ID A1YN96_9PEZI Unreviewed; 373 AA.
AC A1YN96;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Cuticle-degrading serine protease {ECO:0000313|EMBL:ABL74284.1};
DE Flags: Fragment;
OS Arthrobotrys psychrophilus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Arthrobotrys.
OX NCBI_TaxID=47273 {ECO:0000313|EMBL:ABL74284.1};
RN [1] {ECO:0000313|EMBL:ABL74284.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YMF1.01412 {ECO:0000313|EMBL:ABL74284.1};
RX PubMed=20211028; DOI=10.1186/1471-2148-10-68;
RA Li J., Yu L., Yang J., Dong L., Tian B., Yu Z., Liang L., Zhang Y.,
RA Wang X., Zhang K.;
RT "New insights into the evolution of subtilisin-like serine protease genes
RT in Pezizomycotina.";
RL BMC Evol. Biol. 10:68-68(2010).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; EF113090; ABL74284.1; -; Genomic_DNA.
DR AlphaFoldDB; A1YN96; -.
DR MEROPS; S08.120; -.
DR BRENDA; 3.4.21.62; 12127.
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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..84
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 117..334
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 126
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 315
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABL74284.1"
SQ SEQUENCE 373 AA; 38379 MW; 8506DD3EA3A901BB CRC64;
KYIVVFKQGM SESAITKHTN RISSFHSKVA RDLTGARGHG VGKKFRFTAT GFNGYAGGFD
KATLQEILNS PEVDYVEQDA VVKINAEQLD STWGLDRVSH EEYAEPYSYE YDEAAAGAGT
TVYVIDTGIR ITHDEFKTPN GTSRAAWGFN SVDKTDSDGN GHGTHCAGTV AGKTYGVSKK
ANVVAVKVLS AGGSGSTSGV VAGMNWVAEH AIANFSVASM SLGGPKSAAL NTAVDAVFNA
GVTIVVAAGN ENQDAKNVSP ASAPNAITVG AIDSGNKIAS FSNWGTLIDV FAPGVGVLSS
WGTSDTETKT ISGTSMACPH VAGLAAYYIS VTAADGASDP ASISEKLSGS AVIDQVKGNI
RGSPNKIAHN GNA
//
