ID   A8PSM7_MALGO            Unreviewed;       554 AA.
AC   A8PSM7;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE            EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN   ORFNames=MGL_0285 {ECO:0000313|EMBL:EDP45296.1};
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:EDP45296.1, ECO:0000313|Proteomes:UP000008837};
RN   [1] {ECO:0000313|EMBL:EDP45296.1, 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   -!- 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:EDP45296.1}.
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DR   EMBL; AAYY01000001; EDP45296.1; -; Genomic_DNA.
DR   RefSeq; XP_001732510.1; XM_001732458.1.
DR   AlphaFoldDB; A8PSM7; -.
DR   STRING; 425265.A8PSM7; -.
DR   MEROPS; S10.001; -.
DR   GeneID; 5856816; -.
DR   KEGG; mgl:MGL_0285; -.
DR   VEuPathDB; FungiDB:MGL_0285; -.
DR   InParanoid; A8PSM7; -.
DR   OMA; AIANNMS; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000008837; 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; 1.10.287.410; -; 1.
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:SF452; CARBOXYPEPTIDASE; 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:UP000008837};
KW   Signal {ECO:0000256|RuleBase:RU361156}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT   CHAIN           20..554
FT                   /note="Carboxypeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT                   /id="PRO_5006521990"
SQ   SEQUENCE   554 AA;  61954 MW;  8FBA101E52F70376 CRC64;
     MARISVVLCL LAFCAYVHAQ FALMDSALSR FMSVTSQIFH TLKKPSSAIP LASWNPWTSN
     SRIQAGNLSA WLGVRIESIG GIKYQRLFLP LFPDYQLRVA MDENDDEENN DETPFCDPKV
     KQIKGYLDIR EDAHLWFTMF ESRSDPSKDP LVLWLNGGPG CSSSTGMLFE LGPCWVSQQG
     EGTTYNEHSW NSQANLLFLD QPLQVGYSYS DSGEFVDTSN KSAEDVYAFL QLFFARFPKY
     ADLPFTVAAE SYGGHYAPHI GAEIHRRNKE LANLPDNYLA TAKPIRLDSL MIGNGLTDPP
     VQFPSVVEYA CSPENKYHLF DRESETCKTL EAKSEVCTKL MNLCEKMDSR LSCVPAALYC
     WGSLYGPAQD TGVNLYDVRR KCDHEKDGDL CYPEMEHIET LLNKPRIKKM LGVPATVDFQ
     SCNMQVNARF MMQGDSMQNS ATLLAPLLAD GIRVLAYAGE ADFMCNAIGI HEWILDFQNV
     YREAINNATE TPMFTHSVNG AKPRQAGFVI KAGKGAGNLA FAWIQRAGHM VPHDQPAVAL
     TMLNRWLANE DLTV
//