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Database: UniProt
Entry: Q7S314_NEUCR
LinkDB: Q7S314_NEUCR
Original site: Q7S314_NEUCR 
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
//
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