ID S3C0L3_OPHP1 Unreviewed; 507 AA.
AC S3C0L3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 28-JUN-2023, entry version 45.
DE SubName: Full=Aspartic-type endopeptidase {ECO:0000313|EMBL:EPE07084.1};
GN ORFNames=F503_03511 {ECO:0000313|EMBL:EPE07084.1};
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:EPE07084.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE07084.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE07084.1,
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; KE148152; EPE07084.1; -; Genomic_DNA.
DR AlphaFoldDB; S3C0L3; -.
DR STRING; 1262450.S3C0L3; -.
DR MEROPS; A01.015; -.
DR VEuPathDB; FungiDB:F503_03511; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_3_1; -.
DR OMA; LDGHYYH; -.
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 CDD; cd05474; SAP_like; 1.
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 InterPro; IPR033876; SAP-like.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000016923};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..507
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004506690"
FT DOMAIN 60..405
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 454..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 78
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 282
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 317..369
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 507 AA; 51850 MW; EB9509925A9737B8 CRC64;
MKSTLATGAL LAAAVKSASA DIPDGVVQFD VARRQPHPRL LRRASTTQTD ITNDLTQGGY
FIKCEIGTPA QSLTLQLDTG SSDIWVPASD ASVCETSKSN GGCTLGSFAS DSSSTFEVVG
KDEFSISYVD GSHSDGDYFT DVFSIGGSSV TNMTMGLGSD TDIPYGLVGV GYKTDEAIVS
DKQSLSAAYD NLPIVMLNEG LIKTNAYSLW LNDLDASTGS LLFGGIDTDK YHGDLTRISI
YKDSSTGVFT SFIVALTSVQ AVSSSGADTL TSTGFPVAAV LDSGTTLSYL PQDLAQEIWT
EVGAVYNSEA GAALIPCSRA SSGGYLSFGF GGPGGALINV TMDELVLDLT STGNAPTFTS
GRYAGQDACE FGIQNATTDP YLLGDTFLRS AYVVYDLVNN QIALAPTDFN ATSSNIVAFA
SSGAAIPSAT VAPSQAAVTA TSAFTTPAYA AATGFSSSSS TSSSSGSSSG SSSGSKSAAG
MVSVPMDMIH VGLVSMAMFA AGGMLVL
//