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Database: UniProt
Entry: A0A0C9TVJ5_PAXIN
LinkDB: A0A0C9TVJ5_PAXIN
Original site: A0A0C9TVJ5_PAXIN 
ID   A0A0C9TVJ5_PAXIN        Unreviewed;       553 AA.
AC   A0A0C9TVJ5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=PAXINDRAFT_169909 {ECO:0000313|EMBL:KIJ14308.1};
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:KIJ14308.1, ECO:0000313|Proteomes:UP000053647};
RN   [1] {ECO:0000313|EMBL:KIJ14308.1, ECO:0000313|Proteomes:UP000053647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200175 {ECO:0000313|EMBL:KIJ14308.1,
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; KN819344; KIJ14308.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9TVJ5; -.
DR   HOGENOM; CLU_037038_0_0_1; -.
DR   OrthoDB; 1696312at2759; -.
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:SF89; 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   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053647};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..553
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002203902"
FT   DOMAIN          62..405
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        78
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        91..96
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        325..360
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   553 AA;  58481 MW;  83E6296FC245C883 CRC64;
     MSRWSWVFLF HFALCLGTTL ARVSSPSPFK FPSLQPGQLA SNNTGPNSYG ISPVSLADDG
     TYYVVLQAGE ISFRAAIDTG SSDFWLVSTA CDTQTCSAVP RYPLTYASPT FVSINNNATT
     FALSYADGSS ASGFVAREAL EVSNVTAPNQ AFGVVTNSNV TLNDEVSGVL GLGFPRLSEI
     YAATANATPF LASLSEQGIL DYPILGLSLT RNSTGTLALG AIDVSVVQNV SEIVWNDVVP
     FSPIGTQTNT SGYMYWAIHM TNFAVNGSEL TPIPTYPGPT DNSSIALLDV GTPGLYGPYQ
     DVTRLYALFP DSRLVDDSGQ WAIPCDSSAT LSFSFGPGNT FVLQPTDYLI GPTEGNPDLC
     LSWPKASPPS ADGIDWQLGT PFLRTVYSVW SYGIDYNQPP MIGLYPLLNS SAPVESPAFV
     SSFFSAASAT VAAMLPNYIL PTPTFTTPPY AFNTSVPATL GEIVLSELAT STYEPILVTP
     AVGVNELPKV SDAYTLIVTD AQGDVLTSTY HITQPSVVLG LPPGWSGART LHAPYVGLGI
     PILAAVCAGA WIL
//
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