ID A0A178DT90_9PLEO Unreviewed; 509 AA.
AC A0A178DT90;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:OAL47016.1};
GN ORFNames=IQ07DRAFT_146409 {ECO:0000313|EMBL:OAL47016.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL47016.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL47016.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL47016.1,
RC ECO:0000313|Proteomes:UP000077535};
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; KV441653; OAL47016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178DT90; -.
DR STRING; 765867.A0A178DT90; -.
DR InParanoid; A0A178DT90; -.
DR OrthoDB; 1831139at2759; -.
DR Proteomes; UP000077535; 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 Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
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:SF89; SACCHAROPEPSIN; 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:OAL47016.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:OAL47016.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 417..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..382
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 509 AA; 55681 MW; 93E2FEF4D8038DC7 CRC64;
MASNTTVPEA FSFPPSQLWD GNDGKWSTFT VRLGTPPQNY RILPFTTISQ LWIPEVGGCQ
EAGDPVDCGA LRGVYDVDGQ RSTGFSTNRS STWDEIGMYG LVTGNLLRDT TGAVGNHGLD
TVGLTEDPAQ PKFTDDLITL YRVKKFMVGG LGLGPKPTLF PNVTTEYDGL LQKLKKQNMI
PSLTWGYTAG AAYRSSTSFG SLTFGGYDKS RFKGDVVNGS VYDIGSGDYR TLNAPISSIF
ASGSFDGPTA LLLDAPLLAT IDSSVSQLWF PREICDSFER VFGLTYDSAT DLYLVNDTSH
EKLLDLNPTI TITLRSDDLS GSNHIGLPYA ALDLQASYPM YNSTRNYFPI RRSGSSKATL
GRVFLQEAYV IADYDRAKFS VHPVVTEQNL LAPEIISIQP PTSQNIPQQR RLSGSSIAGI
VVGSVAAGVL IFALTFYLWR HSRKLFGAWL HGGSDQDDTE KLREEKRNSK VYEMMGSEVP
ELEKIPDELP GVKLYAEADS RPVNVNGNN
//
