ID   G1_VACCW                Reviewed;         591 AA.
AC   P16713; Q76ZU4;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Metalloendopeptidase G1;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=VACWR078; ORFNames=G1L;
OS   Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS   WR)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10254;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1994576; DOI=10.1016/0042-6822(91)90491-s;
RA   Fathi Z., Condit R.C.;
RT   "Genetic and molecular biological characterization of a vaccinia virus
RT   temperature-sensitive complementation group affecting a virion component.";
RL   Virology 181:258-272(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Rozanov D.V., Strongin A.Y.;
RT   "Vaccinia virus strain WR metalloproteinase GIL.";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA   Wohlhueter R.;
RT   "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT   redundancy and an error rate of 0.16/10kb.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   CHARACTERIZATION, AND MUTAGENESIS OF 41-HIS--HIS-45; GLU-112 AND GLU-114.
RX   PubMed=7933150; DOI=10.1128/jvi.68.11.7603-7608.1994;
RA   Whitehead S.S., Hruby D.E.;
RT   "A transcriptionally controlled trans-processing assay: putative
RT   identification of a vaccinia virus-encoded proteinase which cleaves
RT   precursor protein P25K.";
RL   J. Virol. 68:7603-7608(1994).
RN   [5]
RP   FUNCTION, MUTAGENESIS OF HIS-41; GLU-44 AND HIS-45, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=15194761; DOI=10.1128/jvi.78.13.6855-6863.2004;
RA   Ansarah-Sobrinho C., Moss B.;
RT   "Vaccinia virus G1 protein, a predicted metalloprotease, is essential for
RT   morphogenesis of infectious virions but not for cleavage of major core
RT   proteins.";
RL   J. Virol. 78:6855-6863(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=15331728; DOI=10.1128/jvi.78.18.9947-9953.2004;
RA   Hedengren-Olcott M., Byrd C.M., Watson J., Hruby D.E.;
RT   "The vaccinia virus G1L putative metalloproteinase is essential for viral
RT   replication in vivo.";
RL   J. Virol. 78:9947-9953(2004).
RN   [7]
RP   ACTIVE SITES, AND MUTAGENESIS OF GLU-35; HIS-41; GLU-44; HIS-45; GLU-110;
RP   GLU-112; GLU-114 AND GLU-120.
RX   PubMed=16504157; DOI=10.1186/1743-422x-3-7;
RA   Honeychurch K.M., Byrd C.M., Hruby D.E.;
RT   "Mutational analysis of the potential catalytic residues of the VV G1L
RT   metalloproteinase.";
RL   Virol. J. 3:7-7(2006).
CC   -!- FUNCTION: Probably involved in maturation of some viral proteins by
CC       processing them preferentially at Ala-Gly-|-Ser/Thr/Lys motifs. Does
CC       not seem to be responsible for the cleavage of major core proteins.
CC       {ECO:0000269|PubMed:15194761, ECO:0000269|PubMed:15331728}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion. {ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:15194761}.
CC       Note=Localizes to the virion core.
CC   -!- PTM: Undergoes proteolytic processing during the course of infection.
CC       May be cleaved into 46 kDa and 22 kDa products (Potential).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M44 family. {ECO:0000305}.
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DR   EMBL; J03399; AAB59811.1; -; Genomic_DNA.
DR   EMBL; AY497360; AAR88656.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89357.1; -; Genomic_DNA.
DR   RefSeq; YP_232960.1; NC_006998.1.
DR   SMR; P16713; -.
DR   MEROPS; M44.001; -.
DR   DNASU; 3707534; -.
DR   GeneID; 3707534; -.
DR   KEGG; vg:3707534; -.
DR   Proteomes; UP000000344; 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   1: Evidence at protein level;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Virion; Zinc.
FT   CHAIN           1..591
FT                   /note="Metalloendopeptidase G1"
FT                   /id="PRO_0000218446"
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"
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         35
FT                   /note="E->A: About 60% loss of processing activity."
FT                   /evidence="ECO:0000269|PubMed:16504157"
FT   MUTAGEN         41..45
FT                   /note="HLLEH->SLLED: Complete loss of processing activity."
FT                   /evidence="ECO:0000269|PubMed:7933150"
FT   MUTAGEN         41
FT                   /note="H->A: Complete loss of processing activity."
FT                   /evidence="ECO:0000269|PubMed:15194761,
FT                   ECO:0000269|PubMed:16504157"
FT   MUTAGEN         44
FT                   /note="E->A: Complete loss of processing activity."
FT                   /evidence="ECO:0000269|PubMed:15194761,
FT                   ECO:0000269|PubMed:16504157"
FT   MUTAGEN         45
FT                   /note="H->A: Complete loss of processing activity."
FT                   /evidence="ECO:0000269|PubMed:15194761,
FT                   ECO:0000269|PubMed:16504157"
FT   MUTAGEN         110
FT                   /note="E->A: Complete loss of processing activity."
FT                   /evidence="ECO:0000269|PubMed:16504157"
FT   MUTAGEN         112
FT                   /note="E->A: Complete loss of processing activity."
FT                   /evidence="ECO:0000269|PubMed:16504157,
FT                   ECO:0000269|PubMed:7933150"
FT   MUTAGEN         114
FT                   /note="E->A,D: Complete loss of processing activity."
FT                   /evidence="ECO:0000269|PubMed:16504157,
FT                   ECO:0000269|PubMed:7933150"
FT   MUTAGEN         120
FT                   /note="E->A: No effect on processing activity."
FT                   /evidence="ECO:0000269|PubMed:16504157"
SQ   SEQUENCE   591 AA;  68040 MW;  085EFA55BB3DFCBC 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 NKLFFAKCLV VSTKGDVENF SSLKKDVVIR V