ID   MP44_MCV1               Reviewed;         593 AA.
AC   Q98224; O11329;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Probable metalloendopeptidase G1-type;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=MC056L; ORFNames=B2'-17R;
OS   Molluscum contagiosum virus subtype 1 (MOCV) (MCVI).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Molluscipoxvirus.
OX   NCBI_TaxID=10280;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8670425; DOI=10.1126/science.273.5276.813;
RA   Senkevich T.G., Bugert J.J., Sisler J.R., Koonin E.V., Darai G., Moss B.;
RT   "Genome sequence of a human tumorigenic poxvirus: prediction of specific
RT   host response-evasion genes.";
RL   Science 273:813-816(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 206-392.
RA   Moratilla M., Agromayor M., Nunez A., Funes J.M., Varas A.J.,
RA   Lopez-Estebaranz J.L., Esteban M., Martin-Gallardo A.;
RT   "A random DNA sequencing, computer-based approach for the generation of a
RT   gene map of Molluscum contagiosum virus.";
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Seems to be involved in viral proteins maturation by cleavage
CC       at Ala-Gly-|-Xaa motifs. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion. {ECO:0000305};
CC   -!- SIMILARITY: Belongs to the peptidase M44 family. {ECO:0000305}.
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DR   EMBL; U60315; AAC55184.1; -; Genomic_DNA.
DR   EMBL; U86909; AAB57961.1; -; Genomic_DNA.
DR   PIR; T30658; T30658.
DR   RefSeq; NP_044007.1; NC_001731.1.
DR   PRIDE; Q98224; -.
DR   GeneID; 1487075; -.
DR   KEGG; vg:1487075; -.
DR   Proteomes; UP000000869; Genome.
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   GO; GO:0019058; P:viral life cycle; IEA:InterPro.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR005072; Peptidase_M44.
DR   Pfam; PF03410; Peptidase_M44; 1.
DR   PIRSF; PIRSF015679; Peptidase_M44; 1.
DR   SUPFAM; SSF63411; SSF63411; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN           1..593
FT                   /note="Probable metalloendopeptidase G1-type"
FT                   /id="PRO_0000218449"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000255"
FT   BINDING         41
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
FT   BINDING         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   593 AA;  68420 MW;  142C620E1AB0C61E CRC64;
     MILLENGVRV FPKPGMGKDI YIGLANFGFE NDVPELLGVA HLLEHILISF DYTRFVANAS
     TARTYMSFWC RALRAEDYLA ALETAVSWFF ARGALRTDFS RVRIRNYVRE LENEYYFRNE
     VFHCMDILTF LGGGDLYNGG RLSMLEQLDA VRELLGKRMR RLAGPNVVIF VRELSPAALA
     LLERSFGTLP RFPSTIPATR LGSIHNKAVL VPAPFYALLI QVDNTVENVL AVICLAESYH
     FVDYETLGER LYVSFAFVHE QDCEAFLRNV GELRFEPAPR VELNYSDDYV MNLYVNFPWL
     QHDLADYLYT LNADCVPLLR GLEENLRRSV RERQLVVVYP SFSPSLFNSR DRQDHRLLVL
     DVDLARSAGP ARVPRTFRRQ PRAEVFVRYG DPALLDYVAF ALARPRAAAL RRLPRGVRLA
     HGFSHADMHE IMASETFIKY SRSRPAALFQ YIFLAFFATG RSIAEILERR EALVSFDARR
     CVNRLVFAKR ARYDVVTKSS FVCGVLRGPR LSEAALTRAM WELKRKGLLY SLEHTRMHAK
     HTFYVFAFSI YPEQVYRYFA RWQLVSKHCC VVSMRGERED YSALRKEVVV NFV