ID A0A0D2A5Q6_9PEZI Unreviewed; 407 AA.
AC A0A0D2A5Q6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 28-JUN-2023, entry version 39.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=PV09_06723 {ECO:0000313|EMBL:KIW01875.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW01875.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW01875.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW01875.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KN847552; KIW01875.1; -; Genomic_DNA.
DR RefSeq; XP_016211744.1; XM_016360405.1.
DR AlphaFoldDB; A0A0D2A5Q6; -.
DR STRING; 253628.A0A0D2A5Q6; -.
DR GeneID; 27314696; -.
DR VEuPathDB; FungiDB:PV09_06723; -.
DR HOGENOM; CLU_013253_0_0_1; -.
DR InParanoid; A0A0D2A5Q6; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000053259; 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}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000053259};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..407
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002238182"
FT DOMAIN 96..404
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 112
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 297
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 407 AA; 42557 MW; C20A5E0C3752CB6E CRC64;
MHSLRTVLFL VSLFAAVALS APAPARTLNK RSFTHYVKRS INRRDPTAGP RAMAAAYRKF
GFSMPARAAN TTASSNATGS GTGTVQAVPE ANAAEYLSPV NIGGQTVTLD FDTGSSDLWV
FSTALSQRTI GQHTAFDPNK SQTFKLLQGS TWQISYGDGS GAAGIVGTDT VNIGGATATS
QAVELATAVS QSFVQDTQND GLVGLAFSKL NTVKPTQQTT FFDTVMPQLA MPVFSVDLRN
DSTGSYTFGA IDQTKFQGQL TTVPVNSSSG FWQVTSPAVM IGNQKVTNPN ASPAIADTGT
SLLLVDDAVA NAYYSKVQGA TNDATVGGFT YPCNAALPDF GVNIGPNYMA VVPGSGITFA
QVDANTCFGG VQSNGGSNLQ IYGDVMFRSQ YVVFDGQNKA LMIAPKA
//
