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Database: UniProt
Entry: A0A165IF76_EXIGL
LinkDB: A0A165IF76_EXIGL
Original site: A0A165IF76_EXIGL 
ID   A0A165IF76_EXIGL        Unreviewed;       353 AA.
AC   A0A165IF76;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   08-NOV-2023, entry version 25.
DE   SubName: Full=Aspartic proteinase from Irpex Lacteus {ECO:0000313|EMBL:KZV93318.1};
GN   ORFNames=EXIGLDRAFT_613164 {ECO:0000313|EMBL:KZV93318.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV93318.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV93318.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV93318.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KV425992; KZV93318.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165IF76; -.
DR   InParanoid; A0A165IF76; -.
DR   OrthoDB; 656651at2759; -.
DR   Proteomes; UP000077266; 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; cd05471; pepsin_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; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF51; NAPSIN-A; 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:UP000077266}.
FT   DOMAIN          27..343
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   353 AA;  36337 MW;  6E34388E8F7EB42F CRC64;
     MSSFKASSFA EAAAVGSAHA TNQAIYYLTS VSVGNPATNY QLIIDTGSAN TWVGSKTAYK
     TTNSSVSTGA RFAVNYQSSS VSGNLYMDKV ALSTTLTVAS QQIGIANKQT GFSGVDGVLG
     LGPVGLTKGT SSQGTTTTIP TITDNLYAKG VITSNVVSLS FAPTTVVGAV NGEITFGGVD
     TTQYTGALTY APITAKYPAS AYWGVDAAVS YGSTVFLYGH PTIVESGLTL IYLASDAFKK
     YQAATGGVLD SATGLLKVTA AQFNALQPLT LTIAGQKYSL NANAQIWPRT LNTAIGGQAN
     GVYLVVADLG TPSGSGLDVI AGQVFMERFY TSFDSTNKKV GLAQTKYTSA SVN
//
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