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
//