165R_IIV6
ID 165R_IIV6 Reviewed; 264 AA.
AC O55761;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Putative metalloproteinase 165R;
DE EC=3.4.24.-;
GN ORFNames=IIV6-165R;
OS Invertebrate iridescent virus 6 (IIV-6) (Chilo iridescent virus).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Iridoviridae; Betairidovirinae; Iridovirus.
OX NCBI_TaxID=176652;
OH NCBI_TaxID=6997; Acheta domesticus (House cricket).
OH NCBI_TaxID=168631; Chilo suppressalis (Asiatic rice borer moth).
OH NCBI_TaxID=6999; Gryllus bimaculatus (Two-spotted cricket).
OH NCBI_TaxID=58607; Gryllus campestris.
OH NCBI_TaxID=7108; Spodoptera frugiperda (Fall armyworm).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11448171; DOI=10.1006/viro.2001.0963;
RA Jakob N.J., Mueller K., Bahr U., Darai G.;
RT "Analysis of the first complete DNA sequence of an invertebrate iridovirus:
RT coding strategy of the genome of Chilo iridescent virus.";
RL Virology 286:182-196(2001).
RN [2]
RP GENOME REANNOTATION.
RX PubMed=17239238; DOI=10.1186/1743-422x-4-11;
RA Eaton H.E., Metcalf J., Penny E., Tcherepanov V., Upton C., Brunetti C.R.;
RT "Comparative genomic analysis of the family Iridoviridae: re-annotating and
RT defining the core set of iridovirus genes.";
RL Virol. J. 4:11-11(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; AF303741; AAB94472.1; -; Genomic_DNA.
DR PIR; T03174; T03174.
DR RefSeq; NP_149628.1; NC_003038.1.
DR SMR; O55761; -.
DR GeneID; 1733354; -.
DR KEGG; vg:1733354; -.
DR Proteomes; UP000001359; 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; -; 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; 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 Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..264
FT /note="Putative metalloproteinase 165R"
FT /id="PRO_0000377912"
FT REGION 176..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 264 AA; 30080 MW; 8886A8896F8D3AFE CRC64;
MKINTTDVRT AIYHSLQQWQ SVSLLTFKEE YYDENADIKV SFVKGKHNDG WDFDGKGRIL
AHAFFPSGSM RGVVHLDYDE DWDFASLKQV LLHELGHTFG LGHSSDNKSI MFPWNSSSVD
NVNQDDKNGI EWLYGLKNKW AKLSPPVTKP PVTKPPVTKP ILTTVPRFPV PTTQVPIIQP
RFGNPTTHSP TTRHPLQKIP IQPRFGHSNP PIRYNPPIRY NPKHPLSPPF KSIPNSLLNV
VNSSITNLYV YFPNTWNSSI IKFN