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Database: UniProt
Entry: A0A165F0Y7_EXIGL
LinkDB: A0A165F0Y7_EXIGL
Original site: A0A165F0Y7_EXIGL 
ID   A0A165F0Y7_EXIGL        Unreviewed;       385 AA.
AC   A0A165F0Y7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   08-NOV-2023, entry version 28.
DE   SubName: Full=Family A1 protease {ECO:0000313|EMBL:KZV88127.1};
GN   ORFNames=EXIGLDRAFT_619812 {ECO:0000313|EMBL:KZV88127.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV88127.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV88127.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV88127.1,
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; KV426107; KZV88127.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165F0Y7; -.
DR   InParanoid; A0A165F0Y7; -.
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; 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, ECO:0000313|EMBL:KZV88127.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT   DOMAIN          56..378
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        74
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        255
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   385 AA;  39863 MW;  ABF1BC856B32FED4 CRC64;
     MKTPAQTISA RAPFKKLVNH DKLGDIPAAD KARAQSLLSR AFISTKNAAV NTVVSYVAEI
     SVGTPATPRL LIVDTGSSNT WVGASTPFSS TGTTKQLNVS MGVNYGSGFV RGTQVVDAVS
     FGSPLIIANQ SIGVAQQFSG FSGVDGIVGI GPARLTSGTV HGPSQGLVPT VTDNLFSSGV
     IPAPIVGISF QATNDTFDVN GELVFGGVDS SKFTGELSVF SMSDVPAPAN QFFGINAQFT
     PQGGDPLLNS VGIIDTGTTL IMLSKEAFAS YAAQTGAKLD NATGLLSVTE AQFTQMKTLN
     LVVNGQVTLP ITRDAQRWPQ ALTTAIGGDP KAVYLIIGNL GTSRGSGIDF ILGQFFLERF
     YSVFDSSGFV GLAQTAFTNA VVNGV
//
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