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Database: UniProt
Entry: F0W4K0_9STRA
LinkDB: F0W4K0_9STRA
Original site: F0W4K0_9STRA 
ID   F0W4K0_9STRA            Unreviewed;      1543 AA.
AC   F0W4K0;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   13-SEP-2023, entry version 46.
DE   SubName: Full=PREDICTED: similar to Carbamoylphosphate synthase p {ECO:0000313|EMBL:CCA16033.1};
GN   Name=AlNc14C17G1820 {ECO:0000313|EMBL:CCA16033.1};
GN   ORFNames=ALNC14_021760 {ECO:0000313|EMBL:CCA16033.1};
OS   Albugo laibachii Nc14.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA16033.1};
RN   [1] {ECO:0000313|EMBL:CCA16033.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA   Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA   Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA   Jones J.D.;
RT   "Gene gain and loss during evolution of obligate parasitism in the white
RT   rust pathogen of Arabidopsis thaliana.";
RL   PLoS Biol. 9:e1001094-e1001094(2011).
RN   [2] {ECO:0000313|EMBL:CCA16033.1}
RP   NUCLEOTIDE SEQUENCE.
RA   MacLean D.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FR824062; CCA16033.1; -; Genomic_DNA.
DR   EnsemblProtists; CCA16033; CCA16033; ALNC14_021760.
DR   HOGENOM; CLU_000513_0_1_1; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   Gene3D; 3.40.50.20; -; 2.
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; 2.
DR   Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
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   HAMAP; MF_01209; CPSase_S_chain; 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; IPR006274; CarbamoylP_synth_ssu.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR036480; CarbP_synth_ssu_N_sf.
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; IPR035686; CPSase_GATase1.
DR   InterPro; IPR017926; GATASE.
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   NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR   PANTHER; PTHR11405:SF53; CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF02142; MGS; 1.
DR   PRINTS; PR00098; CPSASE.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR   SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 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; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51855; MGS; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          584..776
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1125..1316
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1387..1532
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   ACT_SITE        326
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        410
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        412
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   1543 AA;  170607 MW;  F66D2AD106602E99 CRC64;
     MSLETLRDTT QTNRSFTLFN QRIVVRYCHF KMLRVSQSLR KQVVQSRATG NRLCLSTSKK
     VDRRNAPRFE TKAVLEFEDG SKYQGYSFGA PRSTSGEVVF TTGMVGYPEA LTDASFKGQI
     LNMTFPMIGN YGVPCTKTLD SIGLNKYIES DRIHAAGMIV QDYSSVYSHW NASSSLSEWL
     VRESIPGIAG IDTREITKKI RSKGAMAGRI IVGDETPPQF QDPNQQNLVA MVSTKEVRVF
     GKGNPLKILA IDCGIKYNII RSLVSRGAEV KLVPWNHDVA SEAHWYDGLF ISNGPGDPAL
     LEETTRHLRS ALNAEGDAVK PIFGICLGNQ LVGRAVGAET YKLPFGNRGH NQPVNNLKTG
     LSYITSQNHG YALDGKSLPS EWEELFVNGN DGTNEGIIHK SKPMFTAQFH PEHCGGPTDT
     EFLFDIFLDA VRRKEKGPIT SLVRAPVIER PQVQKVLVLG SGGLSIGQAG EFDYSGSQAI
     KALKEENIET ILINPNIASV QTNIDKSSEA QASNVYYLPV TTDFVEQVIK RERPDGILIS
     MGGQTALNCG VELHKRGILQ KYGVRVLGTQ IDVIDATEDR EKFNTKLKEI GEKIAESYAV
     NSVEDAVVAA HKIKFPVMIR SAFALGGLGS GICETEKDLR SMATKAFSGS PQILVEKSMK
     GWKEVEYEVV RDTANNCLTV CNMENFDPLG IHTGESIVIA PSQTLSNREY HMLRETAINV
     VRHLGIIGEC NIQYALNPHS EEYCIIEVNA RLSRSSALAS KATGYPLAFV AAKLALGINL
     PELKNSVTKS TTACFEPSLD YCVTKIPRWD LSKFDNVSTE IGSSMKSVGE VMSIARTFEE
     GIQKALRMVE PSIKGFEPRN AEISREELVQ GLSRPTDKRI YQMAYALKHG VLSVDEIHDI
     TKIDIWYLSR LQRIVDCDVN LTDRALADVS SMELKEAKQL GFSDRQLARM FRCSDDDVRA
     RRKQCGVLPV VKQIDTLAAE YPAQTNYLYT TYNGTENDVA AQKPNDGVLV LGSGAYRIGS
     SVEFDWCAVS CIRTLRKLGY RAVMLNYNPE TVSTDYDECN QLYFEELSKE RVMDVYEREG
     VQGVVVSVGG QIPNNLALPL HKVGVKIMGT HPTMIDSAED RYKFSKLMDE AGVRQPAWKE
     LTSMPAALKF ANSVGYPCLV RPSYVLSGAA MNVAYNDHDL ERVLGEAVDV SAEHPVVITK
     FIEGAKELEL DAVARNGEII AAAISEHVEN AGVHSGDATL ILPPVEASSF YLNQIRQCGK
     KIAMALNISG PFNAQFLAKG ADVSVIECNL RASRSFPFVS KTVSADFIQA ATKVMVGEPT
     ESDNLPPLFG PKRPEGYVGI KAPMFSYTRL GGADPLLGVE MASTGEVACF GKNRPEAFLK
     ALLSSNFKLP KENILLSMQD KFSDDFIHAA YQLHELGYNL FATDKTHTFL HKYDIPSTKV
     DFPRDGDSEH DVINFIKEGK IDLVVNLPNS ESKQLKNNYL IRRTAVDFSI PVLTNISLVK
     MFAEAMAIHK KKPLLGLDAD SLFDYYERED REKKAWTGVN EFH
//
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