ID   095L_IIV3               Reviewed;         363 AA.
AC   Q196W5;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Probable matrix metalloproteinase 095L;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   ORFNames=IIV3-095L;
OS   Invertebrate iridescent virus 3 (IIV-3) (Mosquito iridescent virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Iridoviridae; Betairidovirinae; Chloriridovirus.
OX   NCBI_TaxID=345201;
OH   NCBI_TaxID=7163; Aedes vexans (Inland floodwater mosquito) (Culex vexans).
OH   NCBI_TaxID=42431; Culex territans.
OH   NCBI_TaxID=332058; Culiseta annulata.
OH   NCBI_TaxID=310513; Ochlerotatus sollicitans (eastern saltmarsh mosquito).
OH   NCBI_TaxID=329105; Ochlerotatus taeniorhynchus (Black salt marsh mosquito) (Aedes taeniorhynchus).
OH   NCBI_TaxID=7183; Psorophora ferox.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16912294; DOI=10.1128/jvi.00464-06;
RA   Delhon G., Tulman E.R., Afonso C.L., Lu Z., Becnel J.J., Moser B.A.,
RA   Kutish G.F., Rock D.L.;
RT   "Genome of invertebrate iridescent virus type 3 (mosquito iridescent
RT   virus).";
RL   J. Virol. 80:8439-8449(2006).
CC   -!- FUNCTION: Probable endopeptidase.
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:0000305}.
CC   -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC       binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC       dissociation of the cysteine from the zinc ion upon the activation-
CC       peptide release activates the enzyme.
CC   -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR   EMBL; DQ643392; ABF82125.1; -; Genomic_DNA.
DR   RefSeq; YP_654667.1; NC_008187.1.
DR   SMR; Q196W5; -.
DR   SwissPalm; Q196W5; -.
DR   GeneID; 4156239; -.
DR   KEGG; vg:4156239; -.
DR   OrthoDB; 15321at10239; -.
DR   Proteomes; UP000001358; Genome.
DR   GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   InterPro; IPR033739; M10A_MMP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001818; Pept_M10_metallopeptidase.
DR   InterPro; IPR021190; Pept_M10A.
DR   InterPro; IPR021158; Pept_M10A_Zn_BS.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR   PANTHER; PTHR10201:SF272; ZNMC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00413; Peptidase_M10; 1.
DR   PRINTS; PR00138; MATRIXIN.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
DR   PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..126
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000377512"
FT   CHAIN           127..363
FT                   /note="Probable matrix metalloproteinase 095L"
FT                   /id="PRO_0000377513"
FT   MOTIF           117..124
FT                   /note="Cysteine switch"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        276
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /note="in inhibited form"
FT                   /evidence="ECO:0000250"
FT   BINDING         275
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         279
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         285
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   363 AA;  40667 MW;  BFE243A6AF604F1A CRC64;
     MSVDSFTSRL AVVMTAVVLV WWAQALPVPS PRRGESDCDA ACRKFLLQYG YLDLGEENCT
     EVDSNRKLCS VDDELVGVPR PLARVDLAAG VSHLQTMAGL EPTGRIDAST ARLFTSPRCG
     VPDVSKYIVA AGRRRRTRRE SVIVCTTRWT TTKSNSNETL VKWWLDQSSM QWLNSTLNWV
     SLTNVLHHSF WKWSKESMLA FQQVSLERDA QIVVRFENGS HGDGWDFDGP GNVLAHAFQP
     GQSLGGDIHL DAAEPWTIYD IDGHDGNSIL HVVLHEIGHA LGLEHSRDPT SIMYAWYTPF
     KYDLGPEDVS AVAGLYGAKP ASSVAAWNPK IQKFYWDRHV RNDLLPLLER DLDAEEEDSD
     EVR
//