ID   KEX1_PYRTR              Reviewed;         639 AA.
AC   B2W340;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
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=PTRG_03838;
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP;
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
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; DS231617; EDU46676.1; -; Genomic_DNA.
DR   RefSeq; XP_001934171.1; XM_001934136.1.
DR   AlphaFoldDB; B2W340; -.
DR   SMR; B2W340; -.
DR   STRING; 45151.EDU46676; -.
DR   MEROPS; S10.007; -.
DR   EnsemblFungi; EDU46676; EDU46676; PTRG_03838.
DR   GeneID; 6342074; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_0_1; -.
DR   InParanoid; B2W340; -.
DR   OMA; EMADQFV; -.
DR   OrthoDB; 625787at2759; -.
DR   Proteomes; UP000001471; Unassembled WGS sequence.
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..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..639
FT                   /note="Pheromone-processing carboxypeptidase kex1"
FT                   /id="PRO_0000411943"
FT   TOPO_DOM        31..517
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        518..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        539..639
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          477..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..639
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        183
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        384
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        446
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        443
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        495
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   639 AA;  71619 MW;  7F261923AB81FA5A CRC64;
     MAFSHAPSGW RTALLAGLIA TVAWLPAIVA QEKTQADYFI HDLPGAPKPL LKMHAGHIEV
     DAEHNGNLFF WHYQNRHIAD RQRTVLWLNG GPGCSSMDGA MMEIGPYRVR EGGKLEYNNG
     SWDEFANLLF VDQPVGTGFS YVNTDSYLTE LDQMAAHMVI FLEKWFALFP EYENDDLYIA
     GESYAGQHIP YIARAILDRN KKNQAKSPWP LKGLLIGNGW MSPVDQYLSY IPFAYQNGLM
     RSGTDMAKRV EEQQRICVQK LEAGGMDAVD TRDCEQIMVR ILQETKNENA DPMNQCLNMY
     DIRLRDDSSC GMNWPPDLAQ VTPYLRRADV VQALHINTDK KTGWQECNGA VSSHFRAKNS
     KPSVKFLPEV IEQVPVLLFS GDKDFICNHV GTEAMIQNLQ WNGGKGFEAS PGVQNAKQDW
     MFEGEAAGTW QEARNLTYVV FYNSSHMVPF DYPRRTRDML DRFMGVNIEA IGGAPADSLI
     DGEKGPLTSV GDHPNSTKAE EDKSKELKAA EWKAYTRSGE VALVIAVIVA CICGFLLCRS
     RRAKSAYKGD DSDEGRESLL TGMGLDNFRR KERRQDVEAA DFDERELDEV PKKSGKGYGQ
     ISSEKGRVPH NDSSFSLGVD SDDDEAGSSD RGRRKEESR