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Database: UniProt
Entry: W7I6Y4_9PEZI
LinkDB: W7I6Y4_9PEZI
Original site: W7I6Y4_9PEZI 
ID   W7I6Y4_9PEZI            Unreviewed;      1162 AA.
AC   W7I6Y4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   13-SEP-2023, entry version 26.
DE   SubName: Full=Carbamoyl-phosphate synthase arginine-specific large chain {ECO:0000313|EMBL:EWC48038.1};
GN   ORFNames=DRE_02617 {ECO:0000313|EMBL:EWC48038.1};
OS   Drechslerella stenobrocha 248.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Drechslerella.
OX   NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC48038.1, ECO:0000313|Proteomes:UP000024837};
RN   [1] {ECO:0000313|EMBL:EWC48038.1, ECO:0000313|Proteomes:UP000024837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=248 {ECO:0000313|EMBL:EWC48038.1,
RC   ECO:0000313|Proteomes:UP000024837};
RA   Liu X., Zhang W., Liu K.;
RT   "Drechslerella stenobrocha genome reveals carnivorous origination and
RT   mechanical trapping mechanism of predatory fungi.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KI966406; EWC48038.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7I6Y4; -.
DR   HOGENOM; CLU_000513_1_3_1; -.
DR   Proteomes; UP000024837; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR   CDD; cd01423; MGS_CPS_I_III; 1.
DR   Gene3D; 3.40.50.20; -; 2.
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   Gene3D; 3.40.50.1380; Methylglyoxal synthase-like 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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR   PANTHER; PTHR11405:SF51; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC LARGE CHAIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   PRINTS; PR00098; CPSASE.
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; SSF52335; Methylglyoxal synthase-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS51855; MGS; 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}; Reference proteome {ECO:0000313|Proteomes:UP000024837};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          213..405
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          749..946
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1014..1162
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
SQ   SEQUENCE   1162 AA;  127836 MW;  BDFD4622FCBD56D4 CRC64;
     MSQTLIKNIP ISRLSTFAAY TRAFNSLTAI HKLVPPLASS ATTNVVGKRQ LYSSGTRVKS
     ILQARTFSST VARKVHDTTQ VAPSAKAYLE SGVIAGSGNL VDVQKVLVIG SQAIKALKEA
     GKESILINPN IANIQTSHFL ADEVYFLPVT TEYISYVIER ERPDGILLTF GGQTGLNVGV
     KLDKMGVFER MGVKVLGTPI KTLETSEDRD LFAKALKEID IPIAESIAVN TVEEALAAAD
     EIGYPIIVRS AYALGGLGSG FAKDRAELES LSSQSLSLAP QILVEKSLKG WKEVEYEVVR
     DASNNCITVC NMENFDPLGI HTGDSIVVAP SQTLSDEEYH MLRSAAIKIV RHLGVVGECN
     VQYALQPDGL DYRVIEVNAR LSRSSALASK ATGYPLAYTA AKIALGHTLP ELPNAVTKTT
     TANFEPSLDY IVSKIPRWDL SKFGHVKRDI GSAMKSVGEV MAIGRTFEES IQKAIRQVDP
     RFLGFQGDKF DDLDFELANP TDRRWLAVGQ AMLHENYSVD RVHELTKIDK WFLYKLQNIV
     NCHHELRDLG SLDHVNQDLL LKAKKLGFGD KQISLLVNST EDEVRARRKR FDIHPWVKKI
     DTLAAEFPAS TNYLYTTYNA SSHDVTFVDN GTIILGSGVY RIGSSVEFDW CAVSCTLALR
     ELGKKTVMIN YNPETYSTDF DTADRLYFEE LSYERVMDIY ELENASGVVV SVGGQLPQNI
     ALKLSETGAK VLGTDPKDID KAEDRHKFSQ ILDSIGVDQP AWKELTSVDA ALQFSKDVGF
     PVLVRPSYVL SGAAMSVIRD EGELEQKLKN ASAVSPDHPV VITKFIEGAM EIDVDAVAHE
     GKLLIHAISE HVEHAGVHSG DATLVLPPVS LDENTMARLK EIAVKVAKAW SITGPFNMQI
     IKADLQDGSE AALKVIECNL RASRSFPFVS KVLGVNFVDV ATKALANTAV PEPIDVMNQK
     FDRVATKVPQ FSWTRLAGAD PFLGVEMAST GEIACFGKDL VEAYWASIQS VMNFQVPEPG
     SGVLLGGDTN ASYLKQVVEY IGPMGYKLLA ANPAVKEALE KDVPSVKIEV LDFPKTDKRK
     LREIFKQHNI KSVFNLARSR GKNLLDEDYV MRRNAVDFNV PLFMEPKTAV LFAQCLREKL
     PRKEGIPSEV RRWSEFIGGK PL
//
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