ID A8PVL2_MALGO Unreviewed; 404 AA.
AC A8PVL2;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 28-FEB-2018, entry version 52.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDP44417.1};
GN ORFNames=MGL_0899 {ECO:0000313|EMBL:EDP44417.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966)
OS (Dandruff-associated fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP44417.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP44417.1, 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
RT divergent virulence traits shared with plant and human fungal
RT pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|RuleBase:RU004386}.
CC -!- CAUTION: The sequence shown here is derived from an
CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC preliminary data. {ECO:0000313|EMBL:EDP44417.1}.
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DR EMBL; AAYY01000003; EDP44417.1; -; Genomic_DNA.
DR RefSeq; XP_001731631.1; XM_001731579.1.
DR ProteinModelPortal; A8PVL2; -.
DR STRING; 425265.XP_001731631.1; -.
DR MEROPS; M18.A01; -.
DR GeneID; 5855937; -.
DR KEGG; mgl:MGL_0899; -.
DR EuPathDB; FungiDB:MGL_0899; -.
DR eggNOG; KOG2596; Eukaryota.
DR eggNOG; COG1362; LUCA.
DR InParanoid; A8PVL2; -.
DR KO; K01267; -.
DR OrthoDB; EOG092C3JCE; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 2.30.250.10; -; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; PTHR28570; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW Complete proteome {ECO:0000313|Proteomes:UP000008837};
KW Hydrolase {ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|RuleBase:RU004386};
KW Reference proteome {ECO:0000313|Proteomes:UP000008837};
KW Zinc {ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 404 AA; 44874 MW; A7B43EFFC6A801F9 CRC64;
MLENAGFRKL HEHQTWNEKL YVGGRYYVQR NQSSLLAFVI GKKYEAGQGV HIVGAHTDSP
NLRIRPVSRR TKEGYLQCSV ETYGGGIWHT WFDRDLSLAG RVIVTSDKEQ SRFVSRLVHI
RRPLLRVPTL AIHLNRSANE AFKFNQEDQL QPIMGLADML NQPRSTPDAD AVGKPTMASK
HHPVLLELLA QELEVPVEFI QDFELSLFDT NAPTAGGVSN EFLFTPRVDN QMSCFCATEA
LIASVLDLDA LDRATSIRAI ALFDNEEVGS VSYQGAESNL LWSMLHRLAG LRVIGAPEST
ASAQDLTEQS LSRSFLISSD TAHAVHPNYA SVHEEHLRPK LNGGPVIKTN AKQRYASTAV
TTFLLRRIAK KAGVPLQEFE VRNDCPCGST IGPMLSKVRV SEDN
//
