KEX1_PHYIT
ID KEX1_PHYIT Reviewed; 597 AA.
AC D0MVS1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
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=PITG_02213;
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30-4;
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
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; DS028120; EEY63734.1; -; Genomic_DNA.
DR RefSeq; XP_002907170.1; XM_002907124.1.
DR AlphaFoldDB; D0MVS1; -.
DR SMR; D0MVS1; -.
DR ESTHER; phyit-kex1; Carboxypeptidase_S10.
DR MEROPS; S10.A68; -.
DR EnsemblProtists; PITG_02213T0; PITG_02213T0; PITG_02213.
DR GeneID; 9469606; -.
DR KEGG; pif:PITG_02213; -.
DR VEuPathDB; FungiDB:PITG_02213; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_3_1; -.
DR InParanoid; D0MVS1; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000006643; Partially assembled 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: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; IPR033124; Ser_caboxypep_his_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..597
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411936"
FT TOPO_DOM 19..508
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..597
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 436
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 597 AA; 66514 MW; C8C0A32D77A6B9FA CRC64;
MVTRHVLAAA LAGSMTSAQR LHPTSQRASD DLIQNLPGLD PAAKVTQHAG RIALHDNDKN
KMFYWHFQAA QDPEKAPLVI WLNGGPGCTS MQGLFLGNSP FTLKDDSTIG KNEHSWHEFA
NLLFVDQPIG TGMSYTKGND YRLDEETIAQ DFYEFLTKFL QRHNKYLSDG DDGVSNSRAV
YMFGESHAGR WIPEFSDHIM KQNNDPKNQI KINLDGVGIG NGWVHPRIQY EYSDYAHGLG
LLTFGQVRSL KASYAECLAA LDAGTYYSRS CLDNMDSITG SVKPGNGGNS LNFYDVRQYL
RNVGSYPSGQ SNIAKYMNKM EVRKAVHGNE DKNFRFDLCS NGVFRALSKF DGVSTLDKVE
SLLQQGLRMI FYNGQWDMMC NHYGTEKLLL NLNWNGSDAY QQADKYTWRV QGRKEPAGFA
QQGGNLTYLV VTGAGHMVPM DVPDVAADIL RRFVNRLEFN DKVQTVVTTR LNATDMEVSF
CYSPSVSADP DTSLSTRDQT GANSSQVHIG IAWLWVALVI AVVSSVLAVC VTIVCIRNKR
NGKQEHEMIT QVSDDEEVNQ IEDESEEGFS DEDVGVHVLV SNVSQRATSP RSRVTEV
