ID A0A0F7ZHG5_9HYPO Unreviewed; 436 AA.
AC A0A0F7ZHG5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=HIM_07960 {ECO:0000313|EMBL:KJZ72601.1};
OS Hirsutella minnesotensis 3608.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ72601.1, ECO:0000313|Proteomes:UP000054481};
RN [1] {ECO:0000313|EMBL:KJZ72601.1, ECO:0000313|Proteomes:UP000054481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3608 {ECO:0000313|EMBL:KJZ72601.1,
RC ECO:0000313|Proteomes:UP000054481};
RX PubMed=25359922; DOI=10.1093/gbe/evu241;
RA Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA Bushley K.E., Xiang M., Liu X.;
RT "Comparative genomics and transcriptomics analyses reveal divergent
RT lifestyle features of nematode endoparasitic fungus Hirsutella
RT minnesotensis.";
RL Genome Biol. Evol. 6:3077-3093(2014).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ030544; KJZ72601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7ZHG5; -.
DR OrthoDB; 1767283at2759; -.
DR Proteomes; UP000054481; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
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:SF81; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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:UP000054481};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..436
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002526216"
FT DOMAIN 41..391
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 398..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 313..352
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 436 AA; 46296 MW; 35E0E42B17E9303B CRC64;
MASVTISWLL GSLLFFVTFA RELKVVEGSL QHFHGKQFGS FIPMVEIGLG GDGKQKILGQ
LDTGSADLVL AQKNSAACEK QQQDCQDVPK GAGSFDPDRA PGTTKLDIPF NASFVSGESF
TGQFIKTGVQ IGDKITQNVQ LGLYSEAQQP EDTPMFPIFG TGPIGGTAAK VPYPNVPEQM
KLANMTNANA YGVYMNDFRG TNGQVVFGGY DTAKFQGQLQ EAPVVQNSAR NGDLVIDFSS
LNLVPGADSS ARLANASATM QQKVDLSGGK PLPPAFLDTG SPSVILPKEM VQNLARTLGA
NFSDDQGMGP VDCGLARSDA VMEFGFNKDS IKIRLPLEMM LEPKAKTGSD DCMLAVLPSD
GPDKDIATLG AAMMQAAYIV FDIDQKRLLM AQAKPNVTES AIKELPPVER GGTRNPQSAK
TGRKGAEGLQ GSSDKK
//
