ID A8Q2V9_MALGO Unreviewed; 628 AA.
AC A8Q2V9;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDP43239.1};
GN ORFNames=MGL_2249 {ECO:0000313|EMBL:EDP43239.1};
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:EDP43239.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP43239.1, 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:EDP43239.1}.
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DR EMBL; AAYY01000008; EDP43239.1; -; Genomic_DNA.
DR RefSeq; XP_001730453.1; XM_001730401.1.
DR AlphaFoldDB; A8Q2V9; -.
DR STRING; 425265.A8Q2V9; -.
DR GeneID; 5854760; -.
DR KEGG; mgl:MGL_2249; -.
DR VEuPathDB; FungiDB:MGL_2249; -.
DR InParanoid; A8Q2V9; -.
DR OMA; HDQIFLT; -.
DR OrthoDB; 101939at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR CDD; cd07399; MPP_YvnB; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR43143; METALLOPHOSPHOESTERASE, CALCINEURIN SUPERFAMILY; 1.
DR PANTHER; PTHR43143:SF1; SERINE/THREONINE-PROTEIN PHOSPHATASE CPPED1; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008837};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..628
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002725072"
SQ SEQUENCE 628 AA; 70641 MW; B96FAFE37507E65C CRC64;
MLCISRLLAG VLTAASLVVG GQWTDDAYDV TTVKSKPKGQ WQPDAMSLEF TVIVMPDTQY
LFDENRIHPV PMEASFEYIV SPNRSEADKN IVFVSHLGDV AQNGLAKEYA AVTKLFDYMD
ESGVEYSVLA GNHDIDSSTD DQRGPTPYLD VFNPKRFSKI RSWRGSSSDG YNNYHVFHAG
GREWLVLALD WRMSSGTFKW ASDVLRKHAD LPTILTTHEL VTADSGKTEF SEYGERVWNE
LVRDNDQIFL TLNGHFWPPG RTTRKNAAGR DVESHITNYQ NRYYGGAGMI RAYRFNMKEN
KIDVATFSPW IQNLVQRGEA NKLAKQEEEL TSADDKFTMH INFAERFEHL GKSKRENKNG
NDAVIPGTLA YWRFDGSAHS SNSSGSSPGS ALAEFDIIKD LSGHGNDLVT KSANASSQHT
ILWSDQHHPS QPGYGSLKFT GQKKPLKGMY LQTLKQAPLN SETFENGYTF EAFYLVPSSW
NSEQNAWSGI FSRRGSAGEA NKHSNDTDSD EPIVTLSLSN DRELQWRVYP LHQDGGTTNW
GHETPFDRWW HVAVINNGTL TKMYVDGSEV ARNPTQWVPG LTTLNKPWML GGFEYGGKLD
QIFFGSIGDV RIVNRALSLD ELMFQENQ
//