ID   KEX1_UNCRE              Reviewed;         638 AA.
AC   C4JTD3;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-MAY-2023, entry version 52.
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=UREG_05722;
OS   Uncinocarpus reesii (strain UAMH 1704).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX   NCBI_TaxID=336963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 1704;
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; CH476617; EEP80880.1; -; Genomic_DNA.
DR   RefSeq; XP_002585033.1; XM_002584987.1.
DR   AlphaFoldDB; C4JTD3; -.
DR   SMR; C4JTD3; -.
DR   STRING; 336963.C4JTD3; -.
DR   ESTHER; uncre-kex1; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   GlyCosmos; C4JTD3; 6 sites, No reported glycans.
DR   GeneID; 8439360; -.
DR   KEGG; ure:UREG_05722; -.
DR   VEuPathDB; FungiDB:UREG_05722; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_0_1; -.
DR   InParanoid; C4JTD3; -.
DR   OMA; EMADQFV; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000002058; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C: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; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
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.
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..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..638
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411949"
FT   TOPO_DOM        33..519
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        520..540
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        541..638
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          586..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..601
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..626
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        184
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        386
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        448
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        203
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        246
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        437
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        445
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        497
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   638 AA;  71903 MW;  E9974ECF7A5C0FF0 CRC64;
     MSSCQPPPFL SSMVVRWLSV WIILASSAFA SAKCAADYYV RSLPGQPEGP LLKMHAGHIE
     VDHENNGNLF FWHFQNRHIA NRQRTVIWLN GGPGCSSMDG AMMEVGPYRL KDDHTLKYNE
     GSWDEFANLL FVDQPVGTGY SYANTNSYLH ELDEMAAHFV TFMERWFELF PEYEHDDLYF
     AGESYAGQYI PYIAKAILDR NKNETVIAQR RLWHLKGLLI GNGWFSPVEQ YLSYLPYVYK
     EGMVKNDSDE AKGIERAHSD CVAELDRAKG DVKIHVDVCE KILSAILDVS NKSGHCVNMY
     DVRLTDTFPS CGMNWPPDLK HLAPYLRRDD VTSALHINKD KKTGWTECAG AVSSSFRPRK
     SKPSADLLPG LLESGVRIGL FSGAKDLICN HIGTEEFINK MEWSGGKGFE LSPGVWAPRR
     DWTFEGETAG YYQEARNLTY VLFYNASHMV PFDYARRSRD MLDRFLGVDI TSIGGNPTDS
     RIDGEKGALT SVGNHPNSTL AEQREKEKLK AATWKAYYKS GEVALVVVVI AAGAWGFFLW
     RSRRQRQGSG YLGIYPSLNG LSSGSLPRYR NKRSSRDIEA AAEFEASELE TLHDMDDRSP
     GPSRDNYSVG EDSETEDEKR YPPTDFDRQD GTPSASRT
//