ID B3TDY4_SPOFR Unreviewed; 557 AA.
AC B3TDY4;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Putative CAD trifunctional protein {ECO:0000313|EMBL:ABW39017.1};
DE Flags: Fragment;
OS Spodoptera frugiperda (Fall armyworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Amphipyrinae; Spodoptera.
OX NCBI_TaxID=7108 {ECO:0000313|EMBL:ABW39017.1};
RN [1] {ECO:0000313|EMBL:ABW39017.1}
RP NUCLEOTIDE SEQUENCE.
RA Regier J.C.;
RT "PCR primers that amplify across Panarthropoda.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; EU032750; ABW39017.1; -; mRNA.
DR AlphaFoldDB; B3TDY4; -.
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; -; 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; IPR011761; ATP-grasp.
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; 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; 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; PS50975; ATP_GRASP; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 2: Evidence at transcript level;
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}.
FT DOMAIN 480..557
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT ACT_SITE 220
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 304
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 306
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABW39017.1"
FT NON_TER 557
FT /evidence="ECO:0000313|EMBL:ABW39017.1"
SQ SEQUENCE 557 AA; 60841 MW; D56844CA1DDE32FA CRC64;
GYPESLTDPS YHAQLLVLTY PLVGNYGVPD EDERDEHGIP KWFESNRIWA AGLIVGEVST
NACHWRAKRS LGAWLAARGI PGVCDVDTRA LTFRLRAGVT LGRIIQGVPP FGPLPALSDP
NNRNLVAEVS VKEPKIYNPD GQVTIMAVDC GLKYNQIRCL IKRNAKVILV PWDHKLDPSQ
YDGLFISNGP GDPVKCKKLV DNMRTIIGDK NSVKPLFGIC LGHQLLSTAA GCKTYKTSYG
NRGHNLPCTH NGTGRCFMTS QNHGFAVDAD SLPEGWKILF TNENDKTNEG VIHETLPYFS
VQFHPEHTAG PTDLECLFDV FIDAVKSYKN KQTYNVDNAI TEKIKFVPTI HERPKKVLIL
GSGGLSIGQA GEFDYSGSQA VKALQEEKIQ TVLINPNIAT VQTSKGLADK VYFLPITPEY
VEQVIKAERP TGVLLTFGGQ TALNCGVELE KSKILEKYNV SVLGTPIQSI VDTEDRKIFA
EKIHAIGEKV APSAAVTTIE EALIAAKQIG YPVMARSAFS LGGLGSGFAN NEDELRTLAH
HGLSHSDQLI IDKSLKG
//