ID B8MCJ4_TALSN Unreviewed; 689 AA.
AC B8MCJ4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Protease S8 tripeptidyl peptidase I, putative {ECO:0000313|EMBL:EED18810.1};
GN ORFNames=TSTA_125260 {ECO:0000313|EMBL:EED18810.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED18810.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01032};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
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DR EMBL; EQ962655; EED18810.1; -; Genomic_DNA.
DR RefSeq; XP_002482802.1; XM_002482757.1.
DR AlphaFoldDB; B8MCJ4; -.
DR STRING; 441959.B8MCJ4; -.
DR MEROPS; S53.007; -.
DR GeneID; 8100305; -.
DR VEuPathDB; FungiDB:TSTA_125260; -.
DR eggNOG; ENOG502QTN1; Eukaryota.
DR HOGENOM; CLU_013783_4_0_1; -.
DR InParanoid; B8MCJ4; -.
DR OMA; RIGCEEY; -.
DR OrthoDB; 1405251at2759; -.
DR PhylomeDB; B8MCJ4; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR PANTHER; PTHR14218:SF19; SERINE PROTEASE AORO, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G10250)-RELATED; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU01032}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01032};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01032,
KW ECO:0000313|EMBL:EED18810.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..689
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002875024"
FT DOMAIN 233..688
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT REGION 184..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 310
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 314
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 606
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 647
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 666
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 668
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 689 AA; 74442 MW; 70112FB38B3670B4 CRC64;
MLWQYLLVHT SVFSGALAAS LSPVLHEKRD IPLPEIKQRI DGDAIIPVRI GLRQSNLHTG
YNRLMEVSHP SSENYGKHLT KEEVHALFAP AEETLDTVKN WLFGTGLVDH SEIIHYENKG
WLAIDMPAKH AETLLGTHFY EIESHNGDVR IGCEEYYLPA HVSSHVDYIK PGVKLSAPMK
KKQLPQKRSV AGADSFHPSH PRMPHTRPPH YPGWSLPPAA WGLPPELQNC GVNITPTCIK
ALYDIPNPIF SQPENAMGLF ETYDAFSQED ISLFFQHFAT NVPAGTKPNV ISVDGGTAPV
APNDTRNGGE SDIDLDLAIS LIYPQTVTVY QVDDLPNSSG ETGVNGFLNT FLDSVDGSYC
DYSAFGITGD SPGVDASYPD PATDGYKGQK QCGTYNLTRV VSISYGEAEV YLPKAYVERQ
CNEILKLGLQ GHTILVASGD YGVASFPGSN GDAEGCLSSG TMNGTIYNPD YPAGCPYITA
VGATRLYPND TVHDAESAMQ VNLTAFNIAT GAGPTSPPYD FFATGGGFSN YFKPAPFQAL
AIEEYLKKDL PYQSLPYYEI NADATNIGEK GGVYNRIGRG YPDVSANGAF LLTYVNQTAG
TFFGTSLASP IFGAVVTLLN EARSAVGKGP IGFINPALYA NPFVLNDITN GSNPNCGSQG
FQASQGWDPV TGLGTPNFPR MLAYFLSLP
//
