ID F8PT56_SERL3 Unreviewed; 426 AA.
AC F8PT56;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=SERLA73DRAFT_159520 {ECO:0000313|EMBL:EGO00886.1};
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; GL945478; EGO00886.1; -; Genomic_DNA.
DR AlphaFoldDB; F8PT56; -.
DR STRING; 936435.F8PT56; -.
DR MEROPS; A01.019; -.
DR HOGENOM; CLU_038846_0_0_1; -.
DR InParanoid; F8PT56; -.
DR OMA; SEFWGIN; -.
DR OrthoDB; 656651at2759; -.
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; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
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}.
FT DOMAIN 103..416
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 121
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 298
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 426 AA; 43393 MW; 8CDBED6D6C283803 CRC64;
MAVTVSSLPP VCAVLSHPCQ FLVTMFPSSA LLSLLLVALS AVSATPVKRE AKAATLAFTA
KVNASGYANI AEADRARAQS LRQGATKGKR AASISAANTA VTYTASVGVG SPATQYTLLI
DTGSSNTWVG ASAKYTPTSS SKDTGNTVSV SYGSGSFSGE EYTDTVTLSS DLVIKGQSIG
VASTSTGFSG VDGILGVGPV DLTSGTVSNT NTVPTVTDNL FSAGTITDDV LGIFYVPAAA
SDSTGELTFG GTDSSKYTGS IGYVPLTSTS PASEYWGIDQ SITYGSTSIL SSTAGIVDTG
TTLILIASDA FSKYESATGG SMDQTTGLLK ISSAQYSALS PLNFKIGGTT YALSANAQIW
PRSLNTALGG DANSIYLVVS DIGTESGSGL DFINGYTFLE RFYSVFDTGN SQLGFATTSH
TDDTSN
//