ID F8PHL3_SERL3 Unreviewed; 412 AA.
AC F8PHL3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=SERLA73DRAFT_82569 {ECO:0000313|EMBL:EGO05010.1};
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; GL945474; EGO05010.1; -; Genomic_DNA.
DR AlphaFoldDB; F8PHL3; -.
DR STRING; 936435.F8PHL3; -.
DR MEROPS; A01.019; -.
DR HOGENOM; CLU_038846_0_0_1; -.
DR InParanoid; F8PHL3; -.
DR OMA; YPASEYW; -.
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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, 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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..412
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003376693"
FT DOMAIN 87..402
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 105
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 284
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 412 AA; 43189 MW; C143E95B4FC165B2 CRC64;
MFPTASLLST IFLALTVAAK PVAVPDSPIS LPIARRLNTS GGAINLLQHD QARAAALRDR
AEAISSGKMS RRAAAASIPV INEATSYIAQ VGVGNPATTY DLIVDTGSSN TWVGAGTAYK
ETSTSVDTDE PVSVTYGSGS FSGTEYTDTV TLGSLTITTQ SIGVAQTSTG FSGVDGILGI
GPLDLTEGTL TDEQDATIPT VTDNLYSQGT IPEAVVGVSF EPTTSEEVTN GELTFGGTDS
TKYTGAITYT PLTTTYPASY YWGINESITY GSTTILSETA GIVDTGTTLI LIATNAYSKY
QSATGATEDN TTGLLRITTS QYDALEDLNF NVDGTTYALT PNGQVWPRSL NTYIGGTSNY
VYLIVNSIGT PSGEGLDFIN GYTFLERFYS VFDTTNSRVG FATTSYTDAT TN
//
