ID K2RCW5_MACPH Unreviewed; 551 AA.
AC K2RCW5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Peptidase A1 {ECO:0000313|EMBL:EKG12388.1};
GN ORFNames=MPH_10505 {ECO:0000313|EMBL:EKG12388.1};
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:EKG12388.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG12388.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG12388.1,
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:EKG12388.1}.
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DR EMBL; AHHD01000451; EKG12388.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RCW5; -.
DR STRING; 1126212.K2RCW5; -.
DR VEuPathDB; FungiDB:MPH_10505; -.
DR eggNOG; ENOG502RV5I; Eukaryota.
DR HOGENOM; CLU_009988_3_0_1; -.
DR InParanoid; K2RCW5; -.
DR OrthoDB; 1831139at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR CDD; cd12087; TM_EGFR-like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR15549; PAIRED IMMUNOGLOBULIN-LIKE TYPE 2 RECEPTOR; 1.
DR PANTHER; PTHR15549:SF6; PROTEIN SKG6; 1.
DR Pfam; PF00026; Asp; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 335..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..295
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 374..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 59473 MW; CB1D77E054AB97D5 CRC64;
MSASSTWETI GNYSTWVERK LGYDAGATYG YDTVGLGNVG EGGPTLTNTT VGVMMDLDFF
VGAFGLHPKP TNFSTFNDQS PSYMSKLKDA NIIPSLSYGY TAGNQYRLNK VLASLTLGGY
DSSKFTPNNM SFSFAPDNER DVVVGLQGIS MTSATKGNVD LLPTPVTMYI DSTVPQIWLP
VDACAKFEEA FGLAYDNETD LYLVDDALHD TLVAQNANVT FTIGQSTTGG QTIDIVLPYA
AFDLTAQPPY QGLFNATSYF PIRRGMNESQ YVFGRTFLQE AYIIVDHERQ NFSVSQCVFD
FNSKQTIIPI FPIGDENSSS SSDGTESGGS LSTGAIAGIA VGGVVAVLAA LSLVGLFYWR
RRYRALKAKL EPDKLGSAST GDGSSETPPA GGQNEKPTLV IPKAELDAAP SANALQRDKY
AKQDLPTHLY PSEVEANEQQ IFEMPGDFPK TSEADSRELS EKQAMMLREQ KYNGTDPDPS
SPTTPTASDR PRPSPVNPED VKRVIHPGGL PISPLTAYGE HGNTRSPLSP LLAGPSSGEP
SPSRRRFSFE D
//