ID D8PQE6_SCHCM Unreviewed; 614 AA.
AC D8PQE6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
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};
DE Flags: Fragment;
GN ORFNames=SCHCODRAFT_48283 {ECO:0000313|EMBL:EFJ03059.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFJ03059.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL377302; EFJ03059.1; -; Genomic_DNA.
DR RefSeq; XP_003037961.1; XM_003037915.1.
DR AlphaFoldDB; D8PQE6; -.
DR STRING; 578458.D8PQE6; -.
DR MEROPS; S10.007; -.
DR GeneID; 9587854; -.
DR KEGG; scm:SCHCO_02622192; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02622192; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_1_1; -.
DR InParanoid; D8PQE6; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000007431; 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:UP000007431};
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 485..509
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 519..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFJ03059.1"
SQ SEQUENCE 614 AA; 68282 MW; 9BAA6A4A741318B6 CRC64;
VPSAASFYVP SLPDLQPHPD RPLSIFAGHL SSDPDASKAA ATDVTAHLYF VMIKNRRVAD
KERIMFWFNG GPGCSSFDGL MMENGPWRVD GNGGLKVADG GWEEYTTMVY VDQPAGTGFS
YTATNHYVQT LEEASQQLLV FLHNFYDVFP EYKSMETYFG GESYAGQYLP YFADAVLNSD
LYIPLRGVAI GNGWIDSRRQ YPSYIDYLVR VGILSETSDE YKEAKEKTES CIKGFENYVN
EPINIQECEG LIMDVAKVRE KQDGDKQMCM NIYDVRLDDT APACGMNWPP DIKPITEYLD
RSDVVSALHA EAHSGSWVEC RGQVHVQFRE ERSNSSITVL PKVLERIPVL LFAGDQDYIC
NYVGLENMIQ AMSWNDGTGL GKVQTQSWTV DGAPAGTWVS SRNLTYAKIF NASHMAPFDL
PHVSHDMILR FMNVNFSAIL DGSARIPSSI GSEEKPTFTA IEEELPNTPI TPGKTPEQDK
AMWEAYYNAG SAALVLVVVF GIIGAVVWFR RRRGGSLRLP GTVDFSRRPG DFSSRADAEE
SIPLNASDSM GNLRNSSTPR LSEDGDGRTL RGDDDERKDK GKGRALLPPE PIFDVGSDDE
DGYRDEHEHG RKDA
//
