ID   KEX1_PUCGT              Reviewed;         656 AA.
AC   E3L8A5;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   24-JAN-2024, 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=PGTG_18559;
OS   Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS   (Black stem rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=418459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRL 75-36-700-3 / race SCCL;
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=CRL 75-36-700-3 / race SCCL;
RX   PubMed=27913634; DOI=10.1534/g3.116.032797;
RA   Cuomo C.A., Bakkeren G., Khalil H.B., Panwar V., Joly D., Linning R.,
RA   Sakthikumar S., Song X., Adiconis X., Fan L., Goldberg J.M., Levin J.Z.,
RA   Young S., Zeng Q., Anikster Y., Bruce M., Wang M., Yin C., McCallum B.,
RA   Szabo L.J., Hulbert S., Chen X., Fellers J.P.;
RT   "Comparative analysis highlights variable genome content of wheat rusts and
RT   divergence of the mating loci.";
RL   G3 (Bethesda) 7:361-376(2017).
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; DS178373; EFP92780.2; -; Genomic_DNA.
DR   RefSeq; XP_003337199.2; XM_003337151.2.
DR   AlphaFoldDB; E3L8A5; -.
DR   SMR; E3L8A5; -.
DR   STRING; 418459.E3L8A5; -.
DR   ESTHER; pucgt-kex1; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   GlyCosmos; E3L8A5; 7 sites, No reported glycans.
DR   EnsemblFungi; EFP92780; EFP92780; PGTG_18559.
DR   GeneID; 10542492; -.
DR   KEGG; pgr:PGTG_18559; -.
DR   VEuPathDB; FungiDB:PGTG_18559; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_346513_0_0_1; -.
DR   InParanoid; E3L8A5; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000008783; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR033124; Ser_caboxypep_his_AS.
DR   PANTHER; PTHR11802:SF190; PHEROMONE-PROCESSING CARBOXYPEPTIDASE KEX1; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..656
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411942"
FT   TOPO_DOM        ?..559
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        560..580
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        581..656
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..641
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..656
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        228
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   ACT_SITE        423
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   ACT_SITE        481
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        458
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        470
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        478
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        531
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        559
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   656 AA;  72697 MW;  0FD95B1854B5F6CC CRC64;
     MSSFQSATTR QGLHRRNMNS ETPQSEFIQR LRRSPPSESS SSTPSSSTTT SSTTTTSNTS
     GKKKKTAPSA SDFYVPSLPG QPKDSQLILY AGHLSFSPPD TTIEPEKDSY GFFFLNKARH
     IANRPVLLVW LNGGPGCSSF DGSLMEVGPL RMVLKGDGTL KEVDAAWNEY ANMLFIDQPT
     GTGYSYGPKP NYVHELDVSS ANLVNLLARF FKIFPEYQQM DLYICGESFA GQYIPYLAQA
     ILDTNIISAP LKGIMIGNGW IDPINQYLAY PEFAFKVGLV NPSSKAADLV NEELKKCTEW
     IDSNSTTPIH IEACEGILSA ITDSTVQTVN SQKMCLNMYD VRLVDSYPAC GLTWPPDLAD
     ITPYLSRTDV KQALHAQDHA ADWVECEAKV GNNFWAKTSQ PSVTLFPKLL DKIKILLFSG
     DQDLICCHTG TERMIDHLTW AGHQGWTSQA INQPWKVNGS YAGLWKEERN LTYVLVANAS
     HMAPYDVPYV TQDMLVRFLG IDVMTAAGPA AQITSRIGEE TATKVNRVVM NETKLGQEGS
     GTTGLAMTSG PVHDENYYNA SSAMLFLTLV GLVVGLIFFV RRRLRRDGHG DFAHHPSDET
     EIILKNHHHH HLSPDSSLPR SARDRQFQPV PTDDLDDHHL HPNLPSNNTS YQDLPR
//