ID   D9IUW3_9MUSC            Unreviewed;       707 AA.
AC   D9IUW3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Carbamoyl phosphate synthetase-aspartate transcarbamoylase-dihydroorotase {ECO:0000313|EMBL:ADJ19325.1};
DE   Flags: Fragment;
OS   Neosardus principius.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Asiloidea;
OC   Bombyliidae; Neosardus.
OX   NCBI_TaxID=797141 {ECO:0000313|EMBL:ADJ19325.1};
RN   [1] {ECO:0000313|EMBL:ADJ19325.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20399874; DOI=10.1016/j.ympev.2010.04.017;
RA   Trautwein M.D., Wiegmann B.M., Yeates D.K.;
RT   "A multigene phylogeny of the fly superfamily Asiloidea (Insecta): Taxon
RT   sampling and additional genes reveal the sister-group to all higher flies
RT   (Cyclorrhapha).";
RL   Mol. Phylogenet. Evol. 56:918-930(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC         phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC         ChEBI:CHEBI:456216; EC=6.3.4.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00043687};
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DR   EMBL; HM183071; ADJ19325.1; -; Genomic_DNA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR   Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR   PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   PRINTS; PR00098; CPSASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT   DOMAIN          27..220
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          561..707
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADJ19325.1"
FT   NON_TER         707
FT                   /evidence="ECO:0000313|EMBL:ADJ19325.1"
SQ   SEQUENCE   707 AA;  78527 MW;  CC7DEF1B7FC7A4DC CRC64;
     IFNKYNVKIL GTPIESIIDT EDRKIFAQRV GEIGEKVAPS EAVCSVAEAL DSAERLGYPV
     MARXAAFSLG GLGSGFANNP EELRILAQQA LAHSNQLIID KSLKGWKEVE YEVVRDAFDN
     CITVCNMENV DPLGIHTGES IVVAPSQTLS NREYNMLRTT AIKVIKHFGV IGECNIQYAL
     NPASEEYYII EVNARLSRSS ALASKATGYP LAYVAAKLAL GIPLPEIKNS VTGVTTACFE
     PSLDYCVVKI PRWDLTKFTR VSKNIGSSMK SVGEVMAIGR KFEEAFQKAL RMVDETVTGF
     DPYIKPVLEA ELSQPTDKRI YVLAAAMKKN YSIERLYELT KIDPWFLNKM KNIIEYLNFL
     EAHGNNLTXD HLLTAKQLGF SDKQIAAAIK STDLAVRKHR EEVKVTPFVK QIDTVAGEWP
     AATNYLYITY NASAHDIEFP GDYTMVVGSG VYRIGSSVEF DWCAVGCLRE LRNLGRSTIM
     INYNPETVST DYDMCDRLYF EEISFEVVMD IYKLENPEGI ILSMGGQLPN NIAMDLHRQQ
     ARVIGTSPES IDSAENRFKF SRMLDRKGIL QPRWKELTNL QSAIKFCEEV EYPCLVRPSY
     VLSGAAMNVA YSNQDLETYL NAASEVSKEH PVVISKFIME AKEIDVDAVA ADGEILCLAV
     SEHVENAGVH SGDATLXVTP PQDINPETLV KIKEITRDLA ALLDVTG
//