ID G3JDF5_CORMM Unreviewed; 531 AA.
AC G3JDF5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Peptidase M4, thermolysin {ECO:0000313|EMBL:EGX92630.1};
GN ORFNames=CCM_04003 {ECO:0000313|EMBL:EGX92630.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX92630.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX92630.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX92630.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388}.
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DR EMBL; JH126401; EGX92630.1; -; Genomic_DNA.
DR RefSeq; XP_006669214.1; XM_006669151.1.
DR AlphaFoldDB; G3JDF5; -.
DR SMR; G3JDF5; -.
DR STRING; 983644.G3JDF5; -.
DR MEROPS; M04.025; -.
DR GeneID; 18166026; -.
DR KEGG; cmt:CCM_04003; -.
DR VEuPathDB; FungiDB:CCM_04003; -.
DR eggNOG; ENOG502SHBN; Eukaryota.
DR HOGENOM; CLU_008590_0_3_1; -.
DR InParanoid; G3JDF5; -.
DR OMA; MKQFRTT; -.
DR OrthoDB; 2679274at2759; -.
DR Proteomes; UP000001610; Unassembled WGS sequence.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR InterPro; IPR032475; Protealysin_N_PP.
DR PANTHER; PTHR43579; -; 1.
DR PANTHER; PTHR43579:SF1; NEUTRAL METALLOPROTEINASE; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR Pfam; PF16485; PLN_propep; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001610};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 64..107
FT /note="Protealysin N-terminal propeptide"
FT /evidence="ECO:0000259|Pfam:PF16485"
FT DOMAIN 129..243
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 247..400
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT REGION 105..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..448
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 57477 MW; 86D652F35C394DA0 CRC64;
MCDQRCYIVP PHLLQAIADS TSNPEKVRES AKACLLSREK VSLARKELFA TLAQPRGYTT
QQRHQIVPPH VFRQISDAEV NDEETRARAK DNLEHVEGVI AQYKSSQGAE SEAQSLSAQA
KTKPPKATHR AVYDAENTTN ERSLPGKLVR EEGQKAVEDK AVNEAFDNVG SVLKFYKEKF
KWTSIDNHNA DVISSVHFGE AYENAFWDPT VRQMVFGDGG DFLNNFTASI DVIGHELTHA
VTEHTSPLDY QGQPGALNEH ISDVFGIMVK QMVQDEKSDA ADWLIGEDCL LPGVKGMALR
SMKEPGTAYN DARFGKDPQV SNMKDFEQMF DDNGGVHIFS GIPNKAFYLA AVALGGYSWE
KAGQIWWKTM NSGRIPTRCT FLQFADVTVD VAEEDFKVGK EDPDGGDDGD DGDDGDDGDD
GDGDGGDDDD DDNGGDEGDG DDDNDDNDDG GGDKKKDDGK GNGGKDGKDG KDGKDGKDGK
DGKDGKDGKD GKDGKDKDGK GNDGKGGSRC DEKGDGKDGK SENDEGDCGC N
//
