ID   W8QE20_9VIRU            Unreviewed;       366 AA.
AC   W8QE20;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Membrane-type matrix metallopeptidase-1 {ECO:0000313|EMBL:AHL67525.1};
GN   ORFNames=AMIV_027 {ECO:0000313|EMBL:AHL67525.1};
OS   Anopheles minimus iridovirus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Iridoviridae; Betairidovirinae; Chloriridovirus.
OX   NCBI_TaxID=1465751 {ECO:0000313|EMBL:AHL67525.1, ECO:0000313|Proteomes:UP000110868};
RN   [1] {ECO:0000313|EMBL:AHL67525.1, ECO:0000313|Proteomes:UP000110868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMIV {ECO:0000313|EMBL:AHL67525.1};
RA   Tong Y., Zhang J., Huang Y., Li S., Pei G., Zhang Z., Mi Z., An X.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; KF938901; AHL67525.1; -; Genomic_DNA.
DR   RefSeq; YP_009021109.1; NC_023848.1.
DR   GeneID; 18938188; -.
DR   KEGG; vg:18938188; -.
DR   OrthoDB; 15321at10239; -.
DR   Proteomes; UP000110868; 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   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:SF291; MATRIX METALLOPROTEINASE 1, ISOFORM C-RELATED; 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; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
DR   PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001191-2};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000110868};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001191-2};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          104..275
FT                   /note="Peptidase metallopeptidase"
FT                   /evidence="ECO:0000259|SMART:SM00235"
FT   REGION          292..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        233
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001191-1"
FT   BINDING         232
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001191-2"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001191-2"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001191-2"
SQ   SEQUENCE   366 AA;  41839 MW;  19B519F704BC213E CRC64;
     MELHTFLYIM FAAMKLCVSA PLRQSENVLS ALVKYGYIHV QNENEVGNMI HPDERVKMGL
     RKMQKFAGIE TTGVLDQETK NLLNSPRCGV PDLVRTRSKR FAIQGSKWKY VDKETNETVV
     YWYIDLDNYA EIDTRLFKQE IQNIFYHAFK KWSLKTLIRF EEVDSAKLSN ITIQFLRGKH
     DDGYDFDFQG GVLAHAFYPG TGNGGDVHFD LAEKWTTYDE EDSTSLLHVA VHEIGHSLGL
     MHSSLNTSIM FPWYKPQSFE LTEDDHIGLN SIYGVRPEYR FGLLEPKYRI YKKTPSTPST
     PSTPSTPSTS TPSTPSTSTP STPSTPVETP LPRVAPRIRP RYKKVDRLFI QNSKVYIYPK
     SATVTL
//