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Database: UniProt
Entry: A8Q026_MALGO
LinkDB: A8Q026_MALGO
Original site: A8Q026_MALGO 
ID   A8Q026_MALGO            Unreviewed;      1143 AA.
AC   A8Q026;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   08-NOV-2023, entry version 68.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDP43761.1};
GN   ORFNames=MGL_1974 {ECO:0000313|EMBL:EDP43761.1};
OS   Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP43761.1, ECO:0000313|Proteomes:UP000008837};
RN   [1] {ECO:0000313|EMBL:EDP43761.1, ECO:0000313|Proteomes:UP000008837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX   PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA   Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA   Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA   Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA   Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT   "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT   virulence traits shared with plant and human fungal pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDP43761.1}.
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DR   EMBL; AAYY01000006; EDP43761.1; -; Genomic_DNA.
DR   RefSeq; XP_001730975.1; XM_001730923.1.
DR   AlphaFoldDB; A8Q026; -.
DR   STRING; 425265.A8Q026; -.
DR   GeneID; 5855282; -.
DR   KEGG; mgl:MGL_1974; -.
DR   VEuPathDB; FungiDB:MGL_1974; -.
DR   InParanoid; A8Q026; -.
DR   OMA; IEPAGIH; -.
DR   OrthoDB; 309at2759; -.
DR   Proteomes; UP000008837; 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:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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:UP000008837};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          188..380
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          725..923
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          991..1143
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
SQ   SEQUENCE   1143 AA;  126455 MW;  B246EC01D5B47AA6 CRC64;
     MHGQHGIGDS SAASHTLRCR TSRQHLLQAG PASAIEPSAN KSDTSGLERW RKFLPNNPKA
     QVQKVLLVGS GGLSIGQAGE FDYSGSQAIK ALRESGIETV LINPNIATIQ TSQQLASRIY
     FLPVSPDYVA YVLERERPDG VFLNFGGQSA LNVGVKLDEM GVFERLGVQV LGSQPDVLRM
     CEDRDLFVQA LDQIQIPVAR SEAVSTVKEA LRAADEIGYP VIVRAAYALG GLGSGFADNE
     EELRDLSARS LSLSPQILVE KSLRGWKESE YEVLRDQQDN ALICCNMENF DPLGIHTGDS
     IVVAPSQTLS DDNYHMLRTA ALKVIRHLGI VGECNIQYAL SPDSREYRVI EVNPRLSRSS
     ALASKATGYP LAYTAAKLAL GHTLPELPNA VTKTTTACFE PSLDYIVTKI PKWDLSKFQH
     VNREIGSSMK SVGEVMAIGR TFEESLQKAV RQVAPNYQGF DAYVCPDDLD HALRIPTDTR
     LFALAHAMLV KNYDVERLHE LTKIDRWFLF KLENIVNTHR ELQECGSLDK VPAELMRTAK
     QRGFSDVQIA RLVHSSEAHV RVARKAMGVT PFVKRIDTVA AEYPAQTNYL YTTYNASTHD
     IEFDEHGTMV LGSGVYRIGS SVEFDWCAVT CVRRLKELKH NTIMINYNPE TVSTDYDEAG
     RLYFEELGFE RVMDIYELEQ ASGVVVSVGG QLPQNIALRL KEAQVQVLGT DPLKIDSAED
     RHKFSQILDS IGVDQPDWVE VTDVEKAKEF AKRVTYPVLV RPSYVLSGAA MNVIWDETTL
     EHNLTAAAQV NTDYPVVLTK FIPNAQEIDI DAVAHKGKLL VHAVSQHVEN AGVHSGDATL
     VLPPFSLPSQ DMARLKDIAE RVAAAFEISG PFNMQIIRKQ DPAANDESEL KVIECNLRAS
     RSFPFVSKVL GVNFIDVATS AIVGENVPEP VDLMAKTYNH VAIKVPQFSW TRLAGADPFL
     GVEMASTGEV ASFGADIHEA YWASIASTTG FRVPLAHKGV LLGGDTTTPE LRTIAMKLCN
     LGFKLYCSNA DVETFLNGLP HVSAKRIWFP LKDKRKLREV FDDYEIQFVI NLAKYRAPSV
     TDEDYVARRN AVDFGLPLLN EPKTALLFVE TLEHKMPKGC LLPYDEGKIP SEVKAWNEFV
     PST
//
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