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Database: UniProt
Entry: H9U5X8_9CARA
LinkDB: H9U5X8_9CARA
Original site: H9U5X8_9CARA 
ID   H9U5X8_9CARA            Unreviewed;       400 AA.
AC   H9U5X8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=CAD(R) {ECO:0000313|EMBL:AFG32732.1};
DE   Flags: Fragment;
OS   Bembidarenas reicheellum.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Adephaga; Caraboidea; Carabidae;
OC   Trechinae; Bembidarenini; Bembidarenas.
OX   NCBI_TaxID=1166946 {ECO:0000313|EMBL:AFG32732.1};
RN   [1] {ECO:0000313|EMBL:AFG32732.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22421212; DOI=10.1016/j.ympev.2012.01.015;
RA   Maddison D.R.;
RT   "Phylogeny of Bembidion and related ground beetles (Coleoptera: Carabidae:
RT   Trechinae: Bembidiini: Bembidiina).";
RL   Mol. Phylogenet. Evol. 63:533-576(2012).
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DR   EMBL; JN170740; AFG32732.1; -; Genomic_DNA.
DR   AlphaFoldDB; H9U5X8; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.40.50.20; -; 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; 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; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          305..393
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFG32732.1"
FT   NON_TER         400
FT                   /evidence="ECO:0000313|EMBL:AFG32732.1"
SQ   SEQUENCE   400 AA;  45437 MW;  2C526DF5559764DB CRC64;
     FSRVSTKIGS SMKSVGEVMA IGRNFGEAFQ KALRMVDENV IGFDPYIRKI DDEELKEPTD
     KRMFVVAAAL KSGYTVDKLY DLTKIDRWFL QKLKHIIDCI TFLETKDQHS LAYDDLLKAK
     QMGFSDKQIA DFVKSTELAI RKQREECGLL PFVKQIDTVA AEWPATTNYL YITYNAIEHD
     IEFNDEHTMV LGSGVYRIGS SVEFDWCAVG CLRELRKLNR KTIMVNYNPE TVSTDYDMSD
     RLYFEEISFE VVMDIYNLEN PAGIILCMGG QLPNNIAMDL HRQQARILGT SPESIDGAEN
     RFKFSRMLDR IGILQPRWKE LTNLKSAIEF CEEVGYPCLV RPSYVLSGAA MNVAHSNQDL
     ETYLNAASDV SKEHPVVISK FILESKEIDV DAVACDGSIL
//
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