ID   KEX1_VERA1              Reviewed;         635 AA.
AC   C9S688;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, 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=VDBG_00507;
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136;
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS985214; EEY14400.1; -; Genomic_DNA.
DR   RefSeq; XP_003008826.1; XM_003008780.1.
DR   AlphaFoldDB; C9S688; -.
DR   SMR; C9S688; -.
DR   STRING; 526221.C9S688; -.
DR   MEROPS; S10.007; -.
DR   EnsemblFungi; EEY14400; EEY14400; VDBG_00507.
DR   GeneID; 9529181; -.
DR   KEGG; val:VDBG_00507; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_0_1; -.
DR   OMA; EMADQFV; -.
DR   Proteomes; UP000008698; 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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..635
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411952"
FT   TOPO_DOM        25..524
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        525..545
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        546..635
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          464..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..589
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..635
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        376
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        438
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        427
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   635 AA;  71005 MW;  23BDD5BA32051919 CRC64;
     MAPAIRQLAT GLLLALSWAP TTRADSSAAD YYVKSLPGQP AGPPVKMHAG HIETDADHNG
     NLFFWHFENK HIAQRQRTVI WLNGGPGCSS EDGAMMEIGP YRVKGDQLVN NNGSWHEFAN
     LLFVDNPVGT GFSYVDTNSY LHELDEMGDQ FILFLEKFFK LFPQYAQDDL YFAGESYAGQ
     HIPYIAKHIL ERNEKAGPDD QWNLKGLVIG NGWISPFEQY GSYLKFAYEK GLLAQGSEKA
     KQLEQQWKIC RKQMAVDIKI DISECEAILQ KILDVTATLT TSGKRNCYNM YDVRLKDTYP
     SCGMNWPPDL TDVTPYLRRK DVTEALHINA AKNTGWKECN GAVGSAFRAH KSKPSRDLLP
     DLLKKVPITL FSGAEDLICN HIGTEEMIGN MEWNGAKGFE VSPGNWAPRR DWTFEGKDAG
     FWQEARNLTY VLFKEASHMV PFDWPRRSRD MIDRVMKVDI SAIGGEPTDS RIDGEKGPVT
     SVPPSKGSNN HPDTKPGGGD KGSSTNDDET QKQVDEAKWK AYYRSGEIVL VIVVIAAGLW
     GWYIWRDRRR RSGYQGVAGG DGAGPGHRAG ARGLDRFQDR RTARDVETGD FDESELDDLH
     VETPREGPHK EAYAIGDDSD EEDIKGKGPE RSGTR