ID S3CP58_OPHP1 Unreviewed; 399 AA.
AC S3CP58;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 03-MAY-2023, entry version 44.
DE SubName: Full=Vacuolar protease a {ECO:0000313|EMBL:EPE02375.1};
GN ORFNames=F503_03960 {ECO:0000313|EMBL:EPE02375.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE02375.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE02375.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE02375.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KE148180; EPE02375.1; -; Genomic_DNA.
DR AlphaFoldDB; S3CP58; -.
DR STRING; 1262450.S3CP58; -.
DR MEROPS; A01.018; -.
DR VEuPathDB; FungiDB:F503_03960; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_4_1; -.
DR OMA; KYDHDAS; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000016923; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EPE02375.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016923};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..399
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004507370"
FT DOMAIN 87..396
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 105
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 288
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 118..123
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 399 AA; 42930 MW; 772B13EDB86E5360 CRC64;
MKSALLLAAA GLLGTTQAGG VHSLKLKKVP LAKQLESVPI DAQIRGLSQK YMGGRPDTHV
DAMFKTDVAN VEANHPIPVS NFMNAQYFAE ISIGTPPQSF KVVLDTGSSN LWVPSRECGS
IACYLHSKYD SEASSSYKSN GTKFAIQYGS GSLSGFVSQD TVTIGNLKIA KQDFAEATEE
PGLAFAFGRF DGILGLGYNT ISVNKIVPPF YSMIDQKLID SGVFAFYLGY SEDGTDSEAV
FGGVNKDHYT GKITTIPLRR KAYWEVDLDS IALGEDVAEL ENTGVILDTG TSLIALPSQL
AEMLNAQIGA KKGYNGQYSV DCDKRSSLPD VTFTLSGHPF TLPATDYILE VSGSCISTFM
GMDFPEPTGP LAILGDAFLR RYYSIYDLDN NTVGLARAK
//