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RUVC_ECOLI
ID   RUVC_ECOLI              Reviewed;         173 AA.
AC   P0A814; P24239;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Crossover junction endodeoxyribonuclease RuvC;
DE            EC=3.1.21.10;
DE   AltName: Full=Holliday junction nuclease RuvC;
DE   AltName: Full=Holliday junction resolvase RuvC;
GN   Name=ruvC; OrderedLocusNames=b1863, JW1852;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1657895; DOI=10.1128/jb.173.23.7711-7715.1991;
RA   Sharples G.J., Lloyd R.G.;
RT   "Resolution of Holliday junctions in Escherichia coli: identification of
RT   the ruvC gene product as a 19-kilodalton protein.";
RL   J. Bacteriol. 173:7711-7715(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1885548; DOI=10.1128/jb.173.18.5747-5753.1991;
RA   Takahagi M., Iwasaki H., Nakata A., Shinagawa H.;
RT   "Molecular analysis of the Escherichia coli ruvC gene, which encodes a
RT   Holliday junction-specific endonuclease.";
RL   J. Bacteriol. 173:5747-5753(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-42, AND FUNCTION.
RX   PubMed=1661673; DOI=10.1002/j.1460-2075.1991.tb05016.x;
RA   Iwasaki H., Takahagi M., Shiba T., Nakata A., Shinagawa H.;
RT   "Escherichia coli RuvC protein is an endonuclease that resolves the
RT   Holliday structure.";
RL   EMBO J. 10:4381-4389(1991).
RN   [7]
RP   PROTEIN SEQUENCE OF 2-25, AND FUNCTION.
RX   PubMed=1758493; DOI=10.1038/354506a0;
RA   Dunderdale H.J., Benson F.E., Parsons C.A., Sharples G.J., Lloyd R.G.,
RA   West S.C.;
RT   "Formation and resolution of recombination intermediates by E. coli RecA
RT   and RuvC proteins.";
RL   Nature 354:506-510(1991).
RN   [8]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=K12;
RX   PubMed=21219465; DOI=10.1111/j.1365-2958.2010.07465.x;
RA   Babu M., Beloglazova N., Flick R., Graham C., Skarina T., Nocek B.,
RA   Gagarinova A., Pogoutse O., Brown G., Binkowski A., Phanse S.,
RA   Joachimiak A., Koonin E.V., Savchenko A., Emili A., Greenblatt J.,
RA   Edwards A.M., Yakunin A.F.;
RT   "A dual function of the CRISPR-Cas system in bacterial antivirus immunity
RT   and DNA repair.";
RL   Mol. Microbiol. 79:484-502(2011).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=7923356; DOI=10.1016/0092-8674(94)90280-1;
RA   Ariyoshi M., Vassylyev D.G., Iwasaki H., Nakamura H., Shinagawa H.,
RA   Morikawa K.;
RT   "Atomic structure of the RuvC resolvase: a holliday junction-specific
RT   endonuclease from E. coli.";
RL   Cell 78:1063-1072(1994).
RN   [10]
RP   REVIEW.
RX   PubMed=9442895; DOI=10.1146/annurev.genet.31.1.213;
RA   West S.C.;
RT   "Processing of recombination intermediates by the RuvABC proteins.";
RL   Annu. Rev. Genet. 31:213-244(1997).
CC   -!- FUNCTION: Nuclease that resolves Holliday junction intermediates in
CC       genetic recombination. Cleaves the cruciform structure in supercoiled
CC       DNA by nicking to strands with the same polarity at sites symmetrically
CC       opposed at the junction in the homologous arms and leaves a 5'-terminal
CC       phosphate and a 3'-terminal hydroxyl group.
CC       {ECO:0000269|PubMed:1661673, ECO:0000269|PubMed:1758493}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage at a junction such as a reciprocal
CC         single-stranded crossover between two homologous DNA duplexes
CC         (Holliday junction).; EC=3.1.21.10;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- INTERACTION:
CC       P0A814; P0A809: ruvA; NbExp=4; IntAct=EBI-1123014, EBI-555119;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21219465}. Note=In
CC       15% of cell localizes to discrete nucleoid foci (probable DNA damage
CC       sites) upon treatment with mitomycin C (MMC) for 2 hours.
CC   -!- SIMILARITY: Belongs to the RuvC family. {ECO:0000305}.
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DR   EMBL; X59551; CAA42128.1; -; Genomic_DNA.
DR   EMBL; D10165; BAA01032.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74933.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15674.1; -; Genomic_DNA.
DR   PIR; D38113; D38113.
