ID A1CKP1_ASPCL Unreviewed; 398 AA.
AC A1CKP1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Aspartic endopeptidase Pep2 {ECO:0000313|EMBL:EAW09715.1};
GN ORFNames=ACLA_039300 {ECO:0000313|EMBL:EAW09715.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW09715.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW09715.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; DS027056; EAW09715.1; -; Genomic_DNA.
DR RefSeq; XP_001271141.1; XM_001271140.1.
DR AlphaFoldDB; A1CKP1; -.
DR STRING; 344612.A1CKP1; -.
DR MEROPS; A01.018; -.
DR EnsemblFungi; EAW09715; EAW09715; ACLA_039300.
DR GeneID; 4702814; -.
DR KEGG; act:ACLA_039300; -.
DR VEuPathDB; FungiDB:ACLA_039300; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_4_1; -.
DR OMA; KYDHDAS; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:InterPro.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05488; Proteinase_A_fungi; 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; IPR033819; Saccharopepsin.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF89; SACCHAROPEPSIN; 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 Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..398
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002633204"
FT DOMAIN 85..395
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 103
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 287
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 116..121
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 321..354
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 398 AA; 43541 MW; D5E874C011FC3498 CRC64;
MKTVSLLTAS ALLGCASAEV HKLKLNKVPL EEQLYTHNID AHVRALGQKY MGIRPNIHKE
LLEENSFNDM SRHDVLVDNF LNAQYFSEIE LGTPPQKFKV VLDTGSSNLW VPSSECGSIA
CYLHTKYDSS ASSTYKKNGT EFAIRYGSGE LSGFVSQDNL KIGDLKIEKQ DFAEATNEPG
LAFAFGRFDG ILGLGYDTIS VNKIVPPFYN MLNQGLLDEP VFAFYLGDAN KEGDSSVATF
GGIDKDHFTG ELTKIPLRRK AYWEVDLDAI ALGDNVAELD NTGVILDTGT SLIALPSTLA
DLLNKEIGAK KGFTGQYSVE CDKRDSLPDL TFTLSGHNFT IGPYDYTLEV QGSCISSFMG
MDFPEPVGPL AILGDAFLRK YYSVYDLGNH AVGLAKAK
//
