ID Q96UV0_OPHUL Unreviewed; 251 AA.
AC Q96UV0;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Subtilase {ECO:0000313|EMBL:AAL08498.1};
DE Flags: Fragment;
OS Ophiostoma ulmi (Dutch elm disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=5174 {ECO:0000313|EMBL:AAL08498.1};
RN [1] {ECO:0000313|EMBL:AAL08498.1}
RP NUCLEOTIDE SEQUENCE.
RA Hoffman B.G., Breuil C.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAL08498.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12111098; DOI=10.1007/s00294-002-0298-7;
RA Hoffman B., Breuil C.;
RT "Cloning and genetic analysis of subtilases in sapstaining fungi.";
RL Curr. Genet. 41:168-175(2002).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; AF413094; AAL08498.1; -; Genomic_DNA.
DR AlphaFoldDB; Q96UV0; -.
DR MEROPS; S08.052; -.
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; 3.40.50.200; 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 PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 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 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}.
FT DOMAIN 42..247
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 44
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 76
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 242
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAL08498.1"
FT NON_TER 251
FT /evidence="ECO:0000313|EMBL:AAL08498.1"
SQ SEQUENCE 251 AA; 25984 MW; 64DD045240E64CA1 CRC64;
ALTQTGAPWG LARVSHRKQL NFGTFNKYLF ADEGGEGVDA YVIDTGTNVK HEDFEGRAHW
GKTIPQGDED LDGNGHGTHC SGTVAGKKYG VAKKANVYAV KVLKSNGSGT MSDVIAGVEF
AATRHLEQVA LAKKGKRSGF KGSVANMSLG GGKTTPLDAA VNAAVDAGLH FAVAAGNDNA
DACNYSPAAA KNALTVGASA IDDSRAYFSN WGKCTDIFAP GLNIQSTWIG STTAINTISG
TSMATPKGEF H
//
