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Database: UniProt
Entry: A0A177CHX4_9PLEO
LinkDB: A0A177CHX4_9PLEO
Original site: A0A177CHX4_9PLEO 
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
//
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