ID B5WY73_COLGR Unreviewed; 342 AA.
AC B5WY73;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Subtilase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
OS Colletotrichum graminicola (Maize anthracnose fungus) (Glomerella
OS graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=31870 {ECO:0000313|EMBL:CAQ16213.1};
RN [1] {ECO:0000313|EMBL:CAQ16213.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M2 {ECO:0000313|EMBL:CAQ16213.1};
RA Krijger J.J., Horbach R., Behr M., Schweizer P., Deising H.B.,
RA Wirsel S.G.R.;
RT "The Yeast Signal Sequence Trap Identifies Secreted Proteins of the
RT Hemibiotrophic Corn Pathogen Colletotrichum graminicola.";
RL Mol. Plant Microbe Interact. 21:1325-1336(2008).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; AM944417; CAQ16213.1; -; mRNA.
DR AlphaFoldDB; B5WY73; -.
DR VEuPathDB; FungiDB:GLRG_07891; -.
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; 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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 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; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..342
FT /note="Subtilase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002840062"
FT DOMAIN 45..139
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 196..333
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT NON_TER 342
FT /evidence="ECO:0000313|EMBL:CAQ16213.1"
SQ SEQUENCE 342 AA; 36417 MW; 54F679C78A220FD0 CRC64;
MRGFIGAVAG LAAVASATPS LSIETIHDGA APVISSTNAE AVPNSYIIKF KKHVSDTDAE
DHHNWVQQIH SSSQDERLEL RKRGQEPLVD NVFHGLKHTY KIGNDFLGYA GHFDEATIEK
IRRHSDVEFI EVDSVVHTQV PVKSQGAEAE DTCDGELEKL APWGLARVSH RKSLGFGTYD
KYLYAEDAGE GVDAYVIDTG TNVDHVDFEG RAKWGKTIPS GDQDVDGNGH GTHCSGTIAG
KKYGVAKKAN VYAVKVLRSN GSGTMSDVVK GVEWAATSHI EQVKAAKDGK RKGFKGSVAN
MSLGGGKTQA LDAVVNAAVD AGIHFAVAAG NDNADACNYS PT
//
