ID A0A0A1SV67_9HYPO Unreviewed; 426 AA.
AC A0A0A1SV67;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=VHEMI02207 {ECO:0000313|EMBL:CEJ82121.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ82121.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ82121.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(2015).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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; CDHN01000001; CEJ82121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1SV67; -.
DR STRING; 1531966.A0A0A1SV67; -.
DR HOGENOM; CLU_013253_0_3_1; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000039046; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF2; ASPERGILLOPEPSIN-1-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; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000039046};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..426
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001978985"
FT DOMAIN 110..419
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 128
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 313
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 426 AA; 46201 MW; 8FF091B2009F4C15 CRC64;
MRSSAAFLTC MVAAATAAPA LESGLPTEIV ANGKSFRLQQ TRNERFKARD AVHEFYMAHS
KYGKAIPAAL KATIQQRPSL NNKFSIYGDG TVSKGSVTAS PVQPAYDSEY IIPVQVGTPP
QTLPMNLDTG SADFWVFSTT TYAMEIQHQK LYSPNASLTS QVMPGESWKV LYGDGSGASG
IVYKDKVSVA GLEVATQAVQ VAVDVSPDIS KDSASSGILG MASGRANTVR PHIQLTFLDN
IMEKLQQPVF TANLQKGAPG SYDFGYIDHK AYTGKIKYSQ ISLGSPFWQV YLTGYAVGDL
QTYNSTRFPA IVDTGTSLLM LPEDIVKSYY GKVPDSYLDP KIEMMMIPCN ATLPDLTFGI
DEYRGRIPGH FMNYAQNEDG HCYGGLQSSE GLPFGVIGDI LIKSQYVVFN RGDLTVGFAN
KKTPLA
//