ID J4HZW6_9APHY Unreviewed; 415 AA.
AC J4HZW6;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FIBRA_06947 {ECO:0000313|EMBL:CCM04757.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM04757.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM04757.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM04757.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; HE797167; CCM04757.1; -; Genomic_DNA.
DR RefSeq; XP_012184040.1; XM_012328650.1.
DR AlphaFoldDB; J4HZW6; -.
DR STRING; 599839.J4HZW6; -.
DR MEROPS; A01.019; -.
DR GeneID; 24099668; -.
DR HOGENOM; CLU_038846_0_0_1; -.
DR InParanoid; J4HZW6; -.
DR OrthoDB; 656651at2759; -.
DR Proteomes; UP000006352; 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; IPR018222; Nuclear_transport_factor_2_euk.
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; PS50177; NTF2_DOMAIN; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000006352};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..415
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003779380"
FT DOMAIN 70..409
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 387..415
FT /note="NTF2"
FT /evidence="ECO:0000259|PROSITE:PS50177"
FT ACT_SITE 88
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 288
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 415 AA; 43862 MW; 886C54A736D016EA CRC64;
MLRTFASSII LGIISASLSS ATITTLSLDP IQGRTGAYMH GAPGAGRLRA MLMKGHTTTI
PATNLAYVQY TASIGVGSPP TYYSLVIDTG SSNTFVGSGK QYVRTSTSIP TGQEVAVSYG
SGSFSGNEYL DQVTISPGLV ISNQSIGDAL ENSGFKGVDG IIGFGPTNLT LGTLYLDTNA
TIPTVMDNSY SQALIATEVL GVRFAPASTD SDKNGAITLG GVDTNYYIGE ITYTSVTTTA
PSNSYWGVDV TGATYGNTTI IPGSYAGIVD TGTTRKCFLI QVTDIYADIG RLTVIYIAND
WYSTYENSIP GAYYDLNNTG LIVIPESSAE NLQPFNLEIG NATFTLSPKA QLLPKSQNEA
WGGDSGLQYG YIGPIGTPSG SGLDFILGQK FMEQFYAVFD TTNNRVGFAY TDHTY
//
