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 27-MAR-2024, entry version 74.
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 OrthoDB; 4353at10239; -.
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; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.110.10.10; Hemopexin-like domain; 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 PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR PANTHER; PTHR10201:SF272; ZNMC DOMAIN-CONTAINING PROTEIN; 1.
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; Hemopexin-like domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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
//
