ID Q0CVD5_ASPTN Unreviewed; 424 AA.
AC Q0CVD5;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=ATEG_02349 {ECO:0000313|EMBL:EAU37311.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU37311.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; CH476596; EAU37311.1; -; Genomic_DNA.
DR RefSeq; XP_001211527.1; XM_001211527.1.
DR AlphaFoldDB; Q0CVD5; -.
DR STRING; 341663.Q0CVD5; -.
DR MEROPS; A01.079; -.
DR EnsemblFungi; EAU37311; EAU37311; ATEG_02349.
DR GeneID; 4317290; -.
DR VEuPathDB; FungiDB:ATEG_02349; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_0_1; -.
DR OMA; NGVGEYE; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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:SF23; ASPARTIC ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G15950)-RELATED; 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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007963};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..424
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004170644"
FT DOMAIN 105..420
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 121
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 307
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 424 AA; 45246 MW; 0C30F50C517DF554 CRC64;
MKLPESLLIA LSLSYGVLSA PTPGQPQLNG RSFKVERVRR GAGTIHGPTA LRRAYEKFGI
VPMDLGIDLD DFVPISKHAA LQQDVAEPDQ TGAVSAASVQ NDAAFVSPVK IGGQQIVLNF
DTGSSDFWVL NSRLPKLDTR GRTVYNPSNS STFKQMKGST FNITYGDTSF AYGGVGTDVV
DVGGVTVQDQ AIGIPTTVSS SFLEDTYSNG IVGLAFSKLN TISPNQQKTF FDNVAPILDE
PVLTASLKSD GVGEYEFGVI DHDKYQGDLA NITIDSSSGF WEFVSASFSV GGGALQDVRD
VRRSIADTGT SLMLLDQSVV DAYYKQVQGA VYVSSASGYI YPCSAVLPNL TMAVGEKHYA
TVPGEYMNFS EIGTNKTTGE TVCYGGVQSN QGTSMQIFGD VFLKAFFTVF DLRGPSLGLA
SPNF
//
