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Database: UniProt
Entry: I3NR56_9MUSC
LinkDB: I3NR56_9MUSC
Original site: I3NR56_9MUSC 
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
//
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