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Database: UniProt
Entry: B8NS75_ASPFN
LinkDB: B8NS75_ASPFN
Original site: B8NS75_ASPFN 
ID   B8NS75_ASPFN            Unreviewed;       485 AA.
AC   B8NS75;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   SubName: Full=Yapsin, putative {ECO:0000313|EMBL:EED47252.1};
GN   ORFNames=AFLA_053070 {ECO:0000313|EMBL:EED47252.1}, G4B84_000135
GN   {ECO:0000313|EMBL:QMW24890.1};
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952 {ECO:0000313|EMBL:EED47252.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED47252.1, ECO:0000313|Proteomes:UP000001875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167 {ECO:0000313|Proteomes:UP000001875}, and NRRL3357
RC   {ECO:0000313|EMBL:EED47252.1};
RX   PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
RN   [2] {ECO:0000313|EMBL:QMW24890.1, ECO:0000313|Proteomes:UP000515286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW24890.1,
RC   ECO:0000313|Proteomes:UP000515286};
RA   Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W.,
RA   Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R.,
RA   Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D.,
RA   Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.;
RT   "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a
RT   Large Insertion Potentially Contributing to Isolate Stress Tolerance and
RT   Aflatoxin Production.";
RL   Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; EQ963483; EED47252.1; -; Genomic_DNA.
DR   EMBL; CP059866; QMW24890.1; -; Genomic_DNA.
DR   RefSeq; XP_002383432.1; XM_002383391.1.
DR   AlphaFoldDB; B8NS75; -.
DR   SMR; B8NS75; -.
DR   MEROPS; A01.015; -.
DR   EnsemblFungi; EED47252; EED47252; AFLA_053070.
DR   VEuPathDB; FungiDB:AFLA_011206; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_9_3_1; -.
DR   OMA; QCYLAIM; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   Proteomes; UP000515286; Chromosome 1.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00022622};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..485
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5035142845"
FT   DOMAIN          63..390
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        312..351
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   485 AA;  51110 MW;  9F7C00A292CDD2EF CRC64;
     MRGASLLPVA LAALSCVDAL SLHRRDTPAT VELPIERRQH AGGLQKRDST LNLPLINYYD
     SFYILNLTLG TPAQQFAVAL DTGSSDLWVN VANSSYCSSR TNPCKPFGLY DPDASSTYKN
     LGVEFNATYG DGTNAYGYYA TDELGLGDVN VDDMQFGVAE STTITQGIIG VAYDTLTNEA
     SHEGKTYANL PQALVNSGAI KSPAYSLWLN DPQASRGSIL FGGVNKAKYK GELQTIPIVR
     TLRGYSYLAV TLTGVSVEQG KESEDYSSRL PIVVLLDSGT SLTYLPDSLV DELYKKFNAT
     FLEDDGLAYV DCELMKKDYT VNFDFSGATI AVGISELVLK AVAEDFPLGT CAFGVVPSGD
     SQDAMYILGD TFLRSAYVVY DLGNNEISLA NTNFSPGDDD IFEIGTGTSA VPGATPVESP
     VTSATVASAT DIVHTVMVGG TKATATGSNS GAAETSSSSG IAALPTSNTR HLLSGLAGAG
     LLLAL
//
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