ID A0A168HVX1_CORDF Unreviewed; 519 AA.
AC A0A168HVX1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 08-NOV-2023, entry version 27.
DE SubName: Full=Peptidase A1 {ECO:0000313|EMBL:OAA78346.1};
GN ORFNames=LEL_05169 {ECO:0000313|EMBL:OAA78346.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA78346.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA78346.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA78346.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA78346.1}.
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DR EMBL; AZHF01000003; OAA78346.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168HVX1; -.
DR STRING; 1081108.A0A168HVX1; -.
DR OrthoDB; 3087283at2759; -.
DR Proteomes; UP000076881; 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:SF75; ENDOPEPTIDASE (CTSD), PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07040)-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 Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..519
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007897731"
FT DOMAIN 110..412
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 413..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 308
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 141..146
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 342..374
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 519 AA; 52977 MW; 58567B0667319A69 CRC64;
MQLVPSLVCL ALWSSSAHAF YPYEPKWLKE SLESEAKRAA SVDNSEGLAF AIRQRGGRPV
ASQEAARLAA KYDTHGALAR RKNAYAVTTA TTPTTSDAAG INQDGTDYSY FIQVGLGSKG
AKVYMLVDTG AGSSWVMGSD CTSDACAKHD TFGSSQSDSL TISDKDFSVA YGSGKVKGKL
ATDTISVAGM SMKYQFGLAS TTSDDFKDFA FDGILGLSMG SGASANFLST LGSSGAVKST
VFGVALSRAA DGGTSGEIKF GGTNSAKYTG DITYTSVASK SGDWAINLDD MSFNGKKAGV
GGKLAYIDTG TTYIFGPSSI TDKLHAVIDG ASKQGSYYSV PCDSTTPITI TFSGVDYHIP
AKDWIAPKDS SGNCFSNIYG QEVVKDSWLM GATFLKNVYA VFDKDGSRIG FAQPAGSGSS
SSSSSASSSA TPSSSSGSSS PSTFSTKTSS TDSSPSASKP ALGLTGQETM TTAASGTATA
SGADATKTGD KGNGAASGLH AQGARLASIV GVAALLLLI
//