ID J4ICH6_9APHY Unreviewed; 540 AA.
AC J4ICH6;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=FIBRA_08687 {ECO:0000313|EMBL:CCM06426.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM06426.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM06426.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM06426.1,
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}.
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DR EMBL; HE797325; CCM06426.1; -; Genomic_DNA.
DR RefSeq; XP_012185709.1; XM_012330319.1.
DR AlphaFoldDB; J4ICH6; -.
DR STRING; 599839.J4ICH6; -.
DR GeneID; 24101326; -.
DR HOGENOM; CLU_013253_8_2_1; -.
DR InParanoid; J4ICH6; -.
DR OrthoDB; 1449676at2759; -.
DR Proteomes; UP000006352; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006352};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..540
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003778486"
FT TRANSMEM 473..494
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 50..377
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 517..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 66
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 266
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 540 AA; 57810 MW; 46C1D247566E8ABF CRC64;
MILPLSLLLL VSSAYSLHVP LQRRAQSTSV SINSSANGNF GFTDMEGFAY TGTIFVQGQP
FQVQIDTGSA DLWVASPESA FQGLQNTGLN STTVYGSGSV EASGPIVLGD VSFGEFTVHG
QALVIATNPN VPGQGQFTGL LGVAPFGASR IWQKSQMSNS TSFDGKPFMY NLFSSYDVDS
SYMTFYLSRS EVGVTQGGVM TIGEIVSNFS AITSSPQLPL LTDTFWATLM DGIYVDDHFY
TGHSTVIPDN STWHQSHPNA TAAVPDSGTT FAWAPQYYVD AIYKSLPGAV FSSDINGYII
PCDTAINVSM VFSGVKYPLD PLDMLNINNI YSNGTLVCQG TFTYAPDVGL DWVLGDSFMH
NVYTLYKYAD VNSTNPASVD QYYLQFLSVT NASEAWATFP KRNQKRLAQL SQQLESTATA
TVLVASASST YSLIASDITA TATSSNDDVA AAMNAASSSS PSTDYSTLKR NSYIIIGLVG
GVLALLIGVA VLLFKQLGAN SKYQRIGGAT VPPVPFKETY GSDAYEPPSE SFRTPYSDRG
//