ID K2S0S1_MACPH Unreviewed; 851 AA.
AC K2S0S1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:EKG16094.1};
GN ORFNames=MPH_06660 {ECO:0000313|EMBL:EKG16094.1};
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:EKG16094.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG16094.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG16094.1,
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 -!- 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:EKG16094.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AHHD01000285; EKG16094.1; -; Genomic_DNA.
DR AlphaFoldDB; K2S0S1; -.
DR STRING; 1126212.K2S0S1; -.
DR VEuPathDB; FungiDB:MPH_06660; -.
DR eggNOG; ENOG502S90K; Eukaryota.
DR HOGENOM; CLU_014251_1_0_1; -.
DR InParanoid; K2S0S1; -.
DR OrthoDB; 23292at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR005151; Tail-specific_protease.
DR PANTHER; PTHR37049:SF4; CHITIN-BINDING TYPE-2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR37049; PEPTIDASE S41 FAMILY PROTEIN; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..851
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003864654"
FT DOMAIN 362..576
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|Pfam:PF03572"
FT REGION 797..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 851 AA; 92264 MW; 89770A667171B37C CRC64;
MMSFTRLVAL SCLLFGSALS KPAPRASAQA STTVSSAQTL PTTCGDIIQQ ADFEDVYSFS
ASQVYECLTS VPFNDAVALR FIDYYNDTMQ FHSTLAYLKD PPEGYQQPPV DLLDGLAVIK
QNISAGYYKN QYAFEAEVQK LVYSVHDMHV DLSSGILSAF AFGSDSWEIV SVSKDGKELP
QIYLTGDILY TEDPQPITAI NGEDPVEFLT KLAALNAVGT LEPHADWNQL MSSPAIDIQG
IYSVFSQGLT FYPGDKLTFT WADDTKVDTD WLAFYMNAAH TGPLSTGGDF YNYFVLGLLP
DSYNESVYPV FEDDSDGTSE GTLTNWYNAS FKAYPSNPDV YQDGLAPGGG VVTGYLLNET
STGVLSIPSF DMYGDYIYNF STAVVDFVDK ARDANMSRII IDLQQNLGGQ SLLAYDTYRR
FFPQADPYRG SRRRDHEMAN TLGRVTTGFW DSLEPGTDDY DNYYQLLASD EWVVTDRLNA
DTGANFTSWA EYYGPRTYHG DSFSLNERYN LTSDVFVESA FDGYSFGFPG LGQTWAAEDI
LLLTDGLCSS SCAEFVEWMT QRGVRTIVAG GRPSAGPMQA ASGTRGARLY SADLIDADID
WVLSVDNSTA GSLPATRDPG MQTSYAGLNL RDQVREGDAA GVPLQFMYQA AHCRIYYTIH
NVYNMTRLWL DAAAAAWDDD SLCVDGSTGY ASFLNTTAAK DPPARLADEP VQLNVLDTSL
DYNSDANAAE SGLEAATSSA KGGATVCKTK TGGCGANQKA VPAMKVQCGQ TITECVCMPV
CRTDLDCGGA LKCRDKTSTP DKSLGTQTTS KLANNVKGSS SSGSGKGVCK PDTKLQGTKY
LSLCAGQAKS G
//
