KEX1_COLGM
ID KEX1_COLGM Reviewed; 622 AA.
AC E3QDT3;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 45.
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=GLRG_04165;
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212;
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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; GG697343; EFQ29021.1; -; Genomic_DNA.
DR RefSeq; XP_008093041.1; XM_008094850.1.
DR AlphaFoldDB; E3QDT3; -.
DR SMR; E3QDT3; -.
DR STRING; 645133.E3QDT3; -.
DR ESTHER; colgm-kex1; Carboxypeptidase_S10.
DR PRIDE; E3QDT3; -.
DR EnsemblFungi; EFQ29021; EFQ29021; GLRG_04165.
DR GeneID; 24409530; -.
DR VEuPathDB; FungiDB:GLRG_04165; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_0_1; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000008782; 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 InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..622
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411916"
FT TOPO_DOM 24..509
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 465..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 437
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 622 AA; 70070 MW; DBAEAB5DEFF84EC0 CRC64;
MAILSTVPAL LFALASWAPT VAAQSAADYF VHELPGAPKE PFIKMHAGHV EVTPEHNGNI
FFWHFQNQHI ANKQRTVIWL NGGPGCSSED GALMEIGPYR VKDPDHLEYN NGSWNEFANL
LFVDNPVGTG FSFVDTNSYL HELPEMADQF VQFLEKWFAM FPEYEHDDLY ISGESYAGQH
IPYIAKHILE RNKKPGVKTP WQLKGLLMGN AWISPKEQYD AYLKYAYEKK LIEKGSPIAL
QLEQQWRICR TSLAVTNTVD FTECESVLQK LLEQTAKVNA KGERECINMY DIRLRDTFPS
CGMNWPPDLV NLTPYLRKAE VVSALHIKPQ KTTGWTECNG AVGSAFRAPN SVPSRDYLPD
LLKEVPIVLF SGAEDLICNY MGTEAMIGDM EWNGGKGFEL TPGNWAPRRD WTVEGQPAGF
WQEARNLTYI LFYNSSHMVP FDYARRSRDM LDRFMNVDIS SVGGTPTDSR LDGEQGPATS
VGDIGKNGTS ADAETQKKLD EAKWKAYYRS GEIVLVIVII AAGAWGWYVW RERRKRRGYS
GIMGNTPPIA QRGTTRGLEG FRDRRTGRDV ETGDFDESEL DDLHVTTPTV EMDKDRYSVG
GDSDDEPHDE KPSRSNGGRS GR
