ID A0A177CHX4_9PLEO Unreviewed; 396 AA.
AC A0A177CHX4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JUN-2023, entry version 24.
DE SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:OAG06420.1};
GN ORFNames=CC84DRAFT_1187331 {ECO:0000313|EMBL:OAG06420.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG06420.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG06420.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG06420.1,
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; OAG06420.1; -; Genomic_DNA.
DR RefSeq; XP_018036785.1; XM_018180922.1.
DR AlphaFoldDB; A0A177CHX4; -.
DR STRING; 1460663.A0A177CHX4; -.
DR GeneID; 28764408; -.
DR InParanoid; A0A177CHX4; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 3.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 2.
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:OAG06420.1};
KW Protease {ECO:0000313|EMBL:OAG06420.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT DOMAIN 78..396
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 96
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 299
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 396 AA; 43400 MW; 6FFC8897DEDBB28B CRC64;
MGAREQKRIN VKPNSGCEKA GMKSYASLLE KFDEVTKNFK NFFKSKSKKS TKPVLRKVED
DGQKGEVKAE DQLNDSMYLC PVAIGTPPQV CNLHFDTGSS DLWLWSTELD SKTQSTGKSS
GHNIYSPKSS STWKKISGSS WKIRYGDGSN ASGIVGTDNV TLGGLCVENQ AIELASKLSP
QFIKGAGDGL LGLAFGKINT VKPKAVKTPV ESMIDQDDIE EGEELFTCYL GSWRDKDEED
QGESFFTFGY IDEDVVKRCG TEMHYVPIDS SKGFWQFKSE SAIVNGRIID RTGNTAIADT
GTTLALVFPV DTPAEALPKV TVAVGDKQFE IQKEDFGFAK CGNGMQYGGI QSRGDSTFDI
LGDTWLKAVY VVFDQGKKRL GVVQRVEEEQ NVSAPK
//