ID D8Q0I6_SCHCM Unreviewed; 405 AA.
AC D8Q0I6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
DE Flags: Fragment;
GN ORFNames=SCHCODRAFT_107928 {ECO:0000313|EMBL:EFI97747.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFI97747.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; GL377305; EFI97747.1; -; Genomic_DNA.
DR RefSeq; XP_003032650.1; XM_003032604.1.
DR AlphaFoldDB; D8Q0I6; -.
DR MEROPS; A01.019; -.
DR GeneID; 9595370; -.
DR KEGG; scm:SCHCO_02495563; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02495563; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_038846_0_0_1; -.
DR InParanoid; D8Q0I6; -.
DR OMA; ASHYWGV; -.
DR OrthoDB; 656651at2759; -.
DR Proteomes; UP000007431; 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:SF74; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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:UP000007431};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..405
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003120437"
FT DOMAIN 80..391
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT NON_TER 405
FT /evidence="ECO:0000313|EMBL:EFI97747.1"
SQ SEQUENCE 405 AA; 43475 MW; 1400CA53C1BABFF7 CRC64;
MFSSRLYCLL LLAVTVVASP VVEPRADATV NLPLTLQRNV TGGQEMVSAG RQRAQALRAY
GNGQRHHPAD EPVFNQNVVY TAPVGVGSAG ETCKYNNLIV DTGSSNTWVG AAKSYEPSDT
SQDTDEPVEV TYGSGFFLGT EWIDRVSLSR ELVVHRQSIG VARYSRGIGP KFDGILGLGP
TDLTAGSLVF SPGEEIPTVT DNLYTQGNIQ QPALGVYFAP AASQSPGGVL TFGSADDTFP
KTTTSPASAY WGYDQSITYN GTTILSQASG IADTGTTLIY LPTDAYNMYV AQTGAVPDRN
TGLLSVTEKQ FKQMKSLVFN VNGVDYELVP DAQLWPRSRN ADIGGTPKGY YLVVASMGSP
EGQGLDFING YAFLERFYSY YDTANAEMGF ATTKYTNATV NSQTQ
//