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Database: UniProt
Entry: A0A165FJM7_EXIGL
LinkDB: A0A165FJM7_EXIGL
Original site: A0A165FJM7_EXIGL 
ID   A0A165FJM7_EXIGL        Unreviewed;       426 AA.
AC   A0A165FJM7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Acid protease {ECO:0000313|EMBL:KZV89103.1};
GN   ORFNames=EXIGLDRAFT_838727 {ECO:0000313|EMBL:KZV89103.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV89103.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV89103.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV89103.1,
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; KV426081; KZV89103.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165FJM7; -.
DR   STRING; 1314781.A0A165FJM7; -.
DR   InParanoid; A0A165FJM7; -.
DR   OrthoDB; 4946at2759; -.
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};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KZV89103.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..426
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007857821"
FT   DOMAIN          106..423
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        124
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        314
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        137..141
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   426 AA;  45344 MW;  6E42FF63C0268708 CRC64;
     MQSLLTLLFL APVLAIAASI QPPIELQTGH AIELDQRAAV AHNGVANTRG FSVHLARVHA
     KMQRGFAAYA KNTGSVHPNF HFVGKFGRRA LATVGVPLTD DDELLWHGTV SVGNPPVKYK
     VDFDTGSSDF FLPSGDCKTN CAGHVRYNGS KSKSARATTK GFTLNYLDGS QVKGKVYNDT
     VSFSSSAMNG TQLVTTKLTA NGAAVGAASV YSDGFALDQF PPDGLLGLGF PQISHFGRNP
     VVHNLIQQKQ IKPVFGVKLA SSKSELMLGG VNPGKYKGAF TWAAVNPVGF WQIKVGSVQY
     KGKTFKKNFS AVVDTGTTVI MGDEASVRAL YKAIPGSKDV SERVSPGAFS VPCKSIPTVN
     IQIGNMTVPI SPASFNLGQL YAGSKECLGG IVIGDSDFWI LGDVFLRNTY TQFDIGNKRV
     GFAALK
//
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