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
//