ID   KEX1_AJECN              Reviewed;         634 AA.
AC   A6QX86;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=HCAG_01993;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
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; CH476655; EDN04128.1; -; Genomic_DNA.
DR   RefSeq; XP_001544946.1; XM_001544896.1.
DR   AlphaFoldDB; A6QX86; -.
DR   SMR; A6QX86; -.
DR   STRING; 339724.A6QX86; -.
DR   MEROPS; S10.007; -.
DR   EnsemblFungi; EDN04128; EDN04128; HCAG_01993.
DR   GeneID; 5449542; -.
DR   KEGG; aje:HCAG_01993; -.
DR   VEuPathDB; FungiDB:HCAG_01993; -.
DR   HOGENOM; CLU_008523_11_0_1; -.
DR   OMA; EMADQFV; -.
DR   OrthoDB; 607679at2759; -.
DR   Proteomes; UP000009297; 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; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..634
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411896"
FT   TOPO_DOM        34..517
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        518..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        539..634
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          475..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        185
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        384
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        446
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        328
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   634 AA;  70866 MW;  40C8F861DEA7CEBD CRC64;
     MGFSEARAYR AFGGRSTWLT VFLALANSLA VSAKCAADYF VDSLPGQPDS PQVQMHAGHI
     EINHKTSANL FFWHVANQHI ADKPRTVIWL NGGPGCSSED GALMEIGPYR VTNDHLLNHT
     DGSWDEFANL LFVDQPVGTG FSYVSTGAYV SELGEMASQF VTFLEKWFEL FPHYEKNDLY
     FAGESYAGQY IPYIARAILD RNKKGESLTR WKLKGILIGN GWISPRHQYL SYLPYAYQEG
     IIQGGTDSSS RVEAKLSKCL NKLNVEDSTG TVQISACEEV LQAIIDETHK GNRCINMYDI
     RLTDEYSACG MNWPPDLENM APYLRFKNVT KALHINSDKQ TGWSECSGAV SGHFRALKSK
     PSVELLPGLL EEGLPILLFS GQKDMICNHI GNEDLIKDMK WSGGTGFELS PGVWAPRQDW
     IFEGESAGFY QQARNLTYVL FYNASHMVPF NYPPRSREML DRFIGVDIAD IGGNPADSRI
     DGEKGPATSV RAHPNSTAAA EREKEKVKSA MWKAYYKSGE VALIVVAIAA VIWGVFIWRS
     RQKHQDRGYE FRGIYPMLGS SSSGSLPRYS NKRGRRGHDV EAVNIYEAEL DERPSRVVSA
     RSSREQEPYV VGDEDGSDVD DDTSDERKRL VDKP