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
//