ID   KEX1_COCP7              Reviewed;         641 AA.
AC   C5P635;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, 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=CPC735_035110;
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; ACFW01000025; EER28175.1; -; Genomic_DNA.
DR   RefSeq; XP_003070320.1; XM_003070274.1.
DR   AlphaFoldDB; C5P635; -.
DR   SMR; C5P635; -.
DR   MEROPS; S10.007; -.
DR   EnsemblFungi; EER28175; EER28175; CPC735_035110.
DR   GeneID; 9695815; -.
DR   KEGG; cpw:CPC735_035110; -.
DR   VEuPathDB; FungiDB:CPC735_035110; -.
DR   HOGENOM; CLU_008523_11_0_1; -.
DR   Proteomes; UP000009084; 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   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus; Hydrolase;
KW   Membrane; Protease; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..641
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411914"
FT   TOPO_DOM        35..522
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        523..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        544..641
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          486..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..627
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        188
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        389
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        451
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        440
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        448
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        500
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   641 AA;  71773 MW;  DF5FE3A9BC27E772 CRC64;
     MRSTSTFTRT PAFLLHTLAR WLLVWGVLGS SVVAEKKCAS NYYVRSLPGQ PDGPLLKMHA
     GHVEVDHKNN GNLFFWHFQN RHIANRQRTV IWLNGGPGCS SMDGALMEIG PYRLKDDHTL
     IYNEGSWDEF ANILFVDQPV GTGFSYVNTN SYIHELDEMA SHFVTFLEKW FELFPEYEHD
     DLYFAGESYA GQYIPYIAKA ILDRNKNTTT QAQSRLWNLK GLLIGNGWIS PVEQYQAYLT
     YAYKENLIQS GTDAAKRVER AHSECISELD SGGKDRIHAG ACEKVLSAVL EVTRENGKCI
     NMYDIRLRDE FPSCGMNWPP DLKHITPYLR RDDVISALHV NDDKRTGWRE CTGAVSSNFN
     ARNSKPSVQL LPEILESGIP ITLFSGAKDF ICNHIGTEQF IHNMQWSGGT GFELSPGVWA
     PRHDWTFEGE AAGYYQEARN LTYVLFYNAS HMVPFDFGRR SRDMLDRFLG VDITSIGGNP
     ADSRIDGEKG ALTSVGNHPN STTAEQREKE KLKAATWAAY YKSGEVALVV VAIAAAVWGF
     FIWRSRRQRQ GSGYRGIYPN LNGLSSGSFS GFRNKRSSHD DIEAAADFDA SELDTLRGTD
     DRSRGANGHG SVGGDSEDED EKFGAQKESY HPSNMPSSSS S