##gff-version 3 Q71SP7 UniProtKB Chain 1 2513 . . . ID=PRO_0000180274;Note=Fatty acid synthase Q71SP7 UniProtKB Domain 1 406 . . . Note=Ketosynthase family 3 (KS3);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01348 Q71SP7 UniProtKB Domain 845 1107 . . . Note=PKS/mFAS DH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01363 Q71SP7 UniProtKB Domain 2123 2200 . . . Note=Carrier;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00258 Q71SP7 UniProtKB Region 429 817 . . . Note=Acyl and malonyl transferases Q71SP7 UniProtKB Region 845 976 . . . Note=N-terminal hotdog fold;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01363 Q71SP7 UniProtKB Region 986 1107 . . . Note=C-terminal hotdog fold;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01363 Q71SP7 UniProtKB Region 1637 1865 . . . Note=Enoyl reductase Q71SP7 UniProtKB Region 1866 2119 . . . Note=Beta-ketoacyl reductase Q71SP7 UniProtKB Region 2209 2513 . . . Note=Thioesterase Q71SP7 UniProtKB Active site 161 161 . . . Note=For beta-ketoacyl synthase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01348 Q71SP7 UniProtKB Active site 293 293 . . . Note=For beta-ketoacyl synthase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01348 Q71SP7 UniProtKB Active site 331 331 . . . Note=For beta-ketoacyl synthase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01348 Q71SP7 UniProtKB Active site 581 581 . . . Note=For malonyltransferase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10022 Q71SP7 UniProtKB Active site 878 878 . . . Note=Proton acceptor%3B for dehydratase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01363 Q71SP7 UniProtKB Active site 1035 1035 . . . Note=Proton donor%3B for dehydratase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01363 Q71SP7 UniProtKB Active site 2310 2310 . . . Note=For thioesterase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10022 Q71SP7 UniProtKB Active site 2483 2483 . . . Note=For thioesterase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10022 Q71SP7 UniProtKB Binding site 647 648 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19096 Q71SP7 UniProtKB Binding site 671 671 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19096 Q71SP7 UniProtKB Binding site 773 773 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19096 Q71SP7 UniProtKB Binding site 1673 1690 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q71SP7 UniProtKB Binding site 1888 1903 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q71SP7 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327 Q71SP7 UniProtKB Modified residue 63 63 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327 Q71SP7 UniProtKB Modified residue 70 70 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327 Q71SP7 UniProtKB Modified residue 207 207 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327 Q71SP7 UniProtKB Modified residue 298 298 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327 Q71SP7 UniProtKB Modified residue 528 528 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327 Q71SP7 UniProtKB Modified residue 673 673 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327 Q71SP7 UniProtKB Modified residue 725 725 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19096 Q71SP7 UniProtKB Modified residue 996 996 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19096 Q71SP7 UniProtKB Modified residue 1414 1414 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327 Q71SP7 UniProtKB Modified residue 1473 1473 . . . Note=S-nitrosocysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327 Q71SP7 UniProtKB Modified residue 1596 1596 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19096 Q71SP7 UniProtKB Modified residue 1706 1706 . . . Note=N6-(pyridoxal phosphate)lysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q71SP7 UniProtKB Modified residue 1706 1706 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327 Q71SP7 UniProtKB Modified residue 1773 1773 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327 Q71SP7 UniProtKB Modified residue 1849 1849 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327 Q71SP7 UniProtKB Modified residue 1997 1997 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327 Q71SP7 UniProtKB Modified residue 2093 2093 . . . Note=S-nitrosocysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327 Q71SP7 UniProtKB Modified residue 2158 2158 . . . Note=O-(pantetheine 4'-phosphoryl)serine%3B alternate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00258 Q71SP7 UniProtKB Modified residue 2158 2158 . . . Note=Phosphoserine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12785 Q71SP7 UniProtKB Modified residue 2206 2206 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327 Q71SP7 UniProtKB Modified residue 2217 2217 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327 Q71SP7 UniProtKB Modified residue 2238 2238 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327 Q71SP7 UniProtKB Cross-link 2451 2451 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49327