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Database: UniProt
Entry: A0A067P129_PLEOS
LinkDB: A0A067P129_PLEOS
Original site: A0A067P129_PLEOS 
ID   A0A067P129_PLEOS        Unreviewed;       618 AA.
AC   A0A067P129;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Pheromone-processing carboxypeptidase KEX1 {ECO:0000256|ARBA:ARBA00040628};
DE            EC=3.4.16.6 {ECO:0000256|ARBA:ARBA00038895};
DE   AltName: Full=Carboxypeptidase D {ECO:0000256|ARBA:ARBA00042717};
DE   AltName: Full=Pheromone-processing carboxypeptidase kex1 {ECO:0000256|ARBA:ARBA00040403};
GN   ORFNames=PLEOSDRAFT_1096672 {ECO:0000313|EMBL:KDQ29586.1};
OS   Pleurotus ostreatus PC15.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX   NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ29586.1, ECO:0000313|Proteomes:UP000027073};
RN   [1] {ECO:0000313|Proteomes:UP000027073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential release of a C-terminal arginine or lysine
CC         residue.; EC=3.4.16.6; Evidence={ECO:0000256|ARBA:ARBA00001003};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000256|ARBA:ARBA00004393}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004393}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family.
CC       {ECO:0000256|ARBA:ARBA00009431}.
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DR   EMBL; KL198007; KDQ29586.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067P129; -.
DR   STRING; 1137138.A0A067P129; -.
DR   MEROPS; S10.007; -.
DR   VEuPathDB; FungiDB:PLEOSDRAFT_1096672; -.
DR   HOGENOM; CLU_008523_11_1_1; -.
DR   InParanoid; A0A067P129; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000027073; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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; IPR033124; Ser_caboxypep_his_AS.
DR   PANTHER; PTHR11802:SF190; PHEROMONE-PROCESSING CARBOXYPEPTIDASE KEX1; 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; PS00560; CARBOXYPEPT_SER_HIS; 1.
PE   3: Inferred from homology;
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027073};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..618
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001642772"
FT   TRANSMEM        517..541
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          552..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..570
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..595
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..618
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  68323 MW;  9FB6989198BB2184 CRC64;
     MRSTLCTKII LFGWAVAASI RGTLAASAGS DVPSAASFYV PSLPDLHQDS LHPLRIYSGH
     LSSDTSKDAS SSTDVTPHLF FVLVKNRRTA DKERVMFWFN GGPGCSSFDG LMMEVGPWRM
     DGKGGFKVVE GGWEEYTTMV YIDQPAGTGF SYTSTNKLVE GMSEASAQLL VFLENFYKVF
     PEYRTMDTYL GGESFAGQYI PFFADAILNS SLGTRLMGVA IGNGWIDGRR QYPAYIDYAV
     KMGILVENSE DWKYAKAETD ACVAEFDKFT EFEPGNVPRC ERLVLDVARG RNKEKDGSPM
     CINIYDVRYD DTKPACGMNW PPDIKPITTY LDRPEVVKAL HAEAHSEAWV ECRGAIHSAF
     NRRENNSSIT ILPSVIERIP VLIFAGDQDL ICNHVGLEAM IQAMTWNGAK GLGVVQTQSW
     SVAGTPAGTW VSSRNLTYAK IFNASHMAPF DVPHVTHDMI LRFMGVNFSA IMDGSARIPS
     SVGTIMKPIF IEDSEASKTP APVPGKTPEQ DKAMWEAYYN AGSAALVLVL IFLALGTFLW
     CRIRRRRVQL PVSHQDEESI PLNSSIAMNG RQDGEEEDSA SFKSRKGKER AVEPPEPPIF
     ELGESDDEDM KSPSRKQS
//
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