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Database: UniProt
Entry: A0A0M8MPA9_9BASI
LinkDB: A0A0M8MPA9_9BASI
Original site: A0A0M8MPA9_9BASI 
ID   A0A0M8MPA9_9BASI        Unreviewed;       551 AA.
AC   A0A0M8MPA9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE            EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN   ORFNames=Malapachy_2994 {ECO:0000313|EMBL:KOS16516.1};
OS   Malassezia pachydermatis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS16516.1, ECO:0000313|Proteomes:UP000037751};
RN   [1] {ECO:0000313|EMBL:KOS16516.1, ECO:0000313|Proteomes:UP000037751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS16516.1,
RC   ECO:0000313|Proteomes:UP000037751};
RA   Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT   "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT   pachydermatis CBS1879.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a diacylglycerol + H2O = a fatty acid + a monoacylglycerol +
CC         H(+); Xref=Rhea:RHEA:32731, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17408, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868;
CC         Evidence={ECO:0000256|ARBA:ARBA00043665};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a monoacylglycerol + H2O = a fatty acid + glycerol + H(+);
CC         Xref=Rhea:RHEA:15245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17408, ChEBI:CHEBI:17754, ChEBI:CHEBI:28868;
CC         Evidence={ECO:0000256|ARBA:ARBA00043831};
CC   -!- SIMILARITY: Belongs to the peptidase S10 family.
CC       {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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:KOS16516.1}.
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DR   EMBL; LGAV01000001; KOS16516.1; -; Genomic_DNA.
DR   RefSeq; XP_017994148.1; XM_018137475.1.
DR   AlphaFoldDB; A0A0M8MPA9; -.
DR   GeneID; 28729351; -.
DR   VEuPathDB; FungiDB:Malapachy_2994; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000037751; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802:SF64; CARBOXYPEPTIDASE 2-RELATED; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW   ECO:0000256|RuleBase:RU361156};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361156};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361156};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037751};
KW   Signal {ECO:0000256|RuleBase:RU361156}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT   CHAIN           19..551
FT                   /note="Carboxypeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT                   /id="PRO_5006517802"
SQ   SEQUENCE   551 AA;  61129 MW;  4958144D0D06C155 CRC64;
     MLLYSIVALA TSITAVSAQF VKPPTDLKKV SGHAGTTVRY KEVPAGICET TEGVKSYSGY
     VDTEKDEHIF FWYFESRKDP KNAPLTVWFN GGPGSSSMIG LFQEVGPCGI YPNGTLYNNE
     YAWNSESNLL IVDQPVTTGF SYSEVGPVIM DTRGIVVKEL EDNKCPDDTH FFETCATLSL
     PSKTKAPKST SQAAPAMWKT VQGFLGAFPE LENAPITIAT ESYGGHYAPT FATYFLEQND
     KNVEGAILLN LKSVMIGNGW YDPKVQYMAF YNFTVSPGNT YDLKPFSKEK GEDLYTQVFG
     HGMCLDLIED CYRTNSASVC RKADGFCASS VEQFLTRHAH RDEYDIRQVD PDRFPYSRYA
     SYLNEAHVLK AIGAFQNYTE SSDLIWKSFS KTGDDARRRG SISKLRELVK RGITVTLYAG
     DADYNCNWLG GEIVAEKVGG ASFSKAGYQN ITSKNKDVPG QVKQHGRFSF ARIYYSGHEV
     PFYQPIAASE LHHRTVHGLD LATGQEAVSD GYVTKGSPKS EFREGGDTVQ HHIAKTGSLY
     DFKKHIPVKP N
//
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