ID A0A0G2ERP4_9PEZI Unreviewed; 475 AA.
AC A0A0G2ERP4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 28-JUN-2023, entry version 33.
DE SubName: Full=Putative candidapepsin-4 {ECO:0000313|EMBL:KKY25437.1};
GN ORFNames=UCDDS831_g02112 {ECO:0000313|EMBL:KKY25437.1};
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:KKY25437.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY25437.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY25437.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY25437.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY25437.1};
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:KKY25437.1}.
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DR EMBL; LAQI01000038; KKY25437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2ERP4; -.
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; 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}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..475
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002543726"
FT DOMAIN 71..398
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 89
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 289
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 475 AA; 50068 MW; 31C13CB6F8B2C190 CRC64;
MRCTAALTLA TGLISLTDGL QLAKRTNSAP RVIGAEIQRR HVSNPVERDQ QRRRRKRDTL
QATLDNLETL YFANASLGTP AQSLRLHLDT GSSDLWVNTD DSDLCSSAKS GCSTAGTYSA
NDSSTYEYVN SLFNISYVDG SGASGDYVKD TFNFGGTNLT DMQFGVGYTS TSPEGVLGIG
YTRNEVAVNR AGLDAYPNLP QLLVNKGMIQ SNAYSLWLND LDASRGNILF GGVDTEKYHG
ALSTLPILKE NGQYRELVIA MTGVGSNGNI GTYLNSNTSS ADITPVLLDT GSSLTYLPDT
VVDSIYTDFD AVYDENEGAA FIDCNKADST DTLEFTFSSP TITVPMNELV LLAGYSKGQA
VCILGIAPAG DSTSVLGDTF LRSAYVVYDL ANNEISLAQT NYNATDSSIE EITTGTDSVP
DATGVANAVS AVNVATGAAR NGGLDISDNA ALPMKTAMPM APIAAAAAAG LLFAL
//