ID A0A165GM95_9BASI Unreviewed; 383 AA.
AC A0A165GM95;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:KZT58243.1};
GN ORFNames=CALCODRAFT_432909 {ECO:0000313|EMBL:KZT58243.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT58243.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT58243.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT58243.1,
RC ECO:0000313|Proteomes:UP000076842};
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}.
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DR EMBL; KV423953; KZT58243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165GM95; -.
DR STRING; 1353952.A0A165GM95; -.
DR InParanoid; A0A165GM95; -.
DR OrthoDB; 4946at2759; -.
DR Proteomes; UP000076842; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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; 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:SF87; SACCHAROPEPSIN; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KZT58243.1};
KW Protease {ECO:0000313|EMBL:KZT58243.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT DOMAIN 77..380
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 95
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 271
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 383 AA; 40815 MW; ABAACFD42CBF3F0D CRC64;
MSIQLHKRSA LHVKEGVVNV DALRDQLAKV QNKYARTLKQ YEQNTGEPHK LAATFFRNIE
KRATASDGLT DDEDDDWYGN VEVGTPLKTY TVDFDTGSSD FFLPASSCRR CGSHSTYNPS
SSSTSHSLGR SFTLNYGDGS TTSGTQYTDT VAIGGLTVSG QTLGSATSYS TEFQEGVYDG
LMGLGWPSIS SYPATPFVFN LFDQGSLSSG SFSFKLAESG SSLYIGGADS SLYTGSFSYT
PVTEEGYWEV TTQSLKLGST TIASNQDSIV DSGTTLLYVD ASTARSFYSH IAGAKEDDSL
GSGLYTLPCN SIPTNTAIVF AGKTVTIPSS VFNFGQVSEG SSTCVGGIAS GDFGFWILGN
VFMRNVYTQF DMANARVGVA TLA
//
