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RUVC_THET8
ID   RUVC_THET8              Reviewed;         166 AA.
AC   Q5SJC4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Crossover junction endodeoxyribonuclease RuvC {ECO:0000255|HAMAP-Rule:MF_00034};
DE            EC=3.1.21.10 {ECO:0000255|HAMAP-Rule:MF_00034};
DE   AltName: Full=Holliday junction nuclease RuvC {ECO:0000255|HAMAP-Rule:MF_00034};
DE   AltName: Full=Holliday junction resolvase RuvC {ECO:0000255|HAMAP-Rule:MF_00034};
GN   Name=ruvC {ECO:0000255|HAMAP-Rule:MF_00034}; OrderedLocusNames=TTHA1090;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00034}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00034};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00034};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00034};
CC   -!- SIMILARITY: Belongs to the RuvC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00034}.
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DR   EMBL; AP008226; BAD70913.1; -; Genomic_DNA.
DR   RefSeq; WP_011173164.1; NC_006461.1.
DR   RefSeq; YP_144356.1; NC_006461.1.
DR   PDB; 4EP4; X-ray; 1.28 A; A/B=1-166.
DR   PDB; 4EP5; X-ray; 2.08 A; A=1-166.
DR   PDB; 4LD0; X-ray; 3.75 A; A/B=1-166.
DR   PDB; 6S16; X-ray; 3.41 A; A/B=1-166.
DR   PDBsum; 4EP4; -.
DR   PDBsum; 4EP5; -.
DR   PDBsum; 4LD0; -.
DR   PDBsum; 6S16; -.
DR   AlphaFoldDB; Q5SJC4; -.
DR   SMR; Q5SJC4; -.
DR   STRING; 300852.55772472; -.
DR   EnsemblBacteria; BAD70913; BAD70913; BAD70913.
DR   GeneID; 3168165; -.
DR   KEGG; ttj:TTHA1090; -.
DR   PATRIC; fig|300852.9.peg.1070; -.
DR   eggNOG; COG0817; Bacteria.
DR   HOGENOM; CLU_091257_3_1_0; -.
DR   OMA; AICHIWR; -.
DR   PhylomeDB; Q5SJC4; -.
DR   BRENDA; 3.1.21.10; 2305.
DR   Proteomes; UP000000532; Chromosome.
DR   GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
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; 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.
PE   1: Evidence at protein level;
KW   3D-structure; DNA damage; DNA recombination; DNA repair; Hydrolase;
KW   Magnesium; Metal-binding; Nuclease; Reference proteome.
FT   CHAIN           1..166
FT                   /note="Crossover junction endodeoxyribonuclease RuvC"
FT                   /id="PRO_0000225184"
FT   BINDING         7
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT   BINDING         70
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT   BINDING         146
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:4EP4"
FT   STRAND          10..20
FT                   /evidence="ECO:0007829|PDB:4EP4"
FT   STRAND          22..26
FT                   /evidence="ECO:0007829|PDB:4EP4"
FT   STRAND          28..37
FT                   /evidence="ECO:0007829|PDB:4EP4"
FT   STRAND          40..42
FT                   /evidence="ECO:0007829|PDB:4EP5"
FT   HELIX           44..62
FT                   /evidence="ECO:0007829|PDB:4EP4"
FT   STRAND          65..70
FT                   /evidence="ECO:0007829|PDB:4EP4"
FT   HELIX           79..98
FT                   /evidence="ECO:0007829|PDB:4EP4"
FT   STRAND          102..105
FT                   /evidence="ECO:0007829|PDB:4EP4"
FT   HELIX           107..115
FT                   /evidence="ECO:0007829|PDB:4EP4"
FT   STRAND          117..119
FT                   /evidence="ECO:0007829|PDB:6S16"
FT   HELIX           122..132
FT                   /evidence="ECO:0007829|PDB:4EP4"
FT   HELIX           142..159
FT                   /evidence="ECO:0007829|PDB:4EP4"
SQ   SEQUENCE   166 AA;  17755 MW;  214FBE6E1D4A91C3 CRC64;
     MVVAGIDPGI THLGLGVVAV EGKGALKARL LHGEVVKTSP QEPAKERVGR IHARVLEVLH
     RFRPEAVAVE EQFFYRQNEL AYKVGWALGA VLVAAFEAGV PVYAYGPMQV KQALAGHGHA
     AKEEVALMVR GILGLKEAPR PSHLADALAI ALTHAFYARM GTAKPL
 
 
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