KEX1_METRA
ID KEX1_METRA Reviewed; 616 AA.
AC E9ESM3;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 38.
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=MAA_02969;
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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; ADNJ02000004; EFZ01740.1; -; Genomic_DNA.
DR RefSeq; XP_007819158.1; XM_007820967.1.
DR AlphaFoldDB; E9ESM3; -.
DR SMR; E9ESM3; -.
DR ESTHER; metaq-kex1; Carboxypeptidase_S10.
DR MEROPS; S10.007; -.
DR EnsemblFungi; EFZ01740; EFZ01740; MAA_02969.
DR GeneID; 19257255; -.
DR KEGG; maj:MAA_02969; -.
DR HOGENOM; CLU_008523_11_0_1; -.
DR Proteomes; UP000002498; 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; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..616
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411927"
FT TOPO_DOM 29..516
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..537
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 538..616
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 469..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 444
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
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 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 616 AA; 68961 MW; 7EC426936D200C65 CRC64;
MAPRFSWSLA TSWHALAILA LWPASTLAGD KSAADYYVRE LPGLPKNSPP IKMHAGHIEV
TPETNGNLFF WHFQNNHIAN RQRTVIWLNG GPGCSSEDGA LMEVGPYRVT KDNALTLNNG
TWNEFANLLF VDNPVGTGFS YVDTNSYIHG LNAMATQFIT FLEKFFALFP EYQSDDLYIA
GESYAGQHIP YIARAILDRN KSKSRAETWN LGGLLIGNGW ISPQDQSSAY LKFSLERGLI
EKGSDNAQQL QQMQRICDKE MSINPGHVDY PECESILNKI LELTRVGSGD QECINMYDVR
LRDSAPSCGM NWPPDLKYVG PYLRQPQVIS ALNLDKQRNT GWQECNSMVN ANFRNQNATA
SISLLPDILK EVPILLFSGA EDLICNHVGT EELISNLAWN EGKGFEVTPG NWAPRRQWTF
EGEVAGFWQE ARNLTYVLFH NASHMVPFDY PRRSRDMLDR FMKVDISSIG GEPSDSRIDG
EKGPDTSVGG AKNNTQQHEE ETKQKLKEAQ WLAYQRSGEV VLVIVIIAAS VWGYFVWRQR
RKGTAYSALQ SDEAAGQSRT GLAAFHNRQS DRDLEAAAFD ETTVDNIPLQ ESIGRGESKY
SIGDDSDEEE GETNKT
