ID I3NR56_9MUSC Unreviewed; 240 AA.
AC I3NR56;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=CAD {ECO:0000313|EMBL:AEG75377.1};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:AEG75377.1};
OS Stichillus spinosus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Platypezoidea;
OC Phoridae; Stichillus.
OX NCBI_TaxID=1003518 {ECO:0000313|EMBL:AEG75377.1};
RN [1] {ECO:0000313|EMBL:AEG75377.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=5.xii.06-389 {ECO:0000313|EMBL:AEG75377.1};
RA Hash J.M., Brown B.V., Smith P.T., Kanao T.;
RT "A Molecular Phylogenetic Analysis of the Genus Dohrniphora (Diptera:
RT Phoridae).";
RL Ann. Entomol. Soc. Am. 106:401-409(2013).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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DR EMBL; HM367061; AEG75377.1; -; Genomic_DNA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.20; -; 1.
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; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; 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; PF00117; GATase; 1.
DR PRINTS; PR00098; CPSASE.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 3..46
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 201..240
FT /note="Carbamoyl-phosphate synthetase large subunit-like
FT ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF02786"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEG75377.1"
FT NON_TER 240
FT /evidence="ECO:0000313|EMBL:AEG75377.1"
SQ SEQUENCE 240 AA; 26287 MW; 5F96986F08ACF549 CRC64;
PLFTNANDNS NEGIVHKTKP YFSVQFHPEH TAGPXDLEFL FXIFLDAVKE HKTGPVCVRQ
KIIDHLAYTP VKGSIPEVRP QKVLILGSGG LSIGQAGEFD YSGSQAIKAM KEEKIQTILI
NPNIATVQTS KGLADKVYFL PLTKEYVEQV IKAERPNGVL LTFGGQTALN CGVQLEKAGV
FSQYNVKILG TPITSIIATE DRKMFAEKVA EIGERVAPSE AVYSVQKALE AAERLCYPVM
//