HJC_SACS2
ID HJC_SACS2 Reviewed; 143 AA.
AC Q7LXU0; Q9UWX8;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Holliday junction resolvase Hjc {ECO:0000255|HAMAP-Rule:MF_01490};
DE Short=Hjc {ECO:0000255|HAMAP-Rule:MF_01490};
DE EC=3.1.21.10 {ECO:0000255|HAMAP-Rule:MF_01490};
GN Name=hjc {ECO:0000255|HAMAP-Rule:MF_01490}; OrderedLocusNames=SSO0575;
GN ORFNames=ORF-c21_024;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DNA-BINDING.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10701121; DOI=10.1139/g99-108;
RA Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT "Gene content and organization of a 281-kbp contig from the genome of the
RT extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL Genome 43:116-136(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP FUNCTION, DNA-BINDING, AND MUTAGENESIS OF GLU-12; ASP-42; GLU-55 AND
RP LYS-57.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10940317; DOI=10.1074/jbc.m003420200;
RA Kvaratskhelia M., Wardleworth B.N., Norman D.G., White M.F.;
RT "A conserved nuclease domain in the archaeal Holliday junction resolving
RT enzyme Hjc.";
RL J. Biol. Chem. 275:25540-25546(2000).
RN [4]
RP FUNCTION, AND DNA-BINDING.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10736227; DOI=10.1006/jmbi.2000.3624;
RA Kvaratskhelia M., White M.F.;
RT "Two Holliday junction resolving enzymes in Sulfolobus solfataricus.";
RL J. Mol. Biol. 297:923-932(2000).
RN [5]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, AND DNA-BINDING.
RX PubMed=11709558; DOI=10.1074/jbc.m109496200;
RA Kvaratskhelia M., Wardleworth B.N., Bond C.S., Fogg J.M., Lilley D.M.,
RA White M.F.;
RT "Holliday junction resolution is modulated by archaeal chromatin components
RT in vitro.";
RL J. Biol. Chem. 277:2992-2996(2002).
RN [6]
RP MUTAGENESIS OF SER-32.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=15479781; DOI=10.1093/nar/gkh869;
RA Middleton C.L., Parker J.L., Richard D.J., White M.F., Bond C.S.;
RT "Substrate recognition and catalysis by the Holliday junction resolving
RT enzyme Hