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Database: UniProt
Entry: A0A0D2F5Q8_9EURO
LinkDB: A0A0D2F5Q8_9EURO
Original site: A0A0D2F5Q8_9EURO 
ID   A0A0D2F5Q8_9EURO        Unreviewed;       378 AA.
AC   A0A0D2F5Q8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-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=PV04_10511 {ECO:0000313|EMBL:KIW62330.1};
OS   Phialophora macrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW62330.1, ECO:0000313|Proteomes:UP000054266};
RN   [1] {ECO:0000313|EMBL:KIW62330.1, ECO:0000313|Proteomes:UP000054266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW62330.1,
RC   ECO:0000313|Proteomes:UP000054266};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KN846963; KIW62330.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2F5Q8; -.
DR   STRING; 5601.A0A0D2F5Q8; -.
DR   MEROPS; A01.013; -.
DR   HOGENOM; CLU_013253_3_4_1; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000054266; 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   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
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:SF51; NAPSIN-A; 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:UP000054266};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..378
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002241710"
FT   DOMAIN          67..375
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        85
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        300..337
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   378 AA;  41327 MW;  D07AC939E97AC9F4 CRC64;
     MNIVLMLLSM LYSCVFAHIH LKLEQAPSSH DQASLLRHVR ALSNQYGQRV LPDEINLPID
     NLFNGQYFST IGIGTPPQYF KLVMDTGSSN LWVPGQCRPT VCRSHARYNA TLSSTFEKNG
     SQFSTEYGTG GVSGHVSRDT LWVGDVQIKR QLFAEATYED SLIASGSFDG IFGLGHDAVA
     INGIKPPLYR MLDQKLIATP VFSFYFGDSA RGTESFCAIG GIDDAAYEGA VLRLPLRRKI
     YWEVDLNAAS LGGAVALDLN IGAILDTGTS LIAMPSNFAA LFNRYIGATQ VSSGLYEVSC
     HKRDQLPDLT FTLSGSNFSF SAYDYILELE NGSCLSCFQG FDSGEKTGPL FILGNAFLRR
     WYSIFDLENG TVGLAKAI
//
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