ID   KEX1_METAQ              Reviewed;         616 AA.
AC   E9E1Z2;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 38.
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=MAC_03847;
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102;
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(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; GL698493; EFY90089.1; -; Genomic_DNA.
DR   RefSeq; XP_007810187.1; XM_007811996.1.
DR   AlphaFoldDB; E9E1Z2; -.
DR   SMR; E9E1Z2; -.
DR   STRING; 92637.XP_007810187.1; -.
DR   ESTHER; metaq-kex1; Carboxypeptidase_S10.
DR   EnsemblFungi; EFY90089; EFY90089; MAC_03847.
DR   GeneID; 19248158; -.
DR   KEGG; maw:MAC_03847; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_0_1; -.
DR   InParanoid; E9E1Z2; -.
DR   OMA; EMADQFV; -.
DR   OrthoDB; 607679at2759; -.
DR   Proteomes; UP000002499; 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..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..616
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411926"
FT   TOPO_DOM        29..516
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        517..537
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        538..616
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          468..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        183
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        382
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        444
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        433
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   616 AA;  69034 MW;  D823B29F04A4F26D CRC64;
     MAPRFSWSFA TSWHALAILA LWPVSTLAGD KSAADYYVRE LPGLPKDSPP IKMHAGHIEV
     TPETNGNLFF WHFQNNHIAN RQRTVVWLNG GPGCSSEDGA LMEVGPYRVT KDNALTLNNG
     TWNEFANLLF VDNPVGTGFS YVDTNSYIHG LNAMATQFIT FLEKFFALFP EYESDDLYFA
     GESYAGQHIP YIAKAILDRN KLKSRAETWK LSGLLIGNGW ISPQDQSSAY LKFSLEKGLI
     EKGSDNAQQL QHMQRICDKE MSINPGHVDY PECESILNKI LELTREGSGD QACINMYDVR
     LRDSAPSCGM NWPPDLKYVG PYLRQPQVIS ALNLDKQRNT GWQECNSMVN ANFRNQNATA
     SISLLPDILK EVPILLFSGA EDLICNHVGT EELISNLAWN EGKGFEVTPG NWAPRRQWTF
     EGEVAGFWQE ARNLTYVLFH NASHMVPFDY PRRSRDMLDR FMKVDISSIG GQPSDSRIDG
     EKGPDTSVGG AKNNTQQHEE ETKQKLNEAK WHAYQRSGEV VLVIVIIAAS VWGYFVWRQR
     RKGAAYSALQ NDEAAGQSRT GLAAFHDRQS DRDLEAAAFD ETTVDNIPLQ ESIGRGESKY
     SIGDDSDEEE EGTTKT