ID K2RUV9_MACPH Unreviewed; 512 AA.
AC K2RUV9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 28-JUN-2023, entry version 48.
DE SubName: Full=Peptidase A1 {ECO:0000313|EMBL:EKG13964.1};
GN ORFNames=MPH_08838 {ECO:0000313|EMBL:EKG13964.1};
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:EKG13964.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG13964.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG13964.1,
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:EKG13964.1}.
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DR EMBL; AHHD01000376; EKG13964.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RUV9; -.
DR STRING; 1126212.K2RUV9; -.
DR MEROPS; A01.015; -.
DR VEuPathDB; FungiDB:MPH_08838; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_3_1; -.
DR InParanoid; K2RUV9; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05474; SAP_like; 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; IPR033876; SAP-like.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..512
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003864481"
FT TRANSMEM 487..511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..401
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 437..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 84
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 281
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 315..365
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 512 AA; 53187 MW; FE802EEC2E14E8E1 CRC64;
MPSLCAYLAA AAGLASLAHA VDAPAPKVVG FDIAKSRRRA LANLARRNLA RRDTVSATLA
NYRSLYQINV TVGTPGQRIG LQIDTGSSDV WFPYAASVQC TEGGCESAFD PESSSTFEDI
GKGEFQIQYV DGTQITGDYI RDVLAIGDTQ IRNMTMAVAT DADDTPEGIM GVGFIQDETL
AQQENITYPN VPVQLVNQGF INTIAYSLWL NDLDSSTGNV LFGGVDSDKY QGDLIGLPIQ
PDSQSGTITS FTVAMSSINV KAKGGNSVYS QTNLDLPAIL DSGTTLSLLP DDIANAIIQG
VGARPTRDYG YVVNCNIGTT GAAIEFGFGG SDGPTISVGM DEMVLPLTDE EGNPARFRAS
GEEACTFGIE PAGNDPILLG DTFMRSAYVV YDLHNNQIAL ANTKFNATSS NVQEITNTTI
PGVSKVASGL TVTQTATGPI RASGARKTGT ATETAAPGTG TFDLGASSST GGSSEKGAAV
GLPAPRIALE TVMCGVAVAI SAMFGGSLMI LL
//