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Database: UniProt
Entry: A0A139HGU3_9PEZI
LinkDB: A0A139HGU3_9PEZI
Original site: A0A139HGU3_9PEZI 
ID   A0A139HGU3_9PEZI        Unreviewed;       457 AA.
AC   A0A139HGU3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-FEB-2023, entry version 28.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=AC578_2723 {ECO:0000313|EMBL:KXT01701.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT01701.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXT01701.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT01701.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXT01701.1}.
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DR   EMBL; LFZN01000051; KXT01701.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139HGU3; -.
DR   STRING; 321146.A0A139HGU3; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000070133; 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; 2.
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:UP000070133}.
FT   DOMAIN          89..398
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        120..125
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        324..357
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   457 AA;  49857 MW;  BD681BC5397B72AD CRC64;
     MKGALLTSAL AAGAQAGVHK MKLQKIPLSE QLEGFNIEDQ VKNLGQKYMG QKYMGIRPQN
     RMSEMFKETS VHAEKGHPVA VDNFLNAQYF SQIAIGTPPQ EFKVVLDTGS SNLWVPSQDC
     GSIACYLHSK YDHGDSSTYK QNGSDFAIRY GSGSLEGYVS QDTVQIGDLK IKDQLFAEAT
     SEPGLAFAFG RFDGILGLGY DSISVNGIPP PFYNMIDQGL LDENKFAFYL SSTDNGDESE
     AIFGGVNEDH YTGKMTNIPL RRKAYWEVDL DAITFGEQTA EIDATGAILD TGTSLIALPS
     TLAELLNKEI GAKKSYNGQY TVDCSKRDSL PDLTFTLTGH NFTIDSYDYI LEVQGSCISA
     FMGFDIPEPA GPLAILGDAF LRKWYSVYDL GSNSVGLAKA NSRISNANRR VLHLRKAVHG
     NFTRHASSFS VNSGLAADRT AEVVEINHTE DSSSEKP
//
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