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
//