ID A0A066XNH2_COLSU Unreviewed; 418 AA.
AC A0A066XNH2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Metalloprotease {ECO:0008006|Google:ProtNLM};
GN ORFNames=CSUB01_09283 {ECO:0000313|EMBL:KDN70733.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN70733.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388}.
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:KDN70733.1}.
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DR EMBL; JMSE01000302; KDN70733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XNH2; -.
DR STRING; 1173701.A0A066XNH2; -.
DR MEROPS; M04.025; -.
DR eggNOG; ENOG502SHBN; Eukaryota.
DR HOGENOM; CLU_008590_0_3_1; -.
DR OMA; FCTIVPP; -.
DR OrthoDB; 2679274at2759; -.
DR Proteomes; UP000027238; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 66..109
FT /note="Protealysin N-terminal propeptide"
FT /evidence="ECO:0000259|Pfam:PF16485"
FT DOMAIN 124..244
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 248..414
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT COILED 90..117
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 418 AA; 46755 MW; 1D88F12E6013BAE3 CRC64;
MSHICYVVPP YLLKGIADAE CNSHHERQAA KHALELRERF AATRAERLAI LGGPRAQRNR
LASRPSIIPD VLLRHIADSA DVDQDTRANA RRDLEHLQGL QQKIQRAQQD QEQVTLAAAV
DSSKQPKKPT YRAVYDAKNS NDEQDLPGQV VRVEGQKPVD DKAVNEAFDN VGEVLKMYKR
FGWLSIDNHN MNVISSVHFG DKYENAFWDP ERMQMVFGDG GEFLRNFTGT IDVIGHELTH
AVTEHTSPLD YQGMSGALNE HVSDVFGIIT KQIVENEKAD EADWLIGEGC IMPGVKGVAL
RSMKEPGTAY NDPRFGKDPQ PAHFKDYVPT FEDNGGVHIY SGIPNRAFYL VSMAFGGFSY
EKAGPIWWKA MNSGRIPPRC TFLQFADVTT ETAEELYGKE AGKIVRAAWV EVGVERNN
//
