KEX1_TALMQ
ID KEX1_TALMQ Reviewed; 626 AA.
AC B6QQZ9;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
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=PMAA_045500;
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(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; DS995904; EEA20727.1; -; Genomic_DNA.
DR RefSeq; XP_002151727.1; XM_002151691.1.
DR AlphaFoldDB; B6QQZ9; -.
DR SMR; B6QQZ9; -.
DR STRING; 441960.B6QQZ9; -.
DR MEROPS; S10.007; -.
DR EnsemblFungi; EEA20727; EEA20727; PMAA_045500.
DR GeneID; 7029168; -.
DR KEGG; tmf:PMAA_045500; -.
DR VEuPathDB; FungiDB:PMAA_045500; -.
DR HOGENOM; CLU_008523_11_0_1; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; B6QQZ9; -.
DR Proteomes; UP000001294; 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..626
FT /note="Pheromone-processing carboxypeptidase kex1"
FT /id="PRO_0000411934"
FT TOPO_DOM 19..504
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 505..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 526..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 460..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 626 AA; 69623 MW; C2B374719456DD9E CRC64;
MLGKALLLLL SSPICAWAQS AADYYVKSIP GQPDGPLLKM HAGHVEVDAE TNGHLFFWHF
QNRHIANRQR TILWLNGGPG CSSMDGALME IGPYRVKDDH TLIYNNGSWD EFANLLFVDQ
PVGTGFSYVN TNSYLHDLDH VAAHMITFLE KWFAMFPEYE SDDLYIAGES YAGQYIPHIA
RAIVERNKNI QRNQQHWPIK GLLIGNGWIS PRDQYPANLQ YAYAEGIVKE GTAIANELDG
IEKSCDEQLN APGAGDLVDI RQCESILNKL LDLTRTSDDQ CINVYDIRLK DATCGNAWPP
DLDQMTDYLR RADVGAALNL DNGKANGWTE CNNQVTANFR MGHNGVPSIQ LLPGLIESGV
KVLLFSGDRD LICNHLGTES LIHNMKWSGG TGFETKPGVW APRRGWTFEG EAAGYYQQAR
NLTYVLFYNA SHMVPYDFPR RTRDMVDRFI NVDIANIGGP PADSRLDGEK LPQTSVGNTT
SSTSGTDQVD EAKLKDAEWK AYTKSGEAAL IVVIIGVSVW GFFIWRARQR AARDGTSPTK
KGYRAVYQDG VDNNSSTDGA GLLSRFRNQS NSNSSRDLEA RDFDEAELDS LTPNLQNGHE
RDHYVIGEED EDEDNDIGNG AKSSLH
