ID A0A0G2HC86_9PEZI Unreviewed; 434 AA.
AC A0A0G2HC86;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 30.
DE SubName: Full=Putative secreted aspartic proteinase {ECO:0000313|EMBL:KKY32813.1};
GN ORFNames=UCDDA912_g07208 {ECO:0000313|EMBL:KKY32813.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY32813.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY32813.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY32813.1};
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.
RN [2] {ECO:0000313|EMBL:KKY32813.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY32813.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
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:KKY32813.1}.
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DR EMBL; LCUC01000278; KKY32813.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2HC86; -.
DR STRING; 1214573.A0A0G2HC86; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000034680; 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:SF2; ASPERGILLOPEPSIN-1-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; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..434
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002545131"
FT DOMAIN 120..430
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 138
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 322
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 434 AA; 46208 MW; 091ACCF9F1705374 CRC64;
MQPTTSFAAF LAATMAVVDV ASAFPTIPPR VPVPVSGTSS LKQVRNVKYS GRSTTGPIQR
QKAYLKYGAA IPDDLSTAVS RIRNKIMSEL QGVRLPNLPI KDRRTTGSAP ATPEEYDVEY
LTPVQIGTPP QTLNLDFDTG SSDLWVYSSA TPASDVNGQE VYNPGASNTS SKLQGSTWDI
SYGDGSSSSG EVYYDNVTVG GLSVYPMAVE AATDVSAEFT ADTDIDGLLG LAFGKLNTVS
PKKQKTFFES ARATLDKYVF TADLKAGEPG TYNFGFIDET AYTGDIEYIP VDSSDGFWTF
NTTGYQVGSN DYTTDPITGI ADTGTTLMLL PTDVVNAYYS AVEASSYDRI NGGYVFPCNT
DLPDFSFGVG KATVTVPGSY INYAPVDSAN SSCYGGIQDD SGIGFAIFGD VALKASFVVF
DGENEQLGWA SKKL
//