ID   A0A0D0CIP2_9AGAR        Unreviewed;       536 AA.
AC   A0A0D0CIP2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=GYMLUDRAFT_198309 {ECO:0000313|EMBL:KIK62524.1};
OS   Collybiopsis luxurians FD-317 M1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC   Collybiopsis luxurians.
OX   NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK62524.1, ECO:0000313|Proteomes:UP000053593};
RN   [1] {ECO:0000313|EMBL:KIK62524.1, ECO:0000313|Proteomes:UP000053593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK62524.1,
RC   ECO:0000313|Proteomes:UP000053593};
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 (APR-2014) 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; KN834767; KIK62524.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0CIP2; -.
DR   HOGENOM; CLU_013253_1_1_1; -.
DR   OrthoDB; 4946at2759; -.
DR   Proteomes; UP000053593; 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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053593};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..536
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002220327"
FT   DOMAIN          215..533
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          127..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..186
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        233
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        423
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        246..254
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        458..494
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   536 AA;  54604 MW;  96FAA354DD44EE28 CRC64;
     MQLQLSFATL LAGVLFALTT VQDADARPTK RNAGMVTLPL KRVPKAEGIP PTVYLQQHMN
     RAHKRLARMT GREPTPDHQL RRRIERRMMD LEEAPLSKRY NRHGVPKSAR AVRIGLAGAG
     HVPRAELKKG KAQGQAGSKG SAGAVGAGAG AAGAAGAAGA AGAGSGSAAA SGDNGTAGTG
     SQVESGGVPS GVEAANAPTA SNSLGLNIEG QDVGYLATIQ MGTPPQNYFI LMDSGSADLW
     VGSENCQSTA GGGCGDHTFL GTASSSTFVD SGKQFQVTYG TGAVSGTIIN DNIAVAGLNL
     TGHTFGVADS ETDDFADNSV PFDGLMGLAQ STLSEQQTPT PPESLASAGL ISDAITSFKI
     SRAADNLNDG EITFGGLDPT KFQANTLTTF DNVNQQGFWE GAMDSVTVDG TDTGLQGRTA
     ILDTGTTLIV APPNDAAAVH QLIQGSASDG QGGFTVPCNT NASVALSFSG TSFAIDPRDI
     AFQPVNPNDP NGDCVSGISS GEVGAATEWL VGDVFLKNAY FSVDVGKNAI SLAKLA
//