ID   MMP_SFAVA               Reviewed;         386 AA.
AC   Q0E587;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Putative matrix metalloproteinase;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   ORFNames=ORF14;
OS   Spodoptera frugiperda ascovirus 1a (SfAV-1a).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Ascoviridae; Ascovirus.
OX   NCBI_TaxID=113370;
OH   NCBI_TaxID=7108; Spodoptera frugiperda (Fall armyworm).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16987980; DOI=10.1128/jvi.01639-06;
RA   Bideshi D.K., Demattei M.V., Rouleux-Bonnin F., Stasiak K., Tan Y.,
RA   Bigot S., Bigot Y., Federici B.A.;
RT   "Genomic sequence of Spodoptera frugiperda Ascovirus 1a, an enveloped,
RT   double-stranded DNA insect virus that manipulates apoptosis for viral
RT   reproduction.";
RL   J. Virol. 80:11791-11805(2006).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR   EMBL; AM398843; CAL44614.1; -; Genomic_DNA.
DR   RefSeq; YP_762369.1; NC_008361.1.
DR   SMR; Q0E587; -.
DR   GeneID; 4306181; -.
DR   KEGG; vg:4306181; -.
DR   Proteomes; UP000008030; Genome.
DR   GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001818; Pept_M10_metallopeptidase.
DR   InterPro; IPR021190; Pept_M10A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   Pfam; PF00413; Peptidase_M10; 1.
DR   PRINTS; PR00138; MATRIXIN.
DR   SMART; SM00235; ZnMc; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Signal; Zinc.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..386
FT                   /note="Putative matrix metalloproteinase"
FT                   /id="PRO_0000330607"
FT   REGION          235..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        14
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   386 AA;  44456 MW;  070F9DE23912AC7D CRC64;
     MPTAHFQHSI RYLNVTNMLI FSIISFLLIY QTNSVVTLSR IDPAGAVDMG FVDVSYNNFT
     IQSPIHVPDD GTITWCVSKI NCKYDYDEVV GVTAAAFDVW SMTGLVFKPT SRCDRAHIRI
     SFKRRYHGDS DFDGEGGLLA HAFLPNQGAL SGDIHMDNDE TFAFSFNDAD YEGDNAPTSY
     FWTVLHEIGH TLGLQHSSSK QAIMYGFYVK RSFNNGAVTL STDDMNGINE LYHSNEQSTH
     QSTRHRPHRR PSPDGSCRDE RVLRIRRCRR RDRRRRRPKE SGELVLCRSV RCHRVHSRRA
     DHLRRQLHME TRSKRTALRR LSIANDDCVG FTTRFRGYIG VRMDGVHRSR HRQRSASVRR
     NSLPAQCNFR TKRHLSRSLT TTLCTR