ID   SUB1_PSED2              Reviewed;         400 AA.
AC   L8G6I7;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Subtilisin-like protease 1 {ECO:0000305};
DE            EC=3.4.21.- {ECO:0000250|UniProtKB:L8FSM5};
DE   AltName: Full=Destructin-2 {ECO:0000303|PubMed:25944934};
DE   AltName: Full=Serine protease 1 {ECO:0000303|PubMed:25785714};
DE            Short=PdSP1 {ECO:0000303|PubMed:25785714};
DE   Flags: Precursor;
GN   Name=SP1 {ECO:0000303|PubMed:25785714}; ORFNames=GMDG_08491;
OS   Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS   white-nose syndrome fungus) (Geomyces destructans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=658429;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4855 / 20631-21;
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA   Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Geomyces destructans 20631-21.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 120-128, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=25785714; DOI=10.1371/journal.pone.0120508;
RA   Pannkuk E.L., Risch T.S., Savary B.J.;
RT   "Isolation and identification of an extracellular subtilisin-like serine
RT   protease secreted by the bat pathogen Pseudogymnoascus destructans.";
RL   PLoS ONE 10:E0120508-E0120508(2015).
RN   [3]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=25944934; DOI=10.1073/pnas.1507082112;
RA   O'Donoghue A.J., Knudsen G.M., Beekman C., Perry J.A., Johnson A.D.,
RA   DeRisi J.L., Craik C.S., Bennett R.J.;
RT   "Destructin-1 is a collagen-degrading endopeptidase secreted by
RT   Pseudogymnoascus destructans, the causative agent of white-nose syndrome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:7478-7483(2015).
RN   [4]
RP   ERRATUM OF PUBMED:25944934.
RX   PubMed=26015578; DOI=10.1073/pnas.1509071112;
RA   O'Donoghue A.J., Knudsen G.M., Beekman C., Perry J.A., Johnson A.D.,
RA   DeRisi J.L., Craik C.S., Bennett R.J.;
RL   Proc. Natl. Acad. Sci. U.S.A. 112:E3152-E3152(2015).
CC   -!- FUNCTION: Major secreted subtilisin-like serine endopeptidase
CC       (PubMed:25785714). Mediates the degradation of collagen, the major
CC       structural protein in the mammalian host. Degrades the nonhelical
CC       regions of collagen that function in the cross-linking of the helical
CC       components (By similarity). May function as virulence factor involved
CC       in epidermal wing necrosis observed in white nose syndrome (WNS) in
CC       bats (Probable). {ECO:0000250|UniProtKB:L8FSM5,
CC       ECO:0000269|PubMed:25785714, ECO:0000305|PubMed:25785714}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6 to 8. {ECO:0000269|PubMed:25785714};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius.
CC         {ECO:0000269|PubMed:25785714};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25785714,
CC       ECO:0000269|PubMed:25944934}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; GL573547; ELR07576.1; -; Genomic_DNA.
DR   RefSeq; XP_012746953.1; XM_012891499.1.
DR   AlphaFoldDB; L8G6I7; -.
DR   SMR; L8G6I7; -.
DR   STRING; 658429.L8G6I7; -.
DR   EnsemblFungi; ELR07576; ELR07576; GMDG_08491.
DR   VEuPathDB; FungiDB:GMDG_08491; -.
DR   HOGENOM; CLU_011263_1_4_1; -.
DR   InParanoid; L8G6I7; -.
DR   OrthoDB; 308083at2759; -.
DR   Proteomes; UP000011064; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 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   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..119
FT                   /evidence="ECO:0000305|PubMed:25785714"
FT                   /id="PRO_0000434136"
FT   CHAIN           120..400
FT                   /note="Subtilisin-like protease 1"
FT                   /id="PRO_0000434137"
FT   DOMAIN          42..117
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          128..400
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        160
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        192
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        345
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   SITE            119..120
FT                   /note="Cleavage; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:L8FSM5"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   400 AA;  40739 MW;  0834A581465E7D79 CRC64;
     MKFSQSLIAL AACFLPLIAA APVEAQHAKI RSPRAQDIIP DSYIVVFNKG VNDADIESEF
     SSVSRILSKR RSAHKGVGHK YNITGFKGYQ IETDTGSIGE IAASPLVAWI EMDGKVQANA
     LETRSGATWG LGRISHKATG SNSYIYDGSA GSGSTVYVLD TGIYIEHSEF EGRAKWGANY
     ISGSPDTDEN GHGTHCAGTI AGATYGVASK ANLVAVKVLD RDGFGATSAT IAGINFVGQN
     GKDGKSVISM SLRGHYSAAV NSAVESTVSN GVTIVVAAGN DGDDASNYSP ASAKNAITVG
     SVDSTDTRAS SSNYGSVVDI FAPGVNVKSA SIGGKSAFSI KSGTSMATPH VAGLAAYLIG
     LGGLSSPAAI ASKIASIGTK GSVKDPKGSV NLIAYNGNGA