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Database: UniProt
Entry: J4H5F3_9APHY
LinkDB: J4H5F3_9APHY
Original site: J4H5F3_9APHY 
ID   J4H5F3_9APHY            Unreviewed;       446 AA.
AC   J4H5F3;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=FIBRA_08920 {ECO:0000313|EMBL:CCM06639.1};
OS   Fibroporia radiculosa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Fibroporiaceae; Fibroporia.
OX   NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM06639.1, ECO:0000313|Proteomes:UP000006352};
RN   [1] {ECO:0000313|EMBL:CCM06639.1, ECO:0000313|Proteomes:UP000006352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM06639.1,
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; HE797427; CCM06639.1; -; Genomic_DNA.
DR   RefSeq; XP_012185922.1; XM_012330532.1.
DR   AlphaFoldDB; J4H5F3; -.
DR   STRING; 599839.J4H5F3; -.
DR   GeneID; 24101539; -.
DR   HOGENOM; CLU_013253_8_0_1; -.
DR   InParanoid; J4H5F3; -.
DR   OrthoDB; 1697158at2759; -.
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; 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:SF73; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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}; Hydrolase {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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..446
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003778376"
FT   DOMAIN          55..390
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   446 AA;  47912 MW;  034E197624599076 CRC64;
     MRHLLPLCLL CFLHSANALR FPIHARSAST SSSRLTRRAN NDTLLNVKNT QNSEYITNIT
     LGGREIPVLL DTGSSDLWVA GDVPDSTDLG VSESLSYAVG DAAGDINTAT LQFGNYTVEN
     QAFLLVKNTS SFSINIETEG FDGLIGLGPN TGSVIRDKLG DSKGDSVLDR IFQQNASSAN
     YMTILLNRLD DPTSPSTGQM SISEIVPGYE NITSMPKLSV EMVHKLTDLD QHWQTYTDVN
     GVIGPDGNPI EVESIVPSAP DGQLVVVFDS GYTLPQVPRA MSDAIYGRVQ GAEYNSEQGF
     WTIPCAQMLN ISFKFGGVDY PISPLDTSSS EFDVVNSAGD PVCVGAFQPI SSAFSLLGEY
     DIILGMSFMR NVYALFDYGD FVEDTSTDLG SPFIQLLSTT NVAAAHAAFV SVRLNGVDTT
     GAASQALLPV SEEQHSPETE AEKKAQ
//
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