ID A0A0A1TE34_9HYPO Unreviewed; 380 AA.
AC A0A0A1TE34;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Putative Endothiapepsin-like protein {ECO:0000313|EMBL:CEJ87336.1};
GN ORFNames=VHEMI04383 {ECO:0000313|EMBL:CEJ87336.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ87336.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ87336.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(2015).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; CDHN01000002; CEJ87336.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1TE34; -.
DR STRING; 1531966.A0A0A1TE34; -.
DR HOGENOM; CLU_013253_0_3_1; -.
DR OrthoDB; 46443at2759; -.
DR Proteomes; UP000039046; 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 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 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:UP000039046};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..380
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001989927"
FT DOMAIN 76..377
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 94
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 281
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 380 AA; 40023 MW; 77BA2DA112BABE6F CRC64;
MVLLKTILAY GSLASAIAVP APLVNFAGEK GQFTVNLKYN EKFQRSNLPI GTVIPRDDGS
GSTTAHNSKS RPDGEYYAEI LVGTPAQKLN LLFDTGSSDL WLFGADTKGK IDAGQAKWNH
TASNTASLVK NGKWSIGYGD GSGGKGTIYK DTVSIAGASV SGQGVEYATQ VYQQGNGDNI
LGVPVSGIVG FGFDKINTAS PKQKTLFSNL KAHLNQPVFT VDIKHQADGT FGFGFIDESK
YTGNITYTDV DSSRGFWTIT STGYAIGDGE FVPLNYSGIV DTGGSGFSVP SDAFSAWKSQ
ISDSTITAET VLPDFIFGIG SSQIRVPGAN LKEKRADGTY RLTIGDGGDG AFFGSPSLTN
AFVVFEDGPN GPRTGWATSK
//