ID   KEX1_PARBA              Reviewed;         640 AA.
AC   C1GP85;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   22-FEB-2023, entry version 61.
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=PAAG_00330;
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01;
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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; KN293992; EEH36007.1; -; Genomic_DNA.
DR   RefSeq; XP_002797791.1; XM_002797745.2.
DR   AlphaFoldDB; C1GP85; -.
DR   SMR; C1GP85; -.
DR   STRING; 502779.C1GP85; -.
DR   ESTHER; parba-kex1; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   GlyCosmos; C1GP85; 4 sites, No reported glycans.
DR   GeneID; 9100876; -.
DR   KEGG; pbl:PAAG_00330; -.
DR   VEuPathDB; FungiDB:PAAG_00330; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_0_1; -.
DR   OMA; EMADQFV; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000002059; Partially assembled 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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..640
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411931"
FT   TOPO_DOM        25..520
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        521..541
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        542..640
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          478..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..640
FT                   /note="Disordered"
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        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   640 AA;  71356 MW;  71F91973FF0E0B4B CRC64;
     MGFSGSRANT ALGAWSKWLT LCLAMTQPFS VTAKSAADYY VHSLPGQPEG PLLKMHAGHI
     EISPETSGNL FFWHFENRHI ADKPRTVVWL NGGPGCSSED GALMEIGPYR LIDKETLNYT
     EGSWDEFANL LFVDQPVGTG FSYGSTEHYV HELDEMASQF VTFLEKWFEI FPHYEPDDLY
     FAGESYAGQY IPYIARAILD RNKKQDVLAN NRVWNLKGLL IGNGWISPQH QYPAYLPYVY
     QEGVVQGGTQ EANLIEAKAA KCMKELNVED TTGTVHIPDC EDILQAILDY THKGKRCINM
     YDIRLTDEYS ACGMNWPPDL KDVQPYLRRK DVVKALHINE EKQTGWTECA GAVGSSFKAR
     KSKPAVELLP GLLEEGLPIL LFSGQKDLIC NHIGTEDMIK NMKWSGGTGF ELSPGVWAPR
     QYWTFEGEPA GIYQQARNLT YVLFYNASHM VPFDYPRRTR DMLDKFLGVD ITHIGGDPAD
     SRIDGEKGPT TSVGAHPNST AAAEREKEKL NTAAWKAYYK SGEVALIIVS TAAVVWGIFL
     WRSRRKHQSS GYRSIYPMLG LNSTGSLGRF SHKHSRGNGD IEAADFDETE LDGQPSQAFL
     SRSSGDGETY AVGEESSDEE DGASDGQQLM FDQSRGEGRS
//