ID   KEX1_AJEDR              Reviewed;         638 AA.
AC   C5GC75;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 50.
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=BDCG_01958;
OS   Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces
OS   dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ER-3 / ATCC MYA-2586;
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
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; EQ999974; EEQ86838.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5GC75; -.
DR   SMR; C5GC75; -.
DR   STRING; 559297.C5GC75; -.
DR   ESTHER; ajedr-kex1; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   GlyCosmos; C5GC75; 5 sites, No reported glycans.
DR   VEuPathDB; FungiDB:BDCG_01958; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_0_1; -.
DR   OMA; EMADQFV; -.
DR   OrthoDB; 1647009at2759; -.
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; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..638
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411897"
FT   TOPO_DOM        34..520
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        521..541
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        542..638
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          477..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          566..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..638
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        185
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        387
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        449
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        438
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        446
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        498
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   638 AA;  71527 MW;  9885B53732257956 CRC64;
     MGFSETRAYS AWGAWSTWLT ICLALANLLP VTAKSAADYF VDSLPGQPEG PLVKMHAGHI
     EINPETSGNF FFWHFANSHI ADKPRTIVWL NGGPGCSSED GALMEIGPYR VTDDHMLNRT
     DGSWDEFANL LFVDQPVGTG FSYVSTGAYV SELDEMTSQF VTFMEKWFEL FPHYEKDDLY
     FAGESYAGQY IPYIARAILD RNKKESVQAQ NRQWNLKGLL IGNGWISPRH QYLSYLPYAY
     REGIIQGGTD ASLRVEATIS KCMKKLNVED TTGTIHIADC EDILQTIVDE THKGNRCINM
     YDIRLTDAYS ACGMNWPPDL KNIEPYLRYK NVTEALHINS DKQTGWTECS GAVGGNFRAL
     KSKPSVELLP RLLEEGLPIL LFSGQKDLIC NHMGTEDMIK DMKWSGGTGF ELSPGVWAPR
     QDWTFEGDSA GFYQQARNLT YVLFYNASHM VPFDYPRRTR DMLDKFIGVD ITDIGGNPAD
     SRIGGEKGPT TSVGGHPNST TAAEREKEKM KSAAWKAYYK SGEVALIVVA IAAIIWGVFI
     WRSRRQKLRN PSHEYRGIYP MLGSSSSGSL PRFSNKRGRS ADDVEAADFD ETELDERPSR
     AVSSRSSREH EPYAIGEEDG SDREGEGSDE RRRLVDKS
//