ID   G1_VARV                 Reviewed;         591 AA.
AC   P0DOT0; P32991; Q85379; Q89209;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Metalloendopeptidase G1;
DE            EC=3.4.24.-;
GN   ORFNames=G1L;
OS   Variola virus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=10255;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bangladesh-1975;
RX   PubMed=8264798; DOI=10.1038/366748a0;
RA   Massung R.F., Esposito J.J., Liu L.I., Qi J., Utterback T.R., Knight J.C.,
RA   Aubin L., Yuran T.E., Parsons J.M., Loparev V.N., Selivanov N.A.,
RA   Cavallaro K.F., Kerlavage A.R., Mahy B.W.J., Venter J.C.;
RT   "Potential virulence determinants in terminal regions of variola smallpox
RT   virus genome.";
RL   Nature 366:748-751(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Garcia-1966;
RX   PubMed=10639322; DOI=10.1006/viro.1999.0086;
RA   Shchelkunov S.N., Totmenin A.V., Loparev V.N., Safronov P.F., Gutorov V.V.,
RA   Chizhikov V.E., Knight J.C., Parsons J.M., Massung R.F., Esposito J.J.;
RT   "Alastrim smallpox variola minor virus genome DNA sequences.";
RL   Virology 266:361-386(2000).
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 (By
CC       similarity). {ECO:0000250}.
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:0000250}. Note=Localizes to the
CC       virion core. {ECO:0000250}.
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; L22579; AAA60811.1; -; Genomic_DNA.
DR   EMBL; X76267; CAA53868.1; -; Genomic_DNA.
DR   EMBL; Y16780; CAB54663.1; -; Genomic_DNA.
DR   PIR; E72158; E72158.
DR   PIR; T28501; T28501.
DR   SMR; P0DOT0; -.
DR   Proteomes; UP000111493; Genome.
DR   Proteomes; UP000119805; 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; Virion; Zinc.
FT   CHAIN           1..591
FT                   /note="Metalloendopeptidase G1"
FT                   /id="PRO_0000448118"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000250"
FT   BINDING         41
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
FT   VARIANT         182
FT                   /note="F -> L (in strain: Garcia-1966)"
FT   VARIANT         490
FT                   /note="A -> T (in strain: Garcia-1966)"
FT   VARIANT         565
FT                   /note="P -> S (in strain: Garcia-1966)"
SQ   SEQUENCE   591 AA;  68047 MW;  C1E710625B3CF414 CRC64;
     MIVLPNKVRI FINDRMKKDI YLGISNFGFE NDIDEILGIA HLLEHLLISF DSTIFLANAS
     TSRSYMSFWC KSINSATESD AIRTLVSWFF SNGKLKDNFS LSSIRFHIKE LENEYYFRNE
     VFHCMDILTF LSGGDLYNGG RIDMIDNLNI VRDMLVNRMQ RISGSNIVIF VKRLGPGTLD
     FFNQTFGSLP ACPEIIPSSI PVSTNGKIVM TPSPFYTVMV KINPTLDNIL GILYLYETYH
     LIDYETIGNQ LYLTVSFIDE TEYESFLRGE AILQISQCQR INMNYSDDYM MNIYLNFPWL
     SHDLYDYITR INDDSKSILI SLTNEIYTSI INRDIIVIYP NFSKAMCNTR DTQQHPIVVL
     DATNDGLIKK PYRSIPLMKR LTSNEIFIRY GDASLMDMIT LSLSKQDISL KRNAEGIRVK
     HSFSADDIQA IMESDSFLKY SRSKPAAMYQ YIFLSFFASG NSIDDILTNR DSTLEFSKKT
     KSKILFGRNA RYDVTTKSSF VCGIVRGKLL DKTSLVEMMW DLKKKGLIYS MEFTNLLSKN
     TFYLFTFTIY TDEVYDYLNT NKLFPAKCLV ISTKGDVENF SSLKKDVVIR V