ID F8QB65_SERL3 Unreviewed; 593 AA.
AC F8QB65;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=SERLA73DRAFT_188362 {ECO:0000313|EMBL:EGN94451.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; GL945488; EGN94451.1; -; Genomic_DNA.
DR AlphaFoldDB; F8QB65; -.
DR STRING; 936435.F8QB65; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_021426_0_0_1; -.
DR InParanoid; F8QB65; -.
DR OMA; WVPVRGY; -.
DR OrthoDB; 1507272at2759; -.
DR Proteomes; UP000008063; 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:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 2.
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:UP000008063};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..593
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003377209"
FT DOMAIN 75..492
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 593 AA; 62538 MW; 06649FBBEE5B00C1 CRC64;
MVGIYLLSSI ITLSTLPAVV SSISIEHGPS SPSLSTGKHT QGVHLPIYRR ERTSPRKRSG
QTGIAGLGDY LDVSYNVLMQ VGDTQTPVVL DTGSSDLWIL SSASGANGSS SVPLYDPSTF
QPSDLEARLE YGDSLTGTHA FGPIGFDSVS LAGITLSDQY FSAINDTNTT VLQTGSAGIF
GLGFPINSVI WGEVFISQQN SSFTSSKRDN LHDTIPTKSH DFEIRFFPKN DLSHFVGSSS
SVPQISSRQS STSPSGTSAI FASYSSIGPF ISRLVVQGLL ALPMFTVTLQ RDAIQIGGNQ
GMLSLGELPE SVNNDSLTWV PVRGYTPEEG GLNPPADAPN EVYPIAWEIP VDDVYFDGER
LARSQLSSPN ISLSALLDTG NSLIRGPPDV ISYILNTALG GSPFPCSEQH TLAFQIGGQM
FPVDPRDFVS QTQSESLEDC VANITPTDVP VIGSGYLYSW SLGDPFLKSV LAAFYYGNLG
MPSQDPARIG LLSTVPDNAA DELASAVSDV IPTTVIAGAT SVYNSLPVTS NVAPSRIISA
LSTGVGGVPL APTSISGSLS GGKKVNDVRE ALRVNAWTVG LGVSLWILCR LVG
//