ID A8N7D8_COPC7 Unreviewed; 452 AA.
AC A8N7D8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Aspartyl protease {ECO:0000313|EMBL:EAU91113.2};
GN ORFNames=CC1G_03281 {ECO:0000313|EMBL:EAU91113.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU91113.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU91113.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAU91113.2}.
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DR EMBL; AACS02000003; EAU91113.2; -; Genomic_DNA.
DR RefSeq; XP_001830744.2; XM_001830692.2.
DR AlphaFoldDB; A8N7D8; -.
DR MEROPS; A01.078; -.
DR GeneID; 6007189; -.
DR KEGG; cci:CC1G_03281; -.
DR VEuPathDB; FungiDB:CC1G_03281; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_1_2_1; -.
DR InParanoid; A8N7D8; -.
DR OMA; GFFAFPC; -.
DR OrthoDB; 1203010at2759; -.
DR Proteomes; UP000001861; 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:SF57; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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, ECO:0000313|EMBL:EAU91113.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001861};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..452
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002727096"
FT DOMAIN 74..401
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 92
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 284
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 452 AA; 48205 MW; 259B3B466FA19406 CRC64;
MKSLLLPFLW ISLALAVDPI TVPLARRSRT HYGIEHYASV AQSLRAKYNV GSSSGRRRAV
EDIPMINQHS DASYLGEVLI GTPPQAFEVV LDTGSADLWV ADIACATCTG IPLFDPARSS
TVQQSAAGTT IRYGSGAVAG SINRDTVRLG NFTVERQTFL AADQLSSTLL DGGVSGILGL
AFETIASTRA TPFWQNLLEN NQLSSPEMSF WLTRFLNVSI AREAEPGGIF TLGGRNTSLY
SGEIEFLDLP VSFPSFWLLP VRRITVQGRS VPISTGSASL AAIDTGTTLI GGPSGDVEAI
WAAVPGSRRS IGNEGFWYYP CRTEINITLN FGGKSWSISP DDMNLGQTSF GSSLCLGAIF
DLGLGSNIPE NSQNPGWVIG DTFLKNVYSV FRADPPSIGF AELSTLAGGS GTAPGIFNEN
TPSRDSGASH LVAQASRISL ISLYLLIILC YL
//