ID Q7S314_NEUCR Unreviewed; 616 AA.
AC Q7S314;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 3.
DT 24-JAN-2024, entry version 100.
DE SubName: Full=Secreted aspartic proteinase {ECO:0000313|EMBL:EAA29810.3};
GN ORFNames=NCU07533 {ECO:0000313|EMBL:EAA29810.3};
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110 {ECO:0000313|EMBL:EAA29810.3, ECO:0000313|Proteomes:UP000001805};
RN [1] {ECO:0000313|EMBL:EAA29810.3, ECO:0000313|Proteomes:UP000001805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC {ECO:0000313|Proteomes:UP000001805};
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA Lander E.S., Nusbaum C., Birren B.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; CM002238; EAA29810.3; -; Genomic_DNA.
DR RefSeq; XP_959046.3; XM_953953.3.
DR AlphaFoldDB; Q7S314; -.
DR STRING; 367110.Q7S314; -.
DR PaxDb; 5141-EFNCRP00000007867; -.
DR EnsemblFungi; EAA29810; EAA29810; NCU07533.
DR GeneID; 3875184; -.
DR KEGG; ncr:NCU07533; -.
DR VEuPathDB; FungiDB:NCU07533; -.
DR HOGENOM; CLU_013253_0_1_1; -.
DR InParanoid; Q7S314; -.
DR OrthoDB; 1203010at2759; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF2; ASPERGILLOPEPSIN-1-RELATED; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 3.
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:UP000001805};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..616
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004290857"
FT DOMAIN 165..601
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 60..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 454
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 616 AA; 67900 MW; 1E40E8D7540FC24E CRC64;
MLHSQNIASL GALLLLAQTS TTLAHPARHN YHHKHHTVRN IAVEHHIGVP ADTSDILWSD
HTAQTSSRKR GSLEDGSKGR KEDEGRTFTI RQVKNPRLER RSTTQRNGLS ALLHAYAKYG
VEPSPRIKRA MKLNPAFREY REELEKRGDI TATVAAIPPP GNYEYVSPVE IGTPPQTVWM
NIDTGSADFW VVSTDTPRYQ TRGHAIYDPH TSNSSVLVPD LNWRITYADG SGAHGIVYQD
RVSMDETLSF PSQVVQSATS ISWDFTTDPY VSGIMGLGMS SGNTVSDSIK DVEARTGVKI
LTFMDNVREQ LKEPVFTANL RDNAEGSYGF GFINETEYMG EVRYVDVKED GIFWEFEVGG
YLIGSEEEEE KADDDPVMMD PAQPDENPNT KQASTTIQSD QPTSMQSNPI TPSPTQTAQP
DTSSSSSPLL LETTNSTSTT NQKRISYPFT TIADTGTTLL LLPDRVVSDY YSTIPRAFYS
PEWAGYLFPC AYTSSLPDWS FFLGSAASET TTTTSDSKAE PKPDIGPEEV EEGQEKGQEE
KGFYYKGTVP GRYMNYGEVN ATWCYGGMQS SEDIGFSIFG DVLLKAQLVV FDLGGMRVGF
AGKELAEGVG KGEVSL
//