ID   MMP_HVAVE               Reviewed;         474 AA.
AC   A4KX75;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, 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=ORF20;
OS   Heliothis virescens ascovirus 3e (HvAV-3e).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Ascoviridae; Ascovirus.
OX   NCBI_TaxID=260797;
OH   NCBI_TaxID=7100; Noctuidae (owlet moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17374755; DOI=10.1099/vir.0.82651-0;
RA   Asgari S., Davis J., Wood D., Wilson P., McGrath A.;
RT   "Sequence and organization of the Heliothis virescens ascovirus genome.";
RL   J. Gen. Virol. 88:1120-1132(2007).
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; EF133465; ABO37206.1; -; Genomic_DNA.
DR   RefSeq; YP_001110872.1; NC_009233.1.
DR   SMR; A4KX75; -.
DR   GeneID; 5076115; -.
DR   KEGG; vg:5076115; -.
DR   Proteomes; UP000001324; 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; 2.110.10.10; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR036375; Hemopexin-like_dom_sf.
DR   InterPro; IPR018487; Hemopexin-like_repeat.
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   SUPFAM; SSF50923; SSF50923; 1.
DR   PROSITE; PS51642; HEMOPEXIN_2; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Signal; Zinc; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..474
FT                   /note="Putative matrix metalloproteinase"
FT                   /id="PRO_0000330606"
FT   REPEAT          299..344
FT                   /note="Hemopexin"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         189
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         193
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         199
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   474 AA;  53655 MW;  D581E4789E5FB29D CRC64;
     MIIYFAVITC SLKLCRSYYK MLLNVSHTIQ CVFSRMSWYT LAVILSTLVT IHASQGPEKF
     TLATAIVLKR GEDITWSVSR ENLKYNYRTV VDTTSKAFAV WHTAGLNFRF VYNYSEAMIR
     ISFKRRFHGE IGYDFDGLGS LLAHAYLPNQ GDLSSEIHLD NDEIFSFSMK DSDYEGDNAP
     TSYFWTVLHE IGHSLGVQHS ASPSSIMYGW YKSRSFGNGT IVLPKDDANA IHQLYFSNTK
     QYAAIPKFEK NKVVTTTPVP PADRSESTTN TTITTCFSFD SLSEIKHDAT KDSISAYCAG
     VYDAISYVRG DLYVFVGDLH WRFDTSGMLH NGYPQPTGAT WRLPSGSQVN SVFEWMQYIV
     IQTGKRYNLF VGTDFVRSVN FKVAPSITFA SNNRVYAAFL GKLKDITGHL LRRKNLRWRY
     LPPIQLLQNE LRAATDILVA SNGMYIFKSG VHGVVVNGVV EHYKLNKGVW SNCR