KEX1_SCLS1
ID KEX1_SCLS1 Reviewed; 642 AA.
AC A7EYY7;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=SS1G_10553;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(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; CH476636; EDN94679.1; -; Genomic_DNA.
DR RefSeq; XP_001588107.1; XM_001588057.1.
DR AlphaFoldDB; A7EYY7; -.
DR SMR; A7EYY7; -.
DR STRING; 665079.A7EYY7; -.
DR MEROPS; S10.007; -.
DR GeneID; 5484474; -.
DR KEGG; ssl:SS1G_10553; -.
DR VEuPathDB; FungiDB:sscle_09g071760; -.
DR InParanoid; A7EYY7; -.
DR OMA; EMADQFV; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
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..30
FT /evidence="ECO:0000255"
FT CHAIN 31..642
FT /note="Pheromone-processing carboxypeptidase kex1"
FT /id="PRO_0000411945"
FT TOPO_DOM 31..522
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 480..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 451
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 642 AA; 71339 MW; D074077567B63989 CRC64;
MRSLTTKTSS ALLTVWGLLS VSLMPSVGQA DKTAGDYFVH SLPGAPAGPL LKMHAGHIEV
TPEHHGNIFF WHFQNRHIAN KQRTVIWLNG GPGCSSEDGA LMEIGPYRVK DGSNGPKLEY
NPGSWDEFAN VMFVDNPVGT GFSFVDSDSY IHDLPEMADQ FVQFLEKWFA LFPEYEHDDL
YLAGESYAGQ HIPYITKAIL ERNKKPDAKH KWPVKGMLIG NGWISPVEQY MSYLPFAYEK
GLVKKDSEKA KKLESQQAIC TKMLNENGGR DKVDNSQCEQ ILQEILSTTQ SKGSDGNMQC
YNMYDVRLKD SYPSCGMNWP PDLVNVTPYL RRSDVVAALH ISPEKRTGWT ECNGAVGSAF
RAANSKPSIQ ILPELLAEVP TILFSGAEDL ICNHIGTEEL ISNMEWNGGK GFELGSGTWA
PRRDWEFEGE PAGFWQEARN LTYVLFYNSS HMVPFDYARR TRDMLDRFMK VDIASIGGAP
TDSRIDGEKG LETSVGGHPN STAAAEAEEE RLEAAKWNAY YKSGEIVLVI VVIAASAWGY
YIWRERRQRA GYAGIFGGDT PMALAGARSG SRGAAGLEDF RNKRNARDVE AADFDESELD
ELHVRSPTDD MDRDRYSVGS ASDDESIGKR NGNGKGKEKS YS
