ID A8PVL2_MALGO Unreviewed; 404 AA.
AC A8PVL2;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 10-FEB-2021, entry version 62.
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) (Dandruff-associated
OS 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 divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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:EDP44417.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAYY01000003; EDP44417.1; -; Genomic_DNA.
DR RefSeq; XP_001731631.1; XM_001731579.1.
DR MEROPS; M18.A01; -.
DR EnsemblFungi; EDP44417; EDP44417; MGL_0899.
DR GeneID; 5855937; -.
DR KEGG; mgl:MGL_0899; -.
DR VEuPathDB; FungiDB:MGL_0899; -.
DR InParanoid; A8PVL2; -.
DR OMA; GHAVHPN; -.
DR OrthoDB; 769270at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:EnsemblFungi.
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|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU004386};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW Reference proteome {ECO:0000313|Proteomes:UP000008837};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, 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
//
