ID F8PP45_SERL3 Unreviewed; 413 AA.
AC F8PP45;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=SERLA73DRAFT_177556 {ECO:0000313|EMBL:EGO01922.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL945477; EGO01922.1; -; Genomic_DNA.
DR AlphaFoldDB; F8PP45; -.
DR STRING; 936435.F8PP45; -.
DR MEROPS; A01.018; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_4_1; -.
DR InParanoid; F8PP45; -.
DR OMA; KYDHDAS; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000008063; Unassembled WGS sequence.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:InterPro.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05488; Proteinase_A_fungi; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033819; Saccharopepsin.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF87; SACCHAROPEPSIN; 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 Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW 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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..413
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003376807"
FT DOMAIN 102..410
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 120
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 302
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 133..138
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 336..369
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 413 AA; 44610 MW; 376D969647C6B295 CRC64;
MLLSAFAPLL LLPYAAAAGG VHKLKLHKLP KVSPNHGLES AYLAEKYGAE TTYQQLPLMG
AGGAGRHIRP DRPEDSDLFW TQEELVKGGH GVPLTNFMNA QYYTEITLGS PAQTFKVILD
TGSSNLWVPS SKCTSIACFL HTKYDSSSSS TYKANGTEFS IQYGSGSMEG FVSQESMKIG
DLSIQHQDFA EATKEPGLAF AFGKFDGILG LGYDTISVNH ITPPFYNMID QGLLDEPLFS
FRLGSSEDDG GEAVFGGIDS SAYTGSITYV PVRRKAYWEV ELEKVSFGGD ELDLENTGAA
IDTGTSLIAL PTDVAEMLNT QIGATRSWNG QYQVDCAKVP SLPELSFYFG GKPYPLKGTD
YILNVQGTCI SAFTGLDINL PGGALWIIGD VFLRRYFTVY DLGRDAVGFA TAA
//
