ID A1CH14_ASPCL Unreviewed; 468 AA.
AC A1CH14;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Aspartic-type endopeptidase (CtsD), putative {ECO:0000313|EMBL:EAW10169.1};
GN ORFNames=ACLA_046350 {ECO:0000313|EMBL:EAW10169.1};
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:EAW10169.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW10169.1, 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}.
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DR EMBL; DS027054; EAW10169.1; -; Genomic_DNA.
DR RefSeq; XP_001271595.1; XM_001271594.1.
DR AlphaFoldDB; A1CH14; -.
DR STRING; 344612.A1CH14; -.
DR MEROPS; A01.077; -.
DR EnsemblFungi; EAW10169; EAW10169; ACLA_046350.
DR GeneID; 4704302; -.
DR KEGG; act:ACLA_046350; -.
DR VEuPathDB; FungiDB:ACLA_046350; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_10_0_1; -.
DR OMA; MYMLLDT; -.
DR OrthoDB; 3087283at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
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:SF51; 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 Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..468
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002633113"
FT DOMAIN 100..407
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 118
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 301
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 131..136
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 468 AA; 50516 MW; 528ACEA160F3F72D CRC64;
MRFSQCLLTI TYLASTVTAF VPYSFHLEAS TDDSAANDVA RRFVPWTLLA DDPGDEPESI
TLDIKKMPVR RDNKYRIVIA DTPTTPNTAA LSQDGMDYSY FCAVDVGSQR QRMWMLLDTG
GPNTWVFSSE CETETCTNHT RFEQPASKTL KPEPYAWAIG YGKGQVSGVL GNDTLSISGM
DISVTLGLAK NASSHFDTYP ADGILGLGWS NNSNFDRPSF MEIVKKQGLL KSNTLAFSFS
RNSDGAKDGT VNFGTVDTAK FTGEITYTDI VPKSKRWNIP LDDASVNGVP CGFTNKSAFI
DTGTSYAMLP PKDAIKLHNL IPGATTSTAG DNFTLPCNST AVVQFNFSGL SYSISPKDYV
GPRKGSSCLS TIVGQALDGD DMWLLGDVFL KNVYTVFDYD HDRIGFANRS VPIVSTTTTA
VPSATGTGEA SSSSADPVIV HKGSATSTLV LRSLYLPALS VILCIFLL
//
