ID   MP44_VACCA              Reviewed;         591 AA.
AC   P68492; O57194; Q6J3G0;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Metalloendopeptidase G1;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=MVA070L, ACAM3000_MVA_070;
OS   Vaccinia virus (strain Ankara) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=126794;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA   Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT   "The complete genomic sequence of the modified vaccinia Ankara strain:
RT   comparison with other orthopoxviruses.";
RL   Virology 244:365-396(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Acambis 3000;
RA   Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J.,
RA   Khristova M., Wohlhueter R.M.;
RL   Submitted (APR-2004) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U94848; AAB96440.1; -; Genomic_DNA.
DR   EMBL; AY603355; AAT10468.1; -; Genomic_DNA.
DR   PIR; T37346; T37346.
DR   SMR; P68492; -.
DR   MEROPS; M44.001; -.
DR   Proteomes; UP000159908; Genome.
DR   Proteomes; UP000172909; 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; Zinc.
FT   CHAIN           1..591
FT                   /note="Metalloendopeptidase G1"
FT                   /id="PRO_0000218443"
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   591 AA;  67980 MW;  085EEE04FE3DFCBC CRC64;
     MIVLPNKVRI FINDRMKKDI YLGISNFGFE NDIDEILGIA HLLEHLLISF DSTNFLANAS
     TSRSYMSFWC KSINSATESD AIRTLVSWFF SNGKLKDNFS LSSIRFHIKE LENEYYFRNE
     VFHCMDILTF LSGGDLYNGG RIDMIDNLNI VRDMLVNRMQ RISGSNIVIF VKRLGPGTLD
     FFKQTFGSLP ACPEIIPSSI PVSTNGKIVM TPSPFYTVMV KINPTLDNIL GILYLYETYH
     LIDYETIGNQ LYLTVSFIDE TEYESFLRGE AILQISQCQR INMNYSDDYM MNIYLNFPWL
     SHDLYDYITR INDDSKSILI SLTNEIYASI INRDIIVIYP NFSKAMCNTR DTQQHPIVVL
     DATNDGLIKK PYRSIPLMKR LTSNEIFIRY GDASLMDMIT LSLSKQDISL KRNAEGIRVK
     HSFSADDIQA IMESDSFLKY SRSKPAAMYQ YIFLSFFASG NSIDDILANR DSTLEFSKRT
     KSKILFGRNT RYDVTAKSSF VCGIVRGKSL DKTSLVEMMW DLKKKGLIYS MEFTNLLSKN
     TFYLFTFTIY TDEVYDYLNT NKLFSAKCLV VSTKGDVENF SSLKKDVVIR V