ID A0A0G2ENP2_9PEZI Unreviewed; 410 AA.
AC A0A0G2ENP2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 31.
DE SubName: Full=Putative aspartyl protease {ECO:0000313|EMBL:KKY23736.1};
GN ORFNames=UCDDS831_g02767 {ECO:0000313|EMBL:KKY23736.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY23736.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY23736.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY23736.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY23736.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY23736.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKY23736.1}.
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DR EMBL; LAQI01000064; KKY23736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2ENP2; -.
DR Proteomes; UP000034182; 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; cd06097; Aspergillopepsin_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; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF23; ASPARTIC ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G15950)-RELATED; 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; 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:KKY23736.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..410
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002543675"
FT DOMAIN 98..407
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 114
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 299
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 335..370
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 410 AA; 43348 MW; 30B4119C63D96DB5 CRC64;
MHSFRVAILL VALLAAVVLA RPAPTKTTQT LAKRSFKVPR NLNPKIKRKD GAAAMRRAMR
KFGIKHQAAA AAAATPASNA TNENGEVAAN PEENEALFLS PVKIGGQTMN MDFDTGSSDL
WVFSTQLSKQ AIGGHAAFDS AKSKSFQAMD GASFLITYGD GSGAAGNVGL DTVDIGGATV
TKQAIEMATA VSQSFQQDTN TDGLVGLAFS KINTVKPQKQ KTFFDNIMKD LDQPVFTADL
TNDTSGTYEF GTIDKSKFKG ELTYTAVDNS QGFWQFPSKS FMVDGQKMTN TKGSDAIADT
GTSLLMVDDN VAKAYYAKVK GAVNDPQAGG FVYPCDAVMP DIAVAVGDYM ANIPGDQVTF
APVDEANTTC FGGVQGNQGS DLQIFGDTMF KAQFVAFNGG NQSLGMAPKN
//