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Database: UniProt
Entry: K2R5R4_MACPH
LinkDB: K2R5R4_MACPH
Original site: K2R5R4_MACPH 
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
//
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