ID D8PTW4_SCHCM Unreviewed; 427 AA.
AC D8PTW4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=SCHCODRAFT_65201 {ECO:0000313|EMBL:EFI99848.1};
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:EFI99848.1, 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; GL377303; EFI99848.1; -; Genomic_DNA.
DR RefSeq; XP_003034751.1; XM_003034705.1.
DR AlphaFoldDB; D8PTW4; -.
DR GeneID; 9587058; -.
DR KEGG; scm:SCHCO_02483927; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02483927; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_1_4_1; -.
DR InParanoid; D8PTW4; -.
DR OMA; QNHHRFN; -.
DR OrthoDB; 4946at2759; -.
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:SF87; SACCHAROPEPSIN; 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};
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:UP000007431};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..427
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003120283"
FT DOMAIN 116..424
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 143..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 313
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 147..152
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 427 AA; 45632 MW; F864BC00656EB720 CRC64;
MFAYYSLIAT VSLALAAAAS PVVSVPKEGR AIPMRKRAGL TKDNGVFDFD RAVALTVAAQ
NKHRQNLLNL QNNGGTLRQG AVIKDLASIP DDIKAKLQLS KRQAESLEDE NQDTEWAGDI
TIGSDDQKFL IDFDTGSSDL WVPSKSCSSS VCSQKNSYDA SSSDSSKKAS GKFQIQYGDG
STVSGPVYQD TVTVAGVTAK NQYFSPVTTL SDSFSNDPID GILGLAYPAI SNLKQDPWFV
NANSQGAVDK NSFGFYLAKT GSELYLGGSN DKLYSGDVEY HDVDKSEGFW LITGASISVD
GKSAADNFDT IIDSGTTLAY GPPDTIDEIF SKIDGAKAYD QQQGLYSFPC DSAPDVSFSW
GGKDWKISAD NFNAGQAEEG SSDCIASLAG QDLGLGDNTW LLGDAFMKNV YTVFDFDQDA
VGFAELA
//
