ID A0A0L6WHF2_9AGAR Unreviewed; 564 AA.
AC A0A0L6WHF2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Proteinase R {ECO:0000313|EMBL:KNZ74945.1};
GN ORFNames=J132_05846 {ECO:0000313|EMBL:KNZ74945.1};
OS Termitomyces sp. J132.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC Termitomyces.
OX NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ74945.1, ECO:0000313|Proteomes:UP000053712};
RN [1] {ECO:0000313|Proteomes:UP000053712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA Hu H., Poulsen M.;
RT "The genome of Termitomyces.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; KQ412630; KNZ74945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6WHF2; -.
DR STRING; 1306850.A0A0L6WHF2; -.
DR OrthoDB; 1406593at2759; -.
DR Proteomes; UP000053712; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR CDD; cd09274; RNase_HI_RT_Ty3; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR041373; RT_RNaseH.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF17917; RT_RNaseH; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053712};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..564
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005569163"
FT DOMAIN 53..95
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 163..352
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 352..453
FT /note="Reverse transcriptase RNase H-like"
FT /evidence="ECO:0000259|Pfam:PF17917"
SQ SEQUENCE 564 AA; 61766 MW; 21C305621F019CDE CRC64;
MHLYSILVVS AGFLAPVIAA PGYLVPIEKV DGETSGRHIV SLKANADKSS FIEATNIATT
HNWTVINGFA GQFTEDQINV LRAHGDVESI TEDGFAQVSM VTTQTNATWG LARLSSVKKL
ANQNSNALNF QYLRETTAGL GVDVYVIVMP FFGYQVEFGG RARWGATFGG YVSMDKNGHG
THCAGTVAGS SVGVARAASI IAVKVLGDNG ISNFEMKISI SGLDWVYNQA KTSGRPSIVS
MSLSSNSPST PLDSAVTSLT TIGVHAVSYV HVVLSKRKMV QVAAGNNNLD ATNMSPARAS
GAITVGATNI ADSRASFSNY GSVVALFAPG ENIISTWFTG PTALVSLSGT SMPIWLICNA
SKIGVGAMYG QGPSWQKCWP AGFMSKKFTN AQQNYAMHKL ETLAIVEALL RWEDKLLEYK
IHVITDHKAL EFLKTQQDLS PHQQWWMDYM LRFNFDITYI IRELNKVADC LSCYFESRLN
VPIRTLVRYC TLVHLYQKDW LSWIDLTEFA INASISETTC FALFELNGHY MPSMICKIRL
DIAIFREVQQ FMCQALSSST QCNN
//
