ID B8NWT9_ASPFN Unreviewed; 417 AA.
AC B8NWT9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 08-NOV-2023, entry version 71.
DE SubName: Full=Aspartic-type endopeptidase, putative {ECO:0000313|EMBL:EED45897.1};
GN ORFNames=AFLA_121260 {ECO:0000313|EMBL:EED45897.1}, G4B84_011799
GN {ECO:0000313|EMBL:QMW36270.1};
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:EED45897.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED45897.1, 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:EED45897.1};
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:QMW36270.1, ECO:0000313|Proteomes:UP000515286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW36270.1,
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 -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; EQ963485; EED45897.1; -; Genomic_DNA.
DR EMBL; CP059873; QMW36270.1; -; Genomic_DNA.
DR RefSeq; XP_002384833.1; XM_002384792.1.
DR AlphaFoldDB; B8NWT9; -.
DR MEROPS; A01.081; -.
DR EnsemblFungi; EED45897; EED45897; AFLA_121260.
DR VEuPathDB; FungiDB:AFLA_014131; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_035052_1_0_1; -.
DR OMA; WFNRECY; -.
DR OrthoDB; 4940213at2759; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR Proteomes; UP000515286; Chromosome 8.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_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; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF47; ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01220)-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..417
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035105786"
FT DOMAIN 48..409
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 66
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 298
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 417 AA; 45559 MW; C5016F73F7591F14 CRC64;
MKLIQLSSVL HFTALSSALT LPLNRRSPCE EEMSHNAPLL ATLGGSVFDV DVTIGADNQT
FKLLVDTGSS DTYIMQDGFT CINATDNQII APEDCKYGPE TYHVSSSYEQ VPDQNFGIEY
GAGLASGVMA YETITIADVT VRTKLAFADR SHPMGDGVNN GLLGLGYPSL TSAHPGTFTP
NDTYFYNRAV YNPVVNEMYE QGLIEEPYFS IALAHTARDS TGAFGGYISL GELPPVELTS
EFTTVPVEIM ENIPINITSD KRQISYWAFT TPAVKYGPAE EEEDALVVDH TPFQLFIDTG
NEFSILPTAV VDPVNTRFEP PAVYNDELKA YIVDCGAKPP VFGVVVGNQT FYHAPEDLIY
NTGNGYCVST LVPSEKNGRP GLVINILGVP FFKNLVAVFD FGKDEMRFAR VSNGYFL
//