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
//