END7_BPT4
ID END7_BPT4 Reviewed; 157 AA.
AC P13340; Q38426; Q9T0V4;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Recombination endonuclease VII;
DE Short=Endo VII;
DE EC=3.1.-.-;
DE AltName: Full=Gene product 49;
DE Short=gp49;
GN Name=49;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C;
RX PubMed=3575111; DOI=10.1093/nar/15.8.3632;
RA Tomaschewski J., Rueger W.;
RT "Nucleotide sequence and primary structures of gene products coded for by
RT the T4 genome between map positions 48.266 kb and 39.166 kb.";
RL Nucleic Acids Res. 15:3632-3633(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE INITIATION.
RX PubMed=2974005; DOI=10.1093/genetics/120.2.329;
RA Barth K.A., Powell D., Trupin M., Mosig G.;
RT "Regulation of two nested proteins from gene 49 (recombination endonuclease
RT VII) and of a lambda RexA-like protein of bacteriophage T4.";
RL Genetics 120:329-343(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [4]
RP CHARACTERIZATION.
RX PubMed=2269300; DOI=10.1111/j.1432-1033.1990.tb19469.x;
RA Kosak H.G., Kemper B.W.;
RT "Large-scale preparation of T4 endonuclease VII from over-expressing
RT bacteria.";
RL Eur. J. Biochem. 194:779-784(1990).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=10075917; DOI=10.1093/emboj/18.6.1447;
RA Raaijmakers H., Vix O., Toro I., Golz S., Kemper B., Suck D.;
RT "X-ray structure of T4 endonuclease VII: a DNA junction resolvase with a
RT novel fold and unusual domain-swapped dimer architecture.";
RL EMBO J. 18:1447-1458(1999).
CC -!- FUNCTION: Cleaves DNA cruciform and Y-structures as well as
CC heteroduplex loops. Resolves Holliday junctions, recognizes a broad
CC spectrum of DNA substrates ranging from branched DNAs to single base
CC mismatches.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- SUBUNIT: Homodimer.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Long;
CC IsoId=P13340-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P13340-2; Sequence=VSP_018678, VSP_018986;
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DR EMBL; X12629; CAA31148.1; -; Genomic_DNA.
DR EMBL; X12629; CAA31149.1; -; Genomic_DNA.
DR EMBL; Y00122; CAA68307.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42477.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42687.2; -; Genomic_DNA.
DR PIR; S01906; ZNBPT9.
DR RefSeq; NP_049692.1; NC_000866.4. [P13340-1]
DR RefSeq; NP_049693.2; NC_000866.4. [P13340-2]
DR PDB; 1E7D; X-ray; 2.80 A; A/B=1-157.
DR PDB; 1E7L; X-ray; 1.32 A; A/B=1-157.
DR PDB; 1EN7; X-ray; 2.40 A; A/B=1-157.
DR PDB; 2QNC; X-ray; 3.10 A; A/B=1-157.
DR PDB; 2QNF; X-ray; 3.00 A; A/B=1-157.
DR PDBsum; 1E7D; -.
DR PDBsum; 1E7L; -.
DR PDBsum; 1EN7; -.
DR PDBsum; 2QNC; -.
DR PDBsum; 2QNF; -.
DR SMR; P13340; -.
DR DIP; DIP-60245N; -.
DR PRIDE; P13340; -.
DR GeneID; 1258702; -.
DR GeneID; 1258772; -.
DR KEGG; vg:1258702; -.
DR KEGG; vg:1258772; -.
DR BRENDA; 3.1.21.10; 732.
DR EvolutionaryTrace; P13340; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0004519; F:endonuclease activity; IDA:CACAO.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1800.10; -; 1.
DR InterPro; IPR004211; Endonuclease_7.
DR InterPro; IPR038563; Endonuclease_7_sf.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR036309; T4_recomb_endonuclease_dim_sf.
DR InterPro; IPR015208; T4_recomb_endonuclease_dimer.
DR Pfam; PF09124; Endonuc-dimeris; 1.
DR Pfam; PF02945; Endonuclease_7; 1.
DR SUPFAM; SSF54060; SSF54060; 1.
DR SUPFAM; SSF68918; SSF68918; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Calcium; Endonuclease; Hydrolase;
KW Metal-binding; Nuclease; Reference proteome; Zinc.
FT CHAIN 1..157
FT /note="Recombination endonuclease VII"
FT /id="PRO_0000003326"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_018678"
FT VAR_SEQ 53
FT /note="V -> M (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_018986"
FT HELIX 6..18
FT /evidence="ECO:0007829|PDB:1E7L"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:1E7L"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1E7L"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1E7L"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1E7L"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2QNF"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:1E7L"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:1E7L"
FT HELIX 59..74
FT /evidence="ECO:0007829|PDB:1E7L"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1E7L"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1E7L"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:1E7L"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:1E7L"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:1E7L"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1E7D"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:1E7L"
SQ SEQUENCE 157 AA; 18144 MW; 86233D2A7FC0F9A8 CRC64;
MLLTGKLYKE EKQKFYDAQN GKCLICQREL NPDVQANHLD HDHELNGPKA GKVRGLLCNL
CNAAEGQMKH KFNRSGLKGQ GVDYLEWLEN LLTYLKSDYT QNNIHPNFVG DKSKEFSRLG
KEEMMAEMLQ RGFEYNESDT KTQLIASFKK QLRKSLK
