ID A0A094HA39_9PEZI Unreviewed; 450 AA.
AC A0A094HA39;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 37.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=V501_08555 {ECO:0000313|EMBL:KFZ05201.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ05201.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ05201.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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:KFZ05201.1}.
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DR EMBL; JPKD01002328; KFZ05201.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094HA39; -.
DR STRING; 1420914.A0A094HA39; -.
DR HOGENOM; CLU_013253_0_0_1; -.
DR Proteomes; UP000029315; 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:SF23; ASPARTIC ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G15950)-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:UP000029315};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..450
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001897368"
FT DOMAIN 140..447
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 70..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 341
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 450 AA; 46833 MW; D32E7A0437690240 CRC64;
MHSKLYSLIL VTIFAAFVLA IPTPSTSRIQ KRSFKVHRKR NPDFKGYDGP TQLMKAYQKF
GMTVPEGLHL SVGSRHRNGK NRGAGRGNGT ATGAAAGAAA GTAAGNSTAV ANGTVQAAAP
QVSGVGSVTA TPVEPNDLEY IAPVTIGGQL IDMNFDTGSS DLWVFNTQLS AQSSAGHTLY
DPTKSPDFKL IQGATFDISY GDGSGAAGNV GTDTVDIGGA TVTGQAIEMA TDVSDSFIQD
TNSNGLVGLG FSKINTVKPQ KQKTFFDNAM ATLAEPVFTA DLRQDDVGAY EFGKIDTARF
TGDLTWAPID SSNGFWEFTS TKFSVGNGKV LNAIGGTAIA DTGTTLMLVD AAIVNAYYSQ
VAGAVNNAQV GGITFPCDSV LPDLNVDVGG TYTATIEGKF INFAQVNADT CFGGVQPTTG
NLQIYGDIFF KSQFVVFNGG NNTIGLAPHA
//