ID A0A1V6Q7D3_9EURO Unreviewed; 293 AA.
AC A0A1V6Q7D3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN ORFNames=PENSOL_c108G07908 {ECO:0000313|EMBL:OQD85144.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD85144.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQD85144.1}.
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DR EMBL; MDYO01000108; OQD85144.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6Q7D3; -.
DR STRING; 60172.A0A1V6Q7D3; -.
DR OrthoDB; 5392320at2759; -.
DR Proteomes; UP000191612; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000191612};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..293
FT /note="Peptidase S1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012461077"
FT DOMAIN 22..286
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 293 AA; 32016 MW; D278586F85EEACF6 CRC64;
MPWFYYTIYI IALSYINGAC AIYQGTSSNC GEHPYTVHIE HHGAEGVYGA SYQCGGTIIT
PRHILTAAHC MKKHASSYPG IKADAQNMRV QLLKCSNGQL VKTGKLYEAA QLHITEEYLT
QPTPDFDIGV IELAEDIKYH PFLADTATVP AYAGPVQPNW EHDTRLTLVG AGTFGLSQTH
ISEYLRQVRA DVIPRPECEQ RRDSSSGFPG SFVGLDIARF FCAVDRVTLG AACGGDSGSG
SLEYVNGRKK LVGVVSAGDV ICSQPNHFNA YTSVSWYLDW IGAVVAPYQL KQI
//
