ID A0A060SN45_PYCCI Unreviewed; 617 AA.
AC A0A060SN45;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Pheromone-processing carboxypeptidase KEX1 {ECO:0000256|ARBA:ARBA00040628};
DE EC=3.1.1.117 {ECO:0000256|ARBA:ARBA00026105};
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=BN946_scf185015.g152 {ECO:0000313|EMBL:CDO73823.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO73823.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO73823.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO73823.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-O-methyl-alpha-D-glucuronosyl ester derivative + H2O = 4-
CC O-methyl-alpha-D-glucuronate derivative + an alcohol + H(+);
CC Xref=Rhea:RHEA:67452, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:171667, ChEBI:CHEBI:171668;
CC EC=3.1.1.117; Evidence={ECO:0000256|ARBA:ARBA00024511};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453;
CC Evidence={ECO:0000256|ARBA:ARBA00024511};
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 carbohydrate esterase 15 (CE15) family.
CC {ECO:0000256|ARBA:ARBA00010092}.
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:CDO73823.1}.
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DR EMBL; CCBP010000123; CDO73823.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060SN45; -.
DR STRING; 5643.A0A060SN45; -.
DR MEROPS; S10.007; -.
DR HOGENOM; CLU_008523_11_1_1; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000029665; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
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 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.
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:UP000029665};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..617
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001587580"
FT TRANSMEM 515..539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 561..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 617 AA; 68638 MW; 6865A32496161B28 CRC64;
MRAFFPVQLL SCLAPLALLY SHSSTAAPTD IPSAASFYVS RLPDLHQDEE RPLRMYAGHL
PSDPDARTAE PADVTAHLYF FMVKARRTAD KERLIFWLNG GPGCSSFDGL MMEIGPWRVD
GKGGLKTVPG GWEEYATVVF IDQPAGTGFS YAPSNKYDHE LPEASAHFVE FLRNFYKVFP
EYQDVDAYIT GESFAGQYIP YFADAILSSN LKIRLKGAAI GNGWTDARRQ YPSYLDYAVK
HGIVEIGTEA YKNGKEITDK CTEELSKYTD IEPVHVNVCE EVMMTVVSAK SHLTNNTATC
INMYDVRLED TAPECGMNWP PDLTDVYTYL ARRDVVNAIH ANAVPGNWVE CKPRVHTEFS
TRRSNSSITL LPRVLERIPV MLFVGDQDLI CNYVGIESMI QAMQWNGETG LGKVQTQPWT
VDGKPAGTWV ASRNLTYVKI FNASHMVGYD VPHVTHDMIL RFMGVNFTAI TDGSARIPSA
VGDDAKPIPA ILDDLPTSTP APSKSPEQDK AMWEAYYNAG SAALVLILIA IGVGVFLWWR
SRRRKLFLRD IPLSTREENI PLNSSMREDQ DGDDNGSFRS RKGKERASGT LAEQEAIFDV
GSDEEDERGA VSGRTSR
//
