(data stored in ACNUC7421 zone)

SWISSPROT: MEP_ASPNC

ID   MEP_ASPNC               Reviewed;         631 AA.
AC   A2Q7V4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 58.
DE   RecName: Full=Extracellular metalloproteinase mep;
DE            EC=3.4.24.-;
DE   AltName: Full=Elastinolytic metalloproteinase mep;
DE   AltName: Full=Fungalysin mep;
DE   Flags: Precursor;
GN   Name=mep; ORFNames=An01g02070;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
DR   EMBL; AM269955; CAK43577.1; -; Genomic_DNA.
DR   RefSeq; XP_001388645.1; XM_001388608.1.
DR   SMR; A2Q7V4; -.
DR   MEROPS; M36.001; -.
DR   PaxDb; A2Q7V4; -.
DR   GeneID; 4977749; -.
DR   KEGG; ang:ANI_1_2332014; -.
DR   HOGENOM; HOG000159216; -.
DR   KO; K01417; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 1.10.390.10; -; 1.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR001842; Peptidase_M36.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF02128; Peptidase_M36; 1.
DR   PRINTS; PR00999; FUNGALYSIN.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A2Q7V4.
DR   SWISS-2DPAGE; A2Q7V4.
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..241
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407178"
FT   CHAIN           242..631
FT                   /note="Extracellular metalloproteinase mep"
FT                   /id="PRO_5000219322"
FT   ACT_SITE        426
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   METAL           425
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   METAL           429
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        470
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        505
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   631 AA;  69153 MW;  BF13EDD95535B863 CRC64;
     MHGLRLVCSI GTLPLVILAY PAASLHTTSA AVDLDSLRLT SNSEYVNSVH VDTNRSVAVS
     AEEHYTDTAA RLVQNIVPGA SFRLIDDHFV GDNGVAHVYF RQTLHGIDID NADFNVNIGK
     DGLVLSFGHS FFTGALPSSH LDNTNVLSPE AALRGARDAI QLPLTIDNVS TEAAEGRNEY
     IFREAVGAVS DPKAKLVYLV KPEGTLALTW RIETDMYEHW LLTYIDAETT TVHGVVDYVA
     DATYQVYPWG TNDPAEGHRT IVTDPWDLSA SAYTWISDGR DNYTTTRGNN AIAHWNPTGG
     GSYLYNLRPS DPNLNFQWPY SPNMSPPRSY INASIVQLFY TANAYHDLLY TLGFTESAGN
     FQWNNSAHGG RDKDYVILNA QDGSGFSNAN FATPPDGIPG RMRMYIWIES TPSRDGSFDA
     GIVIHEYTHG VSNRLTGGSH NAGCLSALES GGMGEGWGDF MATAIRIKPN DTRTTSYTMG
     AWADNDKCGV RDYPYSTSFT ENPLNYTSVN TMNGVHAIGT VWATMLYEVL WNLIDKYGKN
     DGSRPVFRNG VPTDGKYLMM KLVVDGMALQ PCNPNFVQAR DAILDADIVL TGGKNRCEIW
     RGFAKRGLGQ GAAHSSLNWM RRGSTLLPTG C
//

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