ID   D9IUV9_9MUSC            Unreviewed;       838 AA.
AC   D9IUV9;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Carbamoyl phosphate synthetase-aspartate transcarbamoylase-dihydroorotase {ECO:0000313|EMBL:ADJ19321.1};
DE   Flags: Fragment;
OS   Sericosoma sp. MDT-2010.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Asiloidea;
OC   Bombyliidae; Sericosoma.
OX   NCBI_TaxID=797054 {ECO:0000313|EMBL:ADJ19321.1};
RN   [1] {ECO:0000313|EMBL:ADJ19321.1}
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; HM183068; ADJ19321.1; -; 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; 3.30.1490.20; ATP-grasp fold, A domain; 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; IPR013815; ATP_grasp_subdomain_1.
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; 2.
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};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          33..226
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          567..759
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADJ19321.1"
FT   NON_TER         838
FT                   /evidence="ECO:0000313|EMBL:ADJ19321.1"
SQ   SEQUENCE   838 AA;  92895 MW;  38F201184FF51B4D CRC64;
     NLERAGIFRK YNVKILGTPI KSIIETEDRK IFAQRVSEIG EKVAPSEAVY SVSEALESAK
     RLGYPVMARX AAFSLGGLGS GFANNPEELK TLAQQALAHS NQLIIDKSLK GWKEVEYEVV
     RDAFDNCITV CNMENVDPLG IHTGESIVVA PSQTLSNKEY NMLRTTAIKV IRHFGVIGEC
     NIQYALSPNS EEYYIIEVNA RLSRSSALAS KATGYPLAYV AAKLALGMPL PDIKNSVTGV
     TTACFEPSLD YCVVKIPRWD LTKFTRVSKN IGSSMKSVGE VMAIGRTFEE AFQKALRMVD
     ECVCGFDPYI KPVCEAELSQ PTDKRIYVLA AALKENYSVE KLYELTKIDP WFLNKMKNII
     DYLNFLEAHG NNLTRDHLLN AKQLGFSDKQ IAAAIKSTDL AVRQHREEVD VTPFVKQIDT
     VAGEWPATTN YLYITYNASS HDIEFPGDFT MVVGSGVYRI GSSVEFDWCA VGCLRELRNL
     GRSTIMINYN PETVSTDYDM CDRLYFEEIS FEVVMDIYQL ENPEGIILSM GGQLPNNIAM
     DLHRQQARVL GTSPEQIDCA ENRFKFSRML DRKGILQPRW KELTNLQSAI QFCEEVEYPC
     LVRPSYVLSG AAMNVAYSNQ DLETYLNAAS EVSKEHPVVI SKFLIEAKEI DVDAVAADGE
     ILCLAVSEHV ENAGVHSGDA TLXVTPPQDI NAKTLEKIKE IARDLAALLD VTGPFNMQLI
     AKNNELKVIE CNVRVSRSFP FVSKTLNHDF VAMATRVIIG LPVEPVDVLH GCGKVGVKVP
     QFSFSRLAGA DVQLGVEMAS TGEVACFGDN RYEAYLKAMM STGFQIPKKA ILLSIGSF
//