ID M1W6A8_CLAP2 Unreviewed; 415 AA.
AC M1W6A8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Related to extracellular metalloproteinase {ECO:0000313|EMBL:CCE34516.1};
GN ORFNames=CPUR_08449 {ECO:0000313|EMBL:CCE34516.1};
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE34516.1, ECO:0000313|Proteomes:UP000016801};
RN [1] {ECO:0000313|EMBL:CCE34516.1, ECO:0000313|Proteomes:UP000016801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1 {ECO:0000313|EMBL:CCE34516.1,
RC ECO:0000313|Proteomes:UP000016801};
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
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:CCE34516.1}.
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DR EMBL; CAGA01000092; CCE34516.1; -; Genomic_DNA.
DR AlphaFoldDB; M1W6A8; -.
DR STRING; 1111077.M1W6A8; -.
DR MEROPS; M04.025; -.
DR VEuPathDB; FungiDB:CPUR_08449; -.
DR eggNOG; ENOG502SUPZ; Eukaryota.
DR HOGENOM; CLU_008590_0_3_1; -.
DR OrthoDB; 2679274at2759; -.
DR Proteomes; UP000016801; 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 PANTHER; PTHR43579; -; 1.
DR PANTHER; PTHR43579:SF1; NEUTRAL METALLOPROTEINASE; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 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:UP000016801};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 124..241
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 245..411
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT REGION 108..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 45931 MW; 2710DC3828A10C78 CRC64;
MPCNCFIVPP HLLKAIAASS HNNETTRKSA QLCVDFHEKL IAARRQRMAA AALNQVQDPG
CFRASPFIPQ ILLRHLSKGE GVDDAARSLA AKDLDHAQQL MIVKKGDASK ATLEADRPKK
APKDSPHRAI YDAQHTEDQS ALPGELKRSE GEPKNKDKVV NEAYDQVGAV LEFYKEKFHW
NSIDNKGSKV ASSVHFGESY ENAFWDPEHL QMVFGDGGEF LKNFTKCVDV IGHELTHAIT
EHTSPLEYQD QPGALNEHVS DVFGVMIKQK VENETSDKAD WLIGEGCLVP DVKGLALRSM
KAPGTAYDDP RFGKDPQVDN MSGYEKSYDD NGGVHIYSGI PNKAFYLAAT AFGGYSWEKA
GQIWWKAMTS GNIPPRCSFK QFADVTVDCA EEEFGEEAAK TVRQAWTDVG VSRKI
//
