ID   MMP_TNAVC               Reviewed;         501 AA.
AC   Q06VC5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Putative matrix metalloproteinase;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   ORFNames=ORF158;
OS   Trichoplusia ni ascovirus 2c (TnAV-2c).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Ascoviridae; Ascovirus.
OX   NCBI_TaxID=328615;
OH   NCBI_TaxID=7100; Noctuidae (owlet moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16876847; DOI=10.1016/j.virol.2006.06.029;
RA   Wang L., Xue J., Seaborn C.P., Arif B.M., Cheng X.W.;
RT   "Sequence and organization of the Trichoplusia ni ascovirus 2c
RT   (Ascoviridae) genome.";
RL   Virology 354:167-177(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; DQ517337; ABF70673.1; -; Genomic_DNA.
DR   RefSeq; YP_803380.1; NC_008518.1.
DR   GeneID; 5141669; -.
DR   KEGG; vg:5141669; -.
DR   Proteomes; UP000001323; 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   CDD; cd04278; ZnMc_MMP; 1.
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; IPR033739; M10A_MMP.
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; PF00045; Hemopexin; 1.
DR   Pfam; PF00413; Peptidase_M10; 1.
DR   PIRSF; PIRSF001191; Peptidase_M10A_matrix; 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   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Signal; Zinc.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..501
FT                   /note="Putative matrix metalloproteinase"
FT                   /id="PRO_0000330608"
FT   REPEAT          311..356
FT                   /note="Hemopexin"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
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   CARBOHYD        48
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"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        379
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   501 AA;  58710 MW;  40911D419E9D6446 CRC64;
     MMPQYERKQI IIHISCVIIC VVVTLTLFHV FWNDNYIAVD VNYDVPYNFS VSPDFGFNTT
     NITWSLKPYY KYDINDLMNT ANSVFKIWSR TGLNFTYIKN VDEAMVRIYF YRQDHNDSFP
     FDGKGKILGH AFYPNRHRIN RGLAGEVHID ADEQFYFNDK LENMSEYDDS INLHAILLHE
     VGHAIGLLHS ANKSSIMYPY YGGSKLGVDD FNGIQQIYFA NKYKHNKIFT YNKYHKLETT
     SSSTPSYYGN RDRYPINKKR SLSSVFNITT TTVKPSYDKN NTFTPQKICF NITSSYKTHN
     TKLTAIRKYC TGHIDTISVI RGELYIFVDE YHWRFRSNGL LYSGYPLKTT HSWSVPIIGR
     FKVTSAFETL TGDIVIGVNY TTFYYFDRMS MQLYRMQKLP LHLLPRCRST KKTIVFSIDS
     HLYALCDRII REIDFNSLRM KRMKTKRSML GFPLVSNLIT VLDHDGIYLF RNDNTYAEVI
     RSRVDSSSSY FKNNTDKWTI C