KEX1_CHAGB
ID KEX1_CHAGB Reviewed; 643 AA.
AC Q2GYB7;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=CHGG_07037;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408033; EAQ85784.1; -; Genomic_DNA.
DR RefSeq; XP_001224693.1; XM_001224692.1.
DR AlphaFoldDB; Q2GYB7; -.
DR SMR; Q2GYB7; -.
DR STRING; 38033.XP_001224693.1; -.
DR ESTHER; chagb-q2gyb7; Carboxypeptidase_S10.
DR MEROPS; S10.007; -.
DR EnsemblFungi; EAQ85784; EAQ85784; CHGG_07037.
DR GeneID; 4393231; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_0_1; -.
DR InParanoid; Q2GYB7; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000001056; 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 PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 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..643
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411912"
FT TOPO_DOM 31..519
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 541..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 471..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 185
FT /evidence="ECO:0000250"
FT ACT_SITE 385
FT /evidence="ECO:0000250"
FT ACT_SITE 447
FT /evidence="ECO:0000250"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 643 AA; 71275 MW; 0BFAD91EF80932D3 CRC64;
MVPSWPSTGC WRHLPVVLAA LTLPWTATLA AAEKSAGDYF VHSLPGAPEG PLVKMHAGHI
EVTPETNGNL FFWHFQNKHI ANKQRTVIWL NGGPGCSSED GALMEIGPYR LKDDKTLMYN
DGAWNEFANV LFVDNPVGTG FSYVDTNAYV RELDEMAEQF VIFMEKWYKL FPEYEHDDLY
FAGESYAGQY IPYIAKHVLA RNKEAGTKQW NLKGLLIGNG WISPPEQYEA YLQFAFEKGL
VKKGSDIASK LEVQLRICQK DLAVGESAVD HPECEKILQE ILKLTATRGK DNKLECYNMY
DVRLKDVYPS CGMNWPSDLA NVQPYLRRKD VVQALHVNPN KVTGWVECDG RVGQNFNPVK
SKPSIDLLPD ILSEVPVMLF SGAEDLICNH LGTEALISRM AWNGGRGFEL SPGTWAPRRD
WTFEGEDAGF WQEARNLTYV VFYNASHMVP YDHPRRTRDM LDRFMGVDIS SIGGDPTDSR
LDGEKGPETT VGGTAGNGNA DQEAEKAKLS AAKWEAYRRS GEIVLVIVAV AAAAWGYFVW
RERRKRRGYQ GLASAENGAA GGVMGGNSGF RNTHGGRPRS DVEAGDFDET QLDSLHVRSP
VEGQEDARYS LGAVSDDDDE EEEGSAAGAK GKEKETGKAA ESS
