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