ID KEX1_ASPFC Reviewed; 632 AA.
AC B0XQ16;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-MAY-2023, 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=AFUB_008360;
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 144.89 / FGSC A1163 / CEA10;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499594; EDP56130.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XQ16; -.
DR SMR; B0XQ16; -.
DR ESTHER; aspfu-kex1; Carboxypeptidase_S10.
DR GlyCosmos; B0XQ16; 5 sites, No reported glycans.
DR EnsemblFungi; EDP56130; EDP56130; AFUB_008360.
DR VEuPathDB; FungiDB:AFUB_008360; -.
DR HOGENOM; CLU_008523_11_0_1; -.
DR PhylomeDB; B0XQ16; -.
DR Proteomes; UP000001699; 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; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..632
FT /note="Pheromone-processing carboxypeptidase kex1"
FT /id="PRO_0000411903"
FT TOPO_DOM 39..523
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..632
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 480..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 632 AA; 70499 MW; AFF7584F825F78C1 CRC64;
MLLTTPSSRG SRAQSGIANV SWLALSLLLL FSPTLGSAKS AADYYVRSLP GAPEGPLLKM
HAGHIEVDAQ NNGNLFFWHY QNRHIANRQR TVIWLNGGPG CSSMDGALME IGPYRLKDNH
TLEYNNGSWD EFANLLFVDQ PVGTGFSYVN TNSYIHELDE MSAQFITFLE KWFQLFPEYE
GDDIYIAGES YAGQHIPYIA KAIQERNNKI QNDQSIRWNL RGIVIGNGWI SPAQQYPSYL
TFAYEEGLVT KGSSLAKDLE VYQSVCESKI SASPNAINIR DCEEILQQIL ARTKDTNKQC
YNMYDVRLRD TYPSCGMNWP TDLVDVKPYL QRPDVVQALN INPEKKSGWE ECSGAVSSTF
NAANSLPSVQ LLPELLESGI PILLFSGDKD LICNHVGTEQ LINNMKWNGG TGFETSPGVW
APRHDWTFEG EPAGIYQYAR NLTYVLFYNA SHMVPYDLPR QSRDMLDRFM KVDIANIGGK
PADSRIDGEK LPQTSVGGHP NSTAAEQQAK EKIKETEWKA YAKSGEAALI VVIIGVTVWG
FFIWRSRRRN RGYQGVYQRD IGSGSILERF HNKRSGPADV EAGDFDESEL DNLHSPGLEQ
EHYAVGDDSD EESPNHQPAA PPSSTKPGGA QP
//
