KEX1_ASPCL
ID KEX1_ASPCL Reviewed; 613 AA.
AC A1CQL5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=ACLA_026530;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027059; EAW07936.1; -; Genomic_DNA.
DR RefSeq; XP_001269362.1; XM_001269361.1.
DR AlphaFoldDB; A1CQL5; -.
DR SMR; A1CQL5; -.
DR STRING; 5057.CADACLAP00001892; -.
DR MEROPS; S10.007; -.
DR EnsemblFungi; EAW07936; EAW07936; ACLA_026530.
DR GeneID; 4700961; -.
DR KEGG; act:ACLA_026530; -.
DR VEuPathDB; FungiDB:ACLA_026530; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_0_1; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000006701; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..613
FT /note="Pheromone-processing carboxypeptidase kex1"
FT /id="PRO_0000411902"
FT TOPO_DOM 20..506
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 528..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 463..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 435
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 613 AA; 68819 MW; 88C8D6FD7AB273B9 CRC64;
MTMSFCALLF FLIISPTLAA TKSAADYYVR SLPGAPEGPL LKMHAGHIEV DAPNNGNLFF
WHYQNRHIAN RQRTVIWLNG GPGCSSMDGA LMEIGPYRLK DNHTLEYNNG SWDEFANLLF
VDQPVGTGFS YVNTNSYLHE LDEMAAQFII FLEKWFQLFP EYERDDIYIA GESYAGQHIP
YIAKAIQERN KKVDDKNSAR WNLRGLVIGN GWISPAQQYP SYLNFAYTEG LVKEGSSLAK
DLDVYQSVCE SKISAAPNAV NIKDCESVLQ QILSRTMDSE RKCYNMYDVR LRDVYPSCGM
NWPSDLVSVK PYLQSRDVVR ALNINPDKKS GWEECSGAVG STFTAANSVP SVQLLPELLE
SGVRILLFSG DKDLICNHIG TEQLINNMKW NGGIGFETSP GVWAPRRHWT FEGEPAGIYQ
YARNLTYVLF YNASHMVPYD LPRQSRDMLD RFMRVDIANI GGQPADSRID GEKLPQTSVG
GHPNSTAAEQ QAKEKIKETE WKAYAKSGEA ALIVVIIGVT VWGFFIWRSR RRNRGYEGVY
QKELGSGSIL ERFQNKRSGA GDVEAGDFDE SELDTLHSPG LERENYAVGD DSDEDDPNHP
RPTASSREDG THP
