KEX1_PUCGT
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 03-AUG-2022, entry version 53.
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).
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; 5297.GMQ_23199T0; -.
DR MEROPS; S10.007; -.
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; 607679at2759; -.
DR Proteomes; UP000008783; 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; 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..?
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
