ID G3YDG9_ASPNA Unreviewed; 410 AA.
AC G3YDG9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=Aspartic protease {ECO:0000313|EMBL:EHA18836.1};
DE EC=3.4.23.1 {ECO:0000313|EMBL:EHA18836.1};
DE Flags: Fragment;
GN ORFNames=ASPNIDRAFT_211797 {ECO:0000313|EMBL:EHA18836.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA18836.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA18836.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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:EHA18836.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACJE01000020; EHA18836.1; -; Genomic_DNA.
DR AlphaFoldDB; G3YDG9; -.
DR STRING; 380704.G3YDG9; -.
DR HOGENOM; CLU_013253_9_3_1; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05474; SAP_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; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033876; SAP-like.
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; PS00141; ASP_PROTEASE; 2.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EHA18836.1};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00022622};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EHA18836.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..410
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003460307"
FT DOMAIN 63..385
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 81
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 276
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 311..350
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT NON_TER 410
FT /evidence="ECO:0000313|EMBL:EHA18836.1"
SQ SEQUENCE 410 AA; 44152 MW; 78C40D09DFADD957 CRC64;
MKSTTLLSLA WATQSAYSLS IHERDEPATL QFNFERRQIA DRSRRKRSTA SADLVNLATN
LGYTMNLTLG TPGQEVSVTL DTGSSDLWVN GANSSVCPCT DYGSYNSSAS STYTFVNDEF
YIQYVDGSEA TGDYVNDTLK FSNVTLTNFQ FAVAYDGDSE EGVLGIGYAS NEASQATVGG
GEYTNFPEAL VDQGAINWPA YSLWLDDLDE GKGTILFGGV NTAKYYGSLQ TLPIVSIEDM
YVEFAVNLTA VHLEKNGNSV SVNNSATQFP IPAVLDSGTA LTYIPTSAAA SIYEAVGAQY
LSEYGYGVIE CGVKDEDFTF LFDFGSFNMS VDISEMILEA SSDMTDMNVC TFGLAVIENE
ALLGDTFLRS AYVVYDLGNN EISLAKANFN PGEDHVLEIG TGSDAVPKAT
//
