ID A0A0C9TX61_PAXIN Unreviewed; 412 AA.
AC A0A0C9TX61;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 08-NOV-2023, entry version 33.
DE SubName: Full=Unplaced genomic scaffold PAXINscaffold_18, whole genome shotgun sequence {ECO:0000313|EMBL:KIJ14858.1};
GN ORFNames=PAXINDRAFT_180872 {ECO:0000313|EMBL:KIJ14858.1};
OS Paxillus involutus ATCC 200175.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX NCBI_TaxID=664439 {ECO:0000313|EMBL:KIJ14858.1, ECO:0000313|Proteomes:UP000053647};
RN [1] {ECO:0000313|EMBL:KIJ14858.1, ECO:0000313|Proteomes:UP000053647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200175 {ECO:0000313|EMBL:KIJ14858.1,
RC ECO:0000313|Proteomes:UP000053647};
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 (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200175 {ECO:0000313|Proteomes:UP000053647};
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}.
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DR EMBL; KN819340; KIJ14858.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9TX61; -.
DR HOGENOM; CLU_013253_1_4_1; -.
DR OrthoDB; 4946at2759; -.
DR Proteomes; UP000053647; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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:SF57; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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 Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000053647};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..412
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002203918"
FT DOMAIN 102..409
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 69..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 120
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 299
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 133..137
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 412 AA; 42859 MW; 9D5A4348EF12D1EC CRC64;
MRFTLATAIV GLPFFVAAAP QSVKQRIGTA IPISKRSGLT NPDNSVNLDA LKSHVASTKA
KITRGFDNFE KNTGSSHPSV VNGARKRGSG GDALTDASNE LWYGTISVGT PAHRYTVDFD
TGSSDLFLPG PDCGSNCSGH AVYNPWSSST SQDLGKTFSL RYGDGGTVIG EQYSDTVSIV
GLVAPDQTLG AASQYSSGFG SSEFPADGLM GMAFQSISVY KASPVFQTLV SEGQVDESVF
AFKLAAFGSE LFIGGTNTAL YTGEFSYADV TQEGYWEVNM DSLESNGKTV LSNVDSVIDT
GTTLIVGLPS DVSTLYQAIG GIDASSTVAA GFYTLPCDSF PSISLTFGGT SFPISADTLN
IGQVSPNSSD CVGGIVSQDI GASFWIVGDV FLANVYTAFD VGNSRVGFAT LA
//