KEX1_MAGO7
ID KEX1_MAGO7 Reviewed; 634 AA.
AC A4RE47; G4NEK4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 77.
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=MGG_00775;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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; CM001235; EHA48634.1; -; Genomic_DNA.
DR RefSeq; XP_003718218.1; XM_003718170.1.
DR AlphaFoldDB; A4RE47; -.
DR SMR; A4RE47; -.
DR STRING; 318829.MGG_00775T0; -.
DR MEROPS; S10.007; -.
DR EnsemblFungi; MGG_00775T0; MGG_00775T0; MGG_00775.
DR GeneID; 2675037; -.
DR KEGG; mgr:MGG_00775; -.
DR VEuPathDB; FungiDB:MGG_00775; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_0_1; -.
DR InParanoid; A4RE47; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000009058; Chromosome 5.
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..634
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411925"
FT TOPO_DOM 25..512
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..634
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 468..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 177
FT /evidence="ECO:0000250"
FT ACT_SITE 378
FT /evidence="ECO:0000250"
FT ACT_SITE 440
FT /evidence="ECO:0000250"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 634 AA; 70579 MW; E7AB2907441E625F CRC64;
MKLAMRRAST FALLALSWSA AVSAASSAGD YFVRSLPGAP PGPLVKMHAG HIEVSPEKNG
NLFFWHFQNK HIANRQRTVI WLNGGPGCSS EDGALMEVGP YRLKDDHTLV PNEGSWHEFA
NLMFVDNPVG TGFSYVNTDS YVTELDEMAD QFVIFLEKFF ELFPEYSQDD IYIAGESFAG
QHIPYIAKHI LDRNKNSMTK IKWNLKGLLI GNGWIAPNEQ YRAYLDFSYS KGLLDKNSET
AKTLEAQHKD CAKEWEDNGP KVDVAKCESV LQTLLKLSSK VEADGKRHCV NMYDVRLRDT
YPSCGMNWPP DLVNVTPYLR RKDVVEALHV NPNKATGWTE CTGAVGQSFK AQKSKPSIDL
LPKILEEVPI LLFSGAEDLI CNHIGTEAFI GKMTWNGGKG FEVTPGTWAP RRDWTFEGKD
AGFWQEARNL TYVLFKDSSH MVPFDFPRRS RDMLDRFMGV DISSIGGNPT DSRLDGEKLP
ETTVGGAAGN STSKQEEEKK KLDEAKWYAY RKSGEVVLVI VAVAAVAWGW YVWRDRRRRR
GYQGIFGGSP SESTTRLPGL GSRISSTPSG LEGFRSKRQN GRDVEAGDFD ESELDDLHTQ
TPTDARYSVG ADSDDEEDAS GSRKEGGPSG GRGR
