ID   KEX1_LEPMJ              Reviewed;         641 AA.
AC   E5R540;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Pheromone-processing carboxypeptidase KEX1;
DE            EC=3.4.16.6;
DE   AltName: Full=Carboxypeptidase D;
DE   Flags: Precursor;
GN   Name=KEX1; ORFNames=Lema_P047160;
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS   (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Leptosphaeria; Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8;
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria maculans
RT   genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(2011).
CC   -!- FUNCTION: Protease with a carboxypeptidase B-like function involved in
CC       the C-terminal processing of the lysine and arginine residues from
CC       protein precursors. Promotes cell fusion and is involved in the
CC       programmed cell death (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential release of a C-terminal arginine or lysine
CC         residue.; EC=3.4.16.6;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; FP929083; CBX92010.1; -; Genomic_DNA.
DR   RefSeq; XP_003835375.1; XM_003835327.1.
DR   AlphaFoldDB; E5R540; -.
DR   SMR; E5R540; -.
DR   STRING; 985895.E5R540; -.
DR   MEROPS; S10.007; -.
DR   EnsemblFungi; CBX92010; CBX92010; LEMA_P047160.1.
DR   GeneID; 13284615; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_0_1; -.
DR   InParanoid; E5R540; -.
DR   OMA; EMADQFV; -.
DR   OrthoDB; 607679at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
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; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   3: Inferred from homology;
KW   Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus; Hydrolase;
KW   Membrane; Protease; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..641
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411923"
FT   TOPO_DOM        36..515
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        516..536
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        537..641
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          472..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          585..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        182
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        382
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        444
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        433
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   641 AA;  72004 MW;  EBC87398725E1F59 CRC64;
     MASTYSTPRW RTALLGGFLT TLPWLSSGMA GKTQADYFIK SLPGAPEPLL KMHAGHIEVD
     AEHNGNLFFW HYENRHIADR QRTVLWLNGG PGCSSMDGAL MEVGPYRVQA DGNLHYNNGS
     WDEFANLLFV DQPVGTGFSY VNTDSYLTEL DQMANHMVIF LEKWFGLFPE YEHDDLYIAG
     ESYAGQHIPY IARAIVKRNK EQGKTPWALK GLLIGNGWIS PVDQYLSYIP YAYQNGLMKA
     DSDMAKRVEN QQRICIKKLE DGGMDAVDTN DCEQIMVNIL EETKDRKADR MNQCVNMYDI
     RLRDDASCGM NWPPDLASVT PYLRRPDVIQ ALHINPDKKT GWQECNGAVS GHFRAKKSEP
     SVRFLPELIP EVPTLLFSGD KDFICNHIGT EEMIKNMQWS GGKGFEVTPG VWAPKQDWTF
     EGEAAGSWQE ARNLTYVVFY NSSHMVPFDY PRRTRDMLDR FMGVDIEQIG GVPSDSRIDG
     EKGPLTSVGD HPNSTRAEED KATDVKQAEW KAYYRSGQVA LVVVVIVAAL WGIFLWRSRR
     RHTKTAYQGD DGDEGRESLL TGMGLDNFRR KERRSDLEAA DFDERELDDL DGASKKPGNG
     YASLGSEKER QSHNDSTFSL GGDSDDEAGS SDGPKRKGGS S