ID Q6WLA6_9MUSC Unreviewed; 1294 AA.
AC Q6WLA6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 85.
DE SubName: Full=CAD {ECO:0000313|EMBL:AAQ67181.1};
DE Flags: Fragment;
GN Name=r {ECO:0000313|EMBL:AAQ67181.1};
OS Iteaphila sp. NCSU-99072186.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Empidoidea;
OC Empididae; Empidinae; Iteaphila.
OX NCBI_TaxID=240892 {ECO:0000313|EMBL:AAQ67181.1};
RN [1] {ECO:0000313|EMBL:AAQ67181.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15019631; DOI=10.1016/S1055-7903(03)00284-7;
RA Moulton J.K., Wiegmann B.M.;
RT "Evolution and phylogenetic utility of CAD (rudimentary) among Mesozoic-
RT aged Eremoneuran Diptera (Insecta).";
RL Mol. Phylogenet. Evol. 31:363-378(2004).
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DR EMBL; AY280685; AAQ67181.1; -; Genomic_DNA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; 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; -; 2.
DR Gene3D; 3.40.50.880; -; 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; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
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; IPR006274; CarbamoylP_synth_ssu.
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 NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 1.
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; 2.
DR Pfam; PF02787; CPSase_L_D3; 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; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 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; 2.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 474..666
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1007..1198
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT ACT_SITE 208
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 292
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 294
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAQ67181.1"
FT NON_TER 1294
FT /evidence="ECO:0000313|EMBL:AAQ67181.1"
SQ SEQUENCE 1294 AA; 142724 MW; 2F23FF81EA74CAA5 CRC64;
QILVLTYPLI GNYGVPSEKD LDSLGLPKHF EWTDGISVAG LVVGEICSTP SHWRHTRTLS
KWMEEQGIPG ISDIDTRALT KKIRDNGTML GRIAYGSVPS PKMELKLSDP NARNLVAECS
VKKPIIFNPN GSPRICAIDC GLKLNQIRCF AARGARVELV PWNYNLNPTE FDGLFISNGP
GDPIVCKDTV TQLQKILKQS DVPIFGICLG HQLLATAIGC KTYKMKYGNR GHNLPCIHHG
TGRCFMTSQN HGFAVDADTL PKDWEALFTN ANDHTNEGII HKNKPYFSVQ FHPEHNAGPE
DLEVLFDVFL DSVKDRLAAG QQKKTIKLNL IDTLSYKPSS GLILPERPTK VLILGSGGLS
IGQAGEFDYS GSQAIKALKE EKIQTILINP NIATVQTSKG LADKVYFLPL TPEYVEQVIK
AERPNGVLLT FGGQTALNCG VELDRAGVFQ KYNVKIMGTP IQSIIETEDR KIFADRVAEI
GEKVAPSEAV YSVAEALDAA EKLGYPVMAR AAFSLGGLGS GFASNQEELK ILAKQALAHS
NQLIIDKSLR GWKEVEYEVV RDAFDNCITV CNMENLDPLG IHTGESIVVA PSQTLSNREY
NMLRTTAIKV IRHFGVVGEC NIQYALNPES EEYYIIEVNA RLSRSSALAS KATGYPLAYV
AAKLSLSVAL PDIKNSVTGV TTACFEPSLD YCVVKIPRWD LAKFTRVSKN IGSSMKSVGE
VMSIGRNFEE AFQKALRMVD ETVNGFDPYI KPVKEEELIQ ATDKRTFVLA AAIKANYTIE
NLYNLTKIDP WFLNKMKNII DFLNLLETQG NTLDRPMLLK AKKMGFSDKQ IAAAIKSTDL
VVRRQREELG IIPFVKQIDT VAGEWPATTN YLYLTYNATT NDLEFPGKFT IVVGSGVYRI
GSSVEFDWCA VGCLRELRNL GRSTIMINYN PETVSTDYDM CDRLYFEEIS FEVVMDIYQI
ENADGIILSM GGQLSNNIAM DLHRQQARVL GTSPESIDSA ENRFKFSRML DRKGILQPRW
KELTNLKSAI DFCEEAGYPC LVRPSYVLSG AAMNVAYSNQ DLETYLNAAS LVSKEHPVVI
TKFLQEAKEI DVDAVARDGE ILCMAVSEHV ENAGVHSGDA TLVTPPQDLN AETLEKIKAI
VSDLAVLLDV TGPFNMQFIA KNNELKVIEC NVRVSRSFPF VSKTLNHDFV ATATRAIIGM
PVEPVDVLHG CGKVGVKVPQ FSFSRLAGAD VQLGVEMAST GEVACFGDNR YEAYLKAMMS
TGFQIPKKAI LLSIGSFKHK VELLPSIRDL AKMG
//