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Database: UniProt
Entry: D9IUT5_9MUSC
LinkDB: D9IUT5_9MUSC
Original site: D9IUT5_9MUSC 
ID   D9IUT5_9MUSC            Unreviewed;       561 AA.
AC   D9IUT5;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Carbamoyl phosphate synthetase-aspartate transcarbamoylase-dihydroorotase {ECO:0000313|EMBL:ADJ19297.1};
DE   Flags: Fragment;
OS   Prorates sp. MDT-2010.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Asiloidea;
OC   Scenopinidae; Prorates.
OX   NCBI_TaxID=797029 {ECO:0000313|EMBL:ADJ19297.1};
RN   [1] {ECO:0000313|EMBL:ADJ19297.1}
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).
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DR   EMBL; HM183053; ADJ19297.1; -; Genomic_DNA.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR035686; CPSase_GATase1.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00098; CPSASE.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          1..97
FT                   /note="Carbamoyl-phosphate synthase small subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01097"
FT   ACT_SITE        215
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADJ19297.1"
FT   NON_TER         561
FT                   /evidence="ECO:0000313|EMBL:ADJ19297.1"
SQ   SEQUENCE   561 AA;  61997 MW;  A8A7BFDE91767D1B CRC64;
     QILVLTYPIT GNYGVPSGSD YDEYGLPKHF EWTEXGISVA GLVVGEICXE TPSHWRQTST
     LSKWMEQQDI PGISGIDTRA LTKKIRENXG TILGRIQYVP FNPLLDXNPL LXXDPYSRFL
     VKECSVKEII TFNPTGSPKI CAVDCGLKLN QIRCLVARGA RVDLVPWDHK LNPNDFDGLF
     LSNGPGDPIM XCCETVKEIR KWLKRPXQKP IFGICLGHQL LSSAIGCKTY KMKYGNRGHN
     LPCVHXNGTG RCFMTSQNXH GFAVDISQLP SXDWEILFTN ANDNTNEGII HNKXDPFFSV
     QFHPEHXTAG PRDLELLFDV FLDTVKEYKS KGXSXXLTSV KERLTKALTY SPKPESILKT
     KPRKVLILGS GGLSIGQAGE FDYSGSQAIK AMQEEKIQAI LINPNIATVQ TSKGLADKVY
     FLPLTREYVE QVIKAERPNG VLLTFGGQTA LNCGVELEKA EIFSKYNVKI LGTPIESIIE
     TEDRKIFADR IAEIGEKVAP SEAVYSVNEA LLAAERLGYP VMARXAAFSL GGLGSGFANN
     QEELKTLAQQ ALAHSNQLII D
//
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