ID A0A0L0W3Z5_9BASI Unreviewed; 651 AA.
AC A0A0L0W3Z5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Pheromone-processing carboxypeptidase KEX1 {ECO:0000256|ARBA:ARBA00040628};
DE EC=3.4.16.6 {ECO:0000256|ARBA:ARBA00038895};
DE AltName: Full=Carboxypeptidase D {ECO:0000256|ARBA:ARBA00042717};
DE AltName: Full=Pheromone-processing carboxypeptidase kex1 {ECO:0000256|ARBA:ARBA00040403};
GN ORFNames=PSTG_00963 {ECO:0000313|EMBL:KNF05970.1};
OS Puccinia striiformis f. sp. tritici PST-78.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=1165861 {ECO:0000313|EMBL:KNF05970.1, ECO:0000313|Proteomes:UP000054564};
RN [1] {ECO:0000313|Proteomes:UP000054564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race PST-78 {ECO:0000313|Proteomes:UP000054564};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Hulbert S., Chen X., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Puccinia striiformis f. sp. tritici PST-78.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential release of a C-terminal arginine or lysine
CC residue.; EC=3.4.16.6; Evidence={ECO:0000256|ARBA:ARBA00001003};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000256|ARBA:ARBA00004393}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004393}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNF05970.1}.
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DR EMBL; AJIL01000005; KNF05970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0W3Z5; -.
DR STRING; 1165861.A0A0L0W3Z5; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000054564; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
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 {ECO:0000256|ARBA:ARBA00022703};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054564};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 556..573
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 651 AA; 71603 MW; 49180860D4CA360B CRC64;
MGSFGSATTR EGLARRQIRG EDETQSEYIR RLSRSTPSDP SSSSSSTTDG KKTQPTASDF
YVPSLPGQPK DSQLILYAGH LSFSAPEKKI EPSQDSYGFF FLNKARHIAN RPILIVWLNG
GPGCSSFDGS LMEVGPLRMI SKGEGALKEV DGAWNEYANL LFIDQPTGTG YSYGPQPDYV
HELDVSSNNL VNLLARFFKI FPEYQHMDLY IGGESFAGQY IPYLAQAILD TNIISAPLKG
IIIGNGWIDP VNQYLAYPDF AFKVGLVNPN SKSGEKVKAE LNKCQEWIKS NNNNTSPIHI
EACEGILSAI TDSTVQTVNS QKMCLNMYDV RLVDTYPACG LTWPPDLADI TPYLSRSDVK
NALHAQDHST DWVECNPKVG NEFWAKTSKP AIYLFPKLLE KIKVLLFSGD QDLICCHVGT
ERMIDNLSWG GKKGWTGEGI NQPWKVNGSY AGLWKEERNL TYALVANASH MAPYDVPFVT
QDMLIRFLGI DVMTAAGPAA QITSRIGAEA ATTVNRVLLN ETRLVQDGGS VAGLAASTSG
GAGGIRDENY YNASSAMVFL GLVGLVVGLI FFVRRRLRIS GKGDFAHLHD GENEMILKNH
QASSPPSPSS NRIHHESQFE PVPTDDIDDL HHRLLPNRPN SHNSSYQDVP R
//
