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Database: UniProt
Entry: A0A0C9XC51_9AGAR
LinkDB: A0A0C9XC51_9AGAR
Original site: A0A0C9XC51_9AGAR 
ID   A0A0C9XC51_9AGAR        Unreviewed;       550 AA.
AC   A0A0C9XC51;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=K443DRAFT_377715 {ECO:0000313|EMBL:KIJ93822.1};
OS   Laccaria amethystina LaAM-08-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX   NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIJ93822.1, ECO:0000313|Proteomes:UP000054477};
RN   [1] {ECO:0000313|EMBL:KIJ93822.1, ECO:0000313|Proteomes:UP000054477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIJ93822.1,
RC   ECO:0000313|Proteomes:UP000054477};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KN838822; KIJ93822.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9XC51; -.
DR   STRING; 1095629.A0A0C9XC51; -.
DR   HOGENOM; CLU_021426_0_0_1; -.
DR   OrthoDB; 1507272at2759; -.
DR   Proteomes; UP000054477; 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:SF89; SACCHAROPEPSIN; 1.
DR   Pfam; PF00026; Asp; 2.
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:UP000054477};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..550
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002216693"
FT   DOMAIN          77..494
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   550 AA;  58995 MW;  2BCBC25105658E11 CRC64;
     MWWLKYGVGL LTACHAAARP APTTETLSLE EIARRYTKRT AGGVHLPIVR QVTEASELRR
     RGLTSAIGLG DFVDIRYNVL ISIGGTTTPL LLDTGSSDLW VFSDKCTQGC LSSQSAYPQA
     SFQYSGVDAK LFYGDSNFIT AASGMIGKDT VNLAGLMLQD QYFVAVNLTN TSLGKTGSSG
     IFGLGFPVIS EVSFKLWNQS RSSISTKRQV TEDTPILPSN NKFGTRFFNF RRIKFPSLSD
     YFPSPGEQTQ QTSSKFSSPM TTILPSWSVF GPLLTRFVTA AQLTLPMFTV TLQRDSIQVG
     GNAGMLSIGE MPSGVSKDSL TWVPIRAYPY TQGGLPAPPD SPNEVYPLTW EVALDDVYLD
     GEKLPRSTLS SPSITLSALI DTGNPGLAGP ADVVRNIQSK LAPNGNFPCS EPHTIAFSIG
     GKLFPVDPRD FIEQSFEGNA AECTGLLQST DSPSFRGYQF SWSLGVPFLK SVLAAFYFGN
     ITYPSHDPPR MGFLSTVPQD AASRLVSAVA AVQTGDNFPY ISEAAPSGTF KPAGTASNGV
     PVATATGRAT
//
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