KEX1_NEOFI
ID KEX1_NEOFI Reviewed; 632 AA.
AC A1D3I1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=NFIA_016700;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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; DS027688; EAW22974.1; -; Genomic_DNA.
DR RefSeq; XP_001264871.1; XM_001264870.1.
DR AlphaFoldDB; A1D3I1; -.
DR SMR; A1D3I1; -.
DR STRING; 36630.CADNFIAP00001374; -.
DR ESTHER; aspfu-kex1; Carboxypeptidase_S10.
DR MEROPS; S10.007; -.
DR EnsemblFungi; EAW22974; EAW22974; NFIA_016700.
DR GeneID; 4591422; -.
DR KEGG; nfi:NFIA_016700; -.
DR VEuPathDB; FungiDB:NFIA_016700; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_0_1; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of 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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 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..38
FT /evidence="ECO:0000255"
FT CHAIN 39..632
FT /note="Pheromone-processing carboxypeptidase kex1"
FT /id="PRO_0000411929"
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..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..615
FT /note="Basic and acidic 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; 70581 MW; B2816F2B33C3E0C3 CRC64;
MLLTAPSSRG SRTQSGIANV SWWALSLLLL FSPTLVSAKS AADYYVRSLP GAPEGPLLKM
HAGHIEVDAQ NNGNLFFWHY QNRHIANRQR TVIWLNGGPG CSSMDGALME IGPYRLKDNH
TLEYNNGSWD EFANLLFVDQ PVGTGFSYVS TNSYIHELDE MSAQFITFLE KWFQLFPEYE
GDDIYIAGES YAGQHIPYIA KAIQERNNKI QNDQSVRWNL RGIVIGNGWI SPAQQYPSYL
TFAYEEGLVT EGSSLAKDLE VYQSVCESKI SASPNAINIR DCEEILQQIL ARTKDTNRQC
YNMYDVRLRD TYPSCGMNWP TDLVDVKPYL QRPDVVQALN INPEKKSGWE ECSGAVSSTF
NAANSLPSVQ LLPELLESGI PILLFSGDKD LICNHVGTEQ LINNMKWNGG TGFETSPGVW
APRHDWTFEG EPTGIYQYAR NLTYVLFYNA SHMVPYDLPR QSRDMLDRFM KVDIANIGGK
PADSRIDGEK LPQTSVGGHP NSTAAEQQAK EKIKETEWKA YAKSGEAALI VVIIGVTVWG
FFIWRSRRRN RGYQGVYQRD VGSGSILERF HNKRSGPADV EAGDFDESEL DNLHSPGPEQ
EHYAVGDDSD EEGPNHHPAA PPSSTKPGGA QP
