ID A0A094H642_9PEZI Unreviewed; 442 AA.
AC A0A094H642;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=V501_05821 {ECO:0000313|EMBL:KFZ08794.1};
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:KFZ08794.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ08794.1, 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:KFZ08794.1}.
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DR EMBL; JPKD01001838; KFZ08794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094H642; -.
DR STRING; 1420914.A0A094H642; -.
DR HOGENOM; CLU_013253_0_1_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: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};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW 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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..442
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001904072"
FT DOMAIN 126..434
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 144
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 328
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 364..397
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 442 AA; 47322 MW; FA980F3434DCD08D CRC64;
MHTFIKLLSA VLLVLSLTAW GVDASPRHKT KFSKHHRKGP LVLGGSTFKI NQHHNPKYKR
TANSGTVELA KTYKKFNVLF PDQLANAIAG IVGRLQGTDG VSAPLNVSNV NFGTVETLPE
AFDREYLSPV QIGTPPQTVN LNFDTGSADL WVNTNETPEN QQNGQIEYNP TLSSTAKKME
GATWDITYGD GSASSGIVYT DVVSIGGVTV QSQAVESAQQ VSSSFQADAA SSGLLGLAYG
TINTVQPVQQ KTFFENAMND LASPLFTVNL MKQAAGSYDF GYINASEYTG EIQYTPVDNS
RGFWGFNPSG FQVGNSSFNA SSWYAIADTG TSLLLLPSGM VDIYWSAVSG AKFDALQGGY
TFPCNTTLPS FTFGVEEYRG VIPGHFMNYA AITKATCFGG IQSSDALGFS IFGDVALKAQ
FVVFDGGDNT LGWANKDLSS SV
//