ID A0A177CGL0_9PLEO Unreviewed; 508 AA.
AC A0A177CGL0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:OAG06092.1};
GN ORFNames=CC84DRAFT_1245030 {ECO:0000313|EMBL:OAG06092.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG06092.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG06092.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG06092.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; KV441552; OAG06092.1; -; Genomic_DNA.
DR RefSeq; XP_018036457.1; XM_018184176.1.
DR AlphaFoldDB; A0A177CGL0; -.
DR STRING; 1460663.A0A177CGL0; -.
DR GeneID; 28767662; -.
DR InParanoid; A0A177CGL0; -.
DR OrthoDB; 1831139at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:OAG06092.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:OAG06092.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 404..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..369
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 508 AA; 55190 MW; 9961682BF8121C29 CRC64;
MVAPLIVTVS NTWLGNDGSW STFNIDVGTP PQSFRVLPSF QVQNVWLPIA DECIKISADA
EKCGVSRGAQ PFAQRTSAGF HTNVSSTWEA IGLYELGLER DRGISGNGMS GFDTFRVSNT
TLDRFPVTAY ASPGFWLGQL GLSTVPLNFS ETINSASLLV NLKDKGVIPS LTYGYQAGAS
YRETRVPGSL VLGGYDKSRA TTPLTININA DLSQALTVGL QDILVTNSFN GTLSMITTEP
ILAPLDSSIT ELWLPRSVCD RFEDAFGLEY DTNSGRYALS DATRNQLRQQ KPTLTFTIGT
NTLTGGNTTI IQFPYAAFDL QASFPIFANT TNYFPIRRAD NESQYAIGRV FMQEAYIGVD
YEQGIFNVSA ARWNETDPNI VPLPAGDVQP SEVPRAGADG KSHLAGGAIT GIVVGSIVAV
AILVGLSWFV YKHKQRRSYG AYGGALVATS EEKTYPRELQ DTDTEEVAGG EVFELPAKHG
HSQLHEVERI AELDRHEIIQ ELASNRDG
//