ID D8Q9C2_SCHCM Unreviewed; 408 AA.
AC D8Q9C2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=SCHCODRAFT_235968 {ECO:0000313|EMBL:EFI95626.1};
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:EFI95626.1, 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; GL377308; EFI95626.1; -; Genomic_DNA.
DR RefSeq; XP_003030529.1; XM_003030483.1.
DR AlphaFoldDB; D8Q9C2; -.
DR MEROPS; A01.019; -.
DR GeneID; 9588095; -.
DR KEGG; scm:SCHCO_02703034; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02703034; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_038846_0_0_1; -.
DR InParanoid; D8Q9C2; -.
DR OMA; WDVANAQ; -.
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:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
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:UP000007431};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..408
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003120668"
FT DOMAIN 83..398
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 101
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 280
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 408 AA; 43514 MW; E3357C7FBF1844D5 CRC64;
MRLSPAFGPL LLAVVVATKP ILVDRSPISF ELTRKLNVTS GHNLVQAGKQ RVQKLKALAL
KKEGQAVDEG LIDEPVTNEA VIYSADVGVG ADATKYSLIV DTGSSNTWVG ADKKYSKSST
SKDTGSGVSV SYGSGYFSGE EYTDKVTITS DLVIDSQSIG VADTSSGFTG YDGILGIGPT
SLTQGTLENS NDEIPTVVDS AFKQGLIDDQ VISVYFQPTT KEEDQNGELI WGGVDDSKHT
GDIKYTPVTK TSPASNYWGI DQSIKYGDTV ILKKNAGITD TGTTLLYLAS DAYKAYAKAT
GAKVDNSVGL LSITKDQFSK LKSLFFNIGD DTYEFTANAQ IWPRALNSVI GGSDDAIYLV
VADIGTPSGQ GLDFINGYAF LERFYTVYDS GKGQIGFATT EYTDAETN
//