ID F7W9V7_SORMK Unreviewed; 583 AA.
AC F7W9V7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=WGS project CABT00000000 data, contig 2.55 {ECO:0000313|EMBL:CCC05224.1};
GN ORFNames=SMAC_08716 {ECO:0000313|EMBL:CCC05224.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC05224.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC05224.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC05224.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCC05224.1}.
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DR EMBL; CABT02000055; CCC05224.1; -; Genomic_DNA.
DR RefSeq; XP_003347279.1; XM_003347231.1.
DR AlphaFoldDB; F7W9V7; -.
DR MEROPS; A01.081; -.
DR GeneID; 10804703; -.
DR KEGG; smp:SMAC_08716; -.
DR VEuPathDB; FungiDB:SMAC_08716; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_035052_0_0_1; -.
DR InParanoid; F7W9V7; -.
DR OMA; GAAEMRF; -.
DR OrthoDB; 4940213at2759; -.
DR Proteomes; UP000001881; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
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:SF47; ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01220)-RELATED; 1.
DR Pfam; PF00026; Asp; 2.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001881}.
FT DOMAIN 163..578
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 81..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 583 AA; 61895 MW; E338D4AB77155D30 CRC64;
MLPFLGSLGT FAYGLLVFAL VIHAATINQL TPTERYLRDS APKLPGIKYS IPKPFLGGNT
NANTRQLTVS RNVQTLSGIS HSTSISSKHP ITRSGNRRSA VSVLGQHQRR LKQNAIRTNA
HSSSIRTHGS GSGSSDSGDD NGEEGSAYGY ENVTVTTAFG TQYAAEVHWN SVPLLLLLDT
GSSDTWAITH NFSCLDYLGN DVPQETCGFG PAYTLPPPHT SPVPGGVGIN GTNGTNSSST
SHPAPKPPKE EDLWKPYGPT DPQTHMFIQY GDGEIVTGPM GFADISVGNI TVKKQQVALA
EKTFWFGNNL TSGLMGLAFP SLTNAYLGDV PGGSGSGSGS GSGSGSGEGG DGEGEDDGSG
GGLGNGEGHE SYNQLYYPPL FTSMVNQGSV PPLFSITIDR NASSGLLAWG GLPPAKGLEK
GKDVELDMII TNLIDVPETA YDYSFYTVIP DGWQFGLNTN TRKFPYIVDS GTTLCYLPSA
EAQAINLSFN PPAIYLWMYG AYFTSCDAIV PRLGVILGGK TFYMNPMDLI NQDMVDPLTG
LCMTAIADGG AGPYILGDVF MQNALTVFDV GRGKMRFLGR EFY
//