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Database: UniProt
Entry: S3CP58_OPHP1
LinkDB: S3CP58_OPHP1
Original site: S3CP58_OPHP1 
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}.
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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
//
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