DR   RefSeq; NP_416377.1; NC_000913.3.
DR   RefSeq; WP_001295503.1; NZ_STEB01000009.1.
DR   PDB; 1HJR; X-ray; 2.50 A; A/B/C/D=2-159.
DR   PDBsum; 1HJR; -.
DR   AlphaFoldDB; P0A814; -.
DR   SMR; P0A814; -.
DR   BioGRID; 4263235; 96.
DR   ComplexPortal; CPX-5125; RuvABC Holliday junction resolvase complex.
DR   DIP; DIP-35952N; -.
DR   IntAct; P0A814; 5.
DR   STRING; 511145.b1863; -.
DR   PaxDb; P0A814; -.
DR   PRIDE; P0A814; -.
DR   EnsemblBacteria; AAC74933; AAC74933; b1863.
DR   EnsemblBacteria; BAA15674; BAA15674; BAA15674.
DR   GeneID; 66674246; -.
DR   GeneID; 946378; -.
DR   KEGG; ecj:JW1852; -.
DR   KEGG; eco:b1863; -.
DR   PATRIC; fig|1411691.4.peg.385; -.
DR   EchoBASE; EB0918; -.
DR   eggNOG; COG0817; Bacteria.
DR   HOGENOM; CLU_091257_2_1_6; -.
DR   InParanoid; P0A814; -.
DR   OMA; AICHIWR; -.
DR   PhylomeDB; P0A814; -.
DR   BioCyc; EcoCyc:EG10925-MON; -.
DR   BioCyc; MetaCyc:EG10925-MON; -.
DR   BRENDA; 3.1.21.10; 2026.
DR   EvolutionaryTrace; P0A814; -.
DR   PRO; PR:P0A814; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0048476; C:Holliday junction resolvase complex; IDA:EcoCyc.
DR   GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IDA:EcoCyc.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000725; P:recombinational repair; IMP:EcoCyc.
DR   GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR   CDD; cd16962; RuvC; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_00034; RuvC; 1.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR020563; X-over_junc_endoDNase_Mg_BS.
DR   InterPro; IPR002176; X-over_junc_endoDNase_RuvC.
DR   PANTHER; PTHR30194; PTHR30194; 1.
DR   Pfam; PF02075; RuvC; 1.
DR   PRINTS; PR00696; RSOLVASERUVC.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   TIGRFAMs; TIGR00228; ruvC; 1.
DR   PROSITE; PS01321; RUVC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; DNA damage;
KW   DNA recombination; DNA repair; Hydrolase; Magnesium; Metal-binding;
KW   Nuclease; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1661673,
FT                   ECO:0000269|PubMed:1758493"
FT   CHAIN           2..173
FT                   /note="Crossover junction endodeoxyribonuclease RuvC"
FT                   /id="PRO_0000183096"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         139
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:1HJR"
FT   STRAND          11..22
FT                   /evidence="ECO:0007829|PDB:1HJR"
FT   STRAND          25..35
FT                   /evidence="ECO:0007829|PDB:1HJR"
FT   HELIX           41..59
FT                   /evidence="ECO:0007829|PDB:1HJR"
FT   STRAND          62..68
FT                   /evidence="ECO:0007829|PDB:1HJR"
FT   TURN            75..77
FT                   /evidence="ECO:0007829|PDB:1HJR"
FT   HELIX           78..93
FT                   /evidence="ECO:0007829|PDB:1HJR"
FT   TURN            94..96
FT                   /evidence="ECO:0007829|PDB:1HJR"
FT   STRAND          99..103
FT                   /evidence="ECO:0007829|PDB:1HJR"
FT   HELIX           104..111
FT                   /evidence="ECO:0007829|PDB:1HJR"
FT   STRAND          113..116
FT                   /evidence="ECO:0007829|PDB:1HJR"
FT   HELIX           119..129
FT                   /evidence="ECO:0007829|PDB:1HJR"
FT   HELIX           141..152
FT                   /evidence="ECO:0007829|PDB:1HJR"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:1HJR"
SQ   SEQUENCE   173 AA;  18747 MW;  2170DCFA4AD43FE1 CRC64;
     MAIILGIDPG SRVTGYGVIR QVGRQLSYLG SGCIRTKVDD LPSRLKLIYA GVTEIITQFQ
     PDYFAIEQVF MAKNADSALK LGQARGVAIV AAVNQELPVF EYAARQVKQT VVGIGSAEKS
     QVQHMVRTLL KLPANPQADA ADALAIAITH CHVSQNAMQM SESRLNLARG RLR
 
 
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