ID A0A1B8B9X7_FUSPO Unreviewed; 405 AA.
AC A0A1B8B9X7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FPOA_03474 {ECO:0000313|EMBL:OBS29537.1};
OS Fusarium poae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS29537.1, ECO:0000313|Proteomes:UP000091967};
RN [1] {ECO:0000313|EMBL:OBS29537.1, ECO:0000313|Proteomes:UP000091967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2516 {ECO:0000313|EMBL:OBS29537.1,
RC ECO:0000313|Proteomes:UP000091967};
RA Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT "Living apart together: crosstalk between the core and supernumerary
RT genomes in a fungal plant pathogen.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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:OBS29537.1}.
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DR EMBL; LYXU01000001; OBS29537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8B9X7; -.
DR STRING; 36050.A0A1B8B9X7; -.
DR OMA; HADLEGH; -.
DR OrthoDB; 380531at2759; -.
DR Proteomes; UP000091967; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR43806:SF68; ALKALINE PROTEASE 1; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000091967};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..405
FT /note="Peptidase S8/S53 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008603705"
FT DOMAIN 27..104
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 142..369
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 144
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 176
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 333
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 405 AA; 43488 MW; 30A89A4CF8A29EEE CRC64;
MLSFKILLAL LPSALAQFTI DEVVEDNYII TLKPKVNETE IEQHIEWVDD IHTASLFRRG
EDGVDKVWNS TFKGYCGEFD RNTIRKINQS EDVLAVEPVK KVTLTTVQRN AEWGLASISH
RTTGSTEYLY DASAGNGMYA YLVDTGINTG HQDFQGRASN GYNAYPGVPF VDVNGHGTHC
AGTIAGKVYG VAKRANLIAV KVFHTGSSTT AIVLDGYNWA VNNITNTPGR NQQSVISMSL
GGGKSDAFNL AVEMAYRQNI HTVVAAGNDN VNANNTSPAS AQNATTVGAI DRNNNRASFS
NFGPLVDIFA PGVDIKSTWI GSDNATNTIS GTSMACPHVA GLSLYLRAKE GLRTVKSVQD
RIQQLATKNV IANAGTGSPN LLAYNGGIPS TATGGRRFRE PHGRD
//
