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
//