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G1_VACCC
ID   G1_VACCC                Reviewed;         591 AA.
AC   P21022;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Metalloendopeptidase G1;
DE            EC=3.4.24.-;
GN   ORFNames=G1L;
OS   Vaccinia virus (strain Copenhagen) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10249;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "The complete DNA sequence of vaccinia virus.";
RL   Virology 179:247-266(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL   Virology 179:517-563(1990).
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; M35027; AAA48065.1; -; Genomic_DNA.
DR   PIR; F42511; F42511.
DR   SMR; P21022; -.
DR   MEROPS; M44.001; -.
DR   Proteomes; UP000008269; 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   Virion; Zinc.
FT   CHAIN           1..591
FT                   /note="Metalloendopeptidase G1"
FT                   /id="PRO_0000218444"
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"
SQ   SEQUENCE   591 AA;  67911 MW;  B81BEE410B8DFC0C 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 AILQISQCQS 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
 
 
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