##gff-version 3 Q18990 UniProtKB Chain 1 2198 . . . ID=PRO_0000438771;Note=Multifunctional protein pyr-1;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q18990 UniProtKB Domain 180 366 . . . Note=Glutamine amidotransferase type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 Q18990 UniProtKB Domain 516 708 . . . Note=ATP-grasp 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Domain 1054 1245 . . . Note=ATP-grasp 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Domain 1318 1474 . . . Note=MGS-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01202 Q18990 UniProtKB Region 3 368 . . . Note=GATase (Glutamine amidotransferase);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08955 Q18990 UniProtKB Region 392 1467 . . . Note=CPSase (Carbamoyl-phosphate synthase);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08955 Q18990 UniProtKB Region 392 934 . . . Note=CPSase A;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08955 Q18990 UniProtKB Region 935 1467 . . . Note=CPSase B;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08955 Q18990 UniProtKB Region 1468 1799 . . . Note=DHOase (dihydroorotase);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08955 Q18990 UniProtKB Region 1800 1870 . . . Note=Linker;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08955 Q18990 UniProtKB Region 1871 2196 . . . Note=ATCase (Aspartate transcarbamylase);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08955 Q18990 UniProtKB Active site 255 255 . . . Note=Nucleophile%3B for GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 Q18990 UniProtKB Active site 339 339 . . . Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 Q18990 UniProtKB Active site 341 341 . . . Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 Q18990 UniProtKB Active site 1695 1695 . . . Note=For DHOase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05020 Q18990 UniProtKB Binding site 45 45 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6F1 Q18990 UniProtKB Binding site 226 226 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6F1 Q18990 UniProtKB Binding site 228 228 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6F1 Q18990 UniProtKB Binding site 256 256 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6F1 Q18990 UniProtKB Binding site 259 259 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6F1 Q18990 UniProtKB Binding site 297 297 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6F1 Q18990 UniProtKB Binding site 299 299 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6F1 Q18990 UniProtKB Binding site 300 300 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6F1 Q18990 UniProtKB Binding site 512 512 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 552 552 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 558 558 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 559 559 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 589 589 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 596 596 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 622 622 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 623 623 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 624 624 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 665 665 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 665 665 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Binding site 665 665 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Binding site 679 679 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 679 679 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Binding site 679 679 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Binding site 679 679 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Binding site 679 679 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Binding site 681 681 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Binding site 681 681 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Binding site 1090 1090 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 1129 1129 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 1131 1131 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 1136 1136 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 1161 1161 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 1162 1162 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 1163 1163 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 1164 1164 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 1204 1204 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 1204 1204 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Binding site 1204 1204 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Binding site 1216 1216 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00968 Q18990 UniProtKB Binding site 1216 1216 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Binding site 1216 1216 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Binding site 1216 1216 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Binding site 1216 1216 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Binding site 1218 1218 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Binding site 1218 1218 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q18990 UniProtKB Binding site 1483 1483 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27708 Q18990 UniProtKB Binding site 1483 1483 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27708 Q18990 UniProtKB Binding site 1485 1485 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27708 Q18990 UniProtKB Binding site 1487 1487 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27708 Q18990 UniProtKB Binding site 1517 1517 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27708 Q18990 UniProtKB Binding site 1568 1568 . . . Note=Via carbamate group;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27708 Q18990 UniProtKB Binding site 1568 1568 . . . Note=Via carbamate group;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27708 Q18990 UniProtKB Binding site 1602 1602 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27708 Q18990 UniProtKB Binding site 1626 1626 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27708 Q18990 UniProtKB Binding site 1649 1649 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27708 Q18990 UniProtKB Binding site 1670 1670 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27708 Q18990 UniProtKB Binding site 1695 1695 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27708 Q18990 UniProtKB Binding site 1699 1699 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27708 Q18990 UniProtKB Binding site 1713 1713 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27708 Q18990 UniProtKB Binding site 1929 1929 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A786 Q18990 UniProtKB Binding site 1930 1930 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A786 Q18990 UniProtKB Binding site 1957 1957 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A786 Q18990 UniProtKB Binding site 1978 1978 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A786 Q18990 UniProtKB Binding site 2006 2006 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A786 Q18990 UniProtKB Binding site 2009 2009 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A786 Q18990 UniProtKB Binding site 2039 2039 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A786 Q18990 UniProtKB Binding site 2103 2103 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A786 Q18990 UniProtKB Binding site 2156 2156 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A786 Q18990 UniProtKB Binding site 2157 2157 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A786 Q18990 UniProtKB Modified residue 1568 1568 . . . Note=N6-carboxylysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27708 Q18990 UniProtKB Mutagenesis 1602 1602 . . . Note=In cu8%3B probable loss of dihydroorotase activity. Severe late stage embryonic lethality in 50%25 of animals. The few surviving mutants have a shorter and thicker pharyngeal isthmus%2C an abnormal knobbed tail%2C mild egg-laying defects%2C moderate fluid accumulation in the coelom and a slower growth. Actin and intermediate filaments are disorganized in the pharynx. Moderate reduction in heparan sulfate levels and increased levels of chondroitin sulfate. In an umps-1 zu456 mutant background%2C prevents the formation of abnormally enlarged gut granules in embryos. Complete embryonic lethality in a rnst-2 qx245 mutant background. H->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16828468,ECO:0000269|PubMed:20148972,ECO:0000269|PubMed:30102152;Dbxref=PMID:16828468,PMID:20148972,PMID:30102152