ID F7WBK3_SORMK Unreviewed; 488 AA.
AC F7WBK3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=WGS project CABT00000000 data, contig 2.78 {ECO:0000313|EMBL:CCC14432.1};
GN ORFNames=SMAC_09213 {ECO:0000313|EMBL:CCC14432.1};
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:CCC14432.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC14432.1, 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:CCC14432.1};
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:CCC14432.1}.
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DR EMBL; CABT02000078; CCC14432.1; -; Genomic_DNA.
DR RefSeq; XP_003346910.1; XM_003346862.1.
DR AlphaFoldDB; F7WBK3; -.
DR MEROPS; A01.082; -.
DR GeneID; 10804327; -.
DR KEGG; smp:SMAC_09213; -.
DR VEuPathDB; FungiDB:SMAC_09213; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_4_1; -.
DR InParanoid; F7WBK3; -.
DR OrthoDB; 615305at2759; -.
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 Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..488
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003364355"
FT DOMAIN 92..442
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 110
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 308
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 488 AA; 49845 MW; 65DADFDFAA1DE32D CRC64;
MAAFPFLSAS LVLFQLALCS AQHLNLTGPF HLTNHKSNQN LTAHNTSQPL NLTTHTSGDG
CVHLPIIHST NIDHFARRGI QLALNNRSDV AYYAQLEIGT PPQTVYTQLD TGSFELWVNP
DCTTVSASDS IFCQRIGHYN ASSSSTAVSL GTNKTLHYGI GSANISYVTD VVSLAGTSSA
SSLKKVQFGV ATSSKDAFSG ILGIGYGQGL ATKYPNFVDQ LYAQNVTKVK AYTLALGSKS
AKEGTIVFGG VDTSKFSGPL AKVPIISAAA SPDGVPRFWV QMGGINLTPP SGEPTAKYEG
SQIPAFLDSG STMTILPPKL AGKIAKDFGS PAADANGFYQ VGSVFDLQTH SIWLTQASSC
GSTPAALRNV TDLSRVVGKC AVQPGQQAAV VDVVSETSIP RPSTSTAAPE SGSGGTGTIT
TGFVSTTLAI PTGTASASLT AAGSTDGGVS GIAATAVAGG ASGMRSSAGS RVLGVAVAVG
VAVLTNWG
//
