ID K2R5R4_MACPH Unreviewed; 378 AA.
AC K2R5R4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 22-FEB-2023, entry version 46.
DE SubName: Full=Peptidase A1 {ECO:0000313|EMBL:EKG17726.1};
GN ORFNames=MPH_05037 {ECO:0000313|EMBL:EKG17726.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG17726.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG17726.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG17726.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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:EKG17726.1}.
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DR EMBL; AHHD01000228; EKG17726.1; -; Genomic_DNA.
DR AlphaFoldDB; K2R5R4; -.
DR STRING; 1126212.K2R5R4; -.
DR MEROPS; A01.018; -.
DR VEuPathDB; FungiDB:MPH_05037; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_4_1; -.
DR InParanoid; K2R5R4; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:InterPro.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05488; Proteinase_A_fungi; 1.
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 InterPro; IPR033819; Saccharopepsin.
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:UP000007129}.
FT DOMAIN 65..375
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 83
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 267
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 96..101
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 301..334
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 378 AA; 41126 MW; E13236869A5413DE CRC64;
MKLKKVPLAE QLEHANIGDH VKALSQKYMG SRPQLNSVEE IFKTQPIQAD SEHPVPVTNF
LNAQYFSEVS LGTPPQTFKV ILDTGSSNLW VPSSECGSIA CYLHTKYDSS ASSTYSKNGS
TFEIRYGSGS LSGFVSNDVF TIGDLTVKDQ DFAEATSEPG LAFAFGRFDG ILGLGYDTIS
VNHIVPPFYN MIDQGLLDEP VFAFYLSDTN DEGSESVATF GGIDESHYTG KLTKIPLRRK
AYWEVDLDSI TFGDATAELD NTGAILDTGT SLIALPSTLA ELLNKEIGAK KSFNGQYTVD
CDKRDGLPDL TFTLTGHNFT ITSYDYILEV QGSCISAFMG MDFPEPAGPL AILGDAFLRK
WYSVYDLGND AVGIAKAK
//