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Database: UniProt
Entry: A0A0A1TE34_9HYPO
LinkDB: A0A0A1TE34_9HYPO
Original site: A0A0A1TE34_9HYPO 
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
//
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