKB Mutagenesis 166 166 . . . Note=Strongly reduced ability to ubiquitinate host GBP1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33303953;Dbxref=PMID:33303953 Q8VSC3 UniProtKB Mutagenesis 187 187 . . . Note=Abolishes proteasomal degradation of host proteins%3B when associated with A-163 and A-210. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24248594;Dbxref=PMID:24248594 Q8VSC3 UniProtKB Mutagenesis 190 190 . . . Note=Decreased ability to ubiquitinate host GBP1%3B when associated with A-146. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31216343;Dbxref=PMID:31216343 Q8VSC3 UniProtKB Mutagenesis 196 196 . . . Note=Does not affect autoinhibition in absence of substrate. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33303953;Dbxref=PMID:33303953 Q8VSC3 UniProtKB Mutagenesis 196 196 . . . Note=Reduced autoinhibition in absence of substrate. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33303953;Dbxref=PMID:33303953 Q8VSC3 UniProtKB Mutagenesis 198 198 . . . Note=Does not affect autoinhibition in absence of substrate. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33303953;Dbxref=PMID:33303953 Q8VSC3 UniProtKB Mutagenesis 210 210 . . . Note=Abolishes proteasomal degradation of host proteins%3B when associated with A-163 and A-187. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24248594;Dbxref=PMID:24248594 Q8VSC3 UniProtKB Mutagenesis 211 211 . . . Note=Slightly reduced autoinhibition in absence of substrate. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33303953;Dbxref=PMID:33303953 Q8VSC3 UniProtKB Mutagenesis 216 216 . . . Note=Slightly reduced autoinhibition in absence of substrate. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33303953;Dbxref=PMID:33303953 Q8VSC3 UniProtKB Mutagenesis 219 219 . . . Note=Does not affect autoinhibition in absence of substrate. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33303953;Dbxref=PMID:33303953 Q8VSC3 UniProtKB Mutagenesis 337 337 . . . Note=Abolishes E3 ubiquitin ligase activity and proteasomal degradation of host proteins. C->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18005683,ECO:0000269|PubMed:18997778,ECO:0000269|PubMed:20010814,ECO:0000269|PubMed:24248594,ECO:0000269|PubMed:29144452,ECO:0000269|PubMed:31216343;Dbxref=PMID:18005683,PMID:18997778,PMID:20010814,PMID:24248594,PMID:29144452,PMID:31216343 Q8VSC3 UniProtKB Mutagenesis 338 338 . . . Note=Does not affect E3 ubiquitin ligase activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18997778;Dbxref=PMID:18997778 Q8VSC3 UniProtKB Mutagenesis 339 339 . . . Note=Abolishes E3 ubiquitin ligase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18997778;Dbxref=PMID:18997778 Q8VSC3 UniProtKB Mutagenesis 340 340 . . . Note=Reduced E3 ubiquitin ligase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18997778;Dbxref=PMID:18997778 Q8VSC3 UniProtKB Mutagenesis 387 387 . . . Note=Does not affect E3 ubiquitin ligase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18997778;Dbxref=PMID:18997778 Q8VSC3 UniProtKB Mutagenesis 395 395 . . . Note=Does not affect autoinhibition in absence of substrate. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33303953;Dbxref=PMID:33303953 Q8VSC3 UniProtKB Mutagenesis 395 395 . . . Note=Reduced autoinhibition in absence of substrate. F->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33303953;Dbxref=PMID:33303953 Q8VSC3 UniProtKB Mutagenesis 397 397 . . . Note=Abolishes E3 ubiquitin ligase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18997778;Dbxref=PMID:18997778 Q8VSC3 UniProtKB Sequence conflict 7 7 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8VSC3 UniProtKB Helix 23 35 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B0N Q8VSC3 UniProtKB Helix 43 55 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B0N Q8VSC3 UniProtKB Beta strand 59 62 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B0N Q8VSC3 UniProtKB Beta strand 80 83 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B0N Q8VSC3 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B0N Q8VSC3 UniProtKB Beta strand 121 123 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B0N Q8VSC3 UniProtKB Beta strand 141 143 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B0N Q8VSC3 UniProtKB Beta strand 161 163 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B0N Q8VSC3 UniProtKB Beta strand 185 187 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B0N Q8VSC3 UniProtKB Helix 198 201 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B0N Q8VSC3 UniProtKB Beta strand 208 210 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B0N Q8VSC3 UniProtKB Helix 220 229 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B0N Q8VSC3 UniProtKB Beta strand 237 239 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B0N Q8VSC3 UniProtKB Helix 254 259 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L3P Q8VSC3 UniProtKB Helix 264 273 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L3P Q8VSC3 UniProtKB Helix 274 276 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L3P Q8VSC3 UniProtKB Helix 283 293 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L3P Q8VSC3 UniProtKB Helix 305 318 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L3P Q8VSC3 UniProtKB Helix 320 359 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L3P Q8VSC3 UniProtKB Helix 366 386 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L3P Q8VSC3 UniProtKB Turn 387 389 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L3P Q8VSC3 UniProtKB Helix 400 408 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L3P Q8VSC3 UniProtKB Turn 409 414 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L3P Q8VSC3 UniProtKB Helix 434 448 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L3P Q8VSC3 UniProtKB Helix 451 455 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L3P Q8VSC3 UniProtKB Helix 458 466 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L3P Q8VSC3 UniProtKB Helix 469 484 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L3P Q8VSC3 UniProtKB Helix 486 498 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L3P Q8VSC3 UniProtKB Helix 504 530 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L3P