G5_VARV
ID G5_VARV Reviewed; 434 AA.
AC P0DSS6; P32995;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Putative nuclease G5;
DE EC=3.1.-.-;
GN ORFNames=G5R;
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).
CC -!- FUNCTION: Putative nuclease that seems to be required for double-strand
CC break repair, homologous recombination, and production of full-length
CC viral genomic DNA. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. They probably participate in
CC the reaction catalyzed by the enzyme. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Note=Present in the virion
CC core. {ECO:0000250}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
CC subfamily. {ECO:0000305}.
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DR EMBL; L22579; AAA60815.1; -; Genomic_DNA.
DR PIR; T28505; T28505.
DR RefSeq; NP_042111.1; NC_001611.1.
DR GeneID; 1486433; -.
DR KEGG; vg:1486433; -.
DR Proteomes; UP000119805; Genome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR InterPro; IPR007678; Poxvirus_G5.
DR Pfam; PF04599; Pox_G5; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; Early protein; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Virion.
FT CHAIN 1..434
FT /note="Putative nuclease G5"
FT /id="PRO_0000448193"
FT BINDING 33
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 434 AA; 49884 MW; DD5214A9C9810ACD CRC64;
MGIKNLKSLL LENKSLTILD DNLYKVYNGI FVDTMSIYIA VANCVRNLEE LTTVFIKYVN
GWVKKGGHVT LFIDRGSIKI KQNVRDKRRK YSKSTKDRKM LELEKCTSKI QNVTGFMEEE
IKAEIQLKID KLTFQIYLSD SDNIKISLNE ILTHFNNNEN VTLFYCDERD AEFVMCLEAK
TYFFTTGEWP LIISTDQDTM LFASVDNHPK MIKNLTQLFK FVPSAEDNYL AKLTALVNGC
DFFPGLYGAS ITPTNLNKIQ LFSDFTINNI VTSLAIKNYY RKTNSTVDVR NIVTFINDYA
NLDDVYSYIP PCQCTVQEFI FSALDEKWND FKSSYLETVP LPCQLMYALE PRKEIDVSEV
KTLSSYIDFE NTKSDIDVIK SISSIFGYSN ENCNTIVFGI YKDNLLLSIN SSFYFNNSLL
ITNTKSDNII NIGY