ID KEX1_PYRTR Reviewed; 639 AA.
AC B2W340;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=PTRG_03838;
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP;
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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; DS231617; EDU46676.1; -; Genomic_DNA.
DR RefSeq; XP_001934171.1; XM_001934136.1.
DR AlphaFoldDB; B2W340; -.
DR SMR; B2W340; -.
DR STRING; 426418.B2W340; -.
DR ESTHER; pyrtr-kex1; Carboxypeptidase_S10.
DR MEROPS; S10.007; -.
DR GlyCosmos; B2W340; 4 sites, No reported glycans.
DR EnsemblFungi; EDU46676; EDU46676; PTRG_03838.
DR GeneID; 6342074; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_0_1; -.
DR InParanoid; B2W340; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
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; IPR018202; Ser_caboxypep_ser_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; PS00131; CARBOXYPEPT_SER_SER; 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..30
FT /evidence="ECO:0000255"
FT CHAIN 31..639
FT /note="Pheromone-processing carboxypeptidase kex1"
FT /id="PRO_0000411943"
FT TOPO_DOM 31..517
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 539..639
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 477..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 639 AA; 71619 MW; 7F261923AB81FA5A CRC64;
MAFSHAPSGW RTALLAGLIA TVAWLPAIVA QEKTQADYFI HDLPGAPKPL LKMHAGHIEV
DAEHNGNLFF WHYQNRHIAD RQRTVLWLNG GPGCSSMDGA MMEIGPYRVR EGGKLEYNNG
SWDEFANLLF VDQPVGTGFS YVNTDSYLTE LDQMAAHMVI FLEKWFALFP EYENDDLYIA
GESYAGQHIP YIARAILDRN KKNQAKSPWP LKGLLIGNGW MSPVDQYLSY IPFAYQNGLM
RSGTDMAKRV EEQQRICVQK LEAGGMDAVD TRDCEQIMVR ILQETKNENA DPMNQCLNMY
DIRLRDDSSC GMNWPPDLAQ VTPYLRRADV VQALHINTDK KTGWQECNGA VSSHFRAKNS
KPSVKFLPEV IEQVPVLLFS GDKDFICNHV GTEAMIQNLQ WNGGKGFEAS PGVQNAKQDW
MFEGEAAGTW QEARNLTYVV FYNSSHMVPF DYPRRTRDML DRFMGVNIEA IGGAPADSLI
DGEKGPLTSV GDHPNSTKAE EDKSKELKAA EWKAYTRSGE VALVIAVIVA CICGFLLCRS
RRAKSAYKGD DSDEGRESLL TGMGLDNFRR KERRQDVEAA DFDERELDEV PKKSGKGYGQ
ISSEKGRVPH NDSSFSLGVD SDDDEAGSSD RGRRKEESR
//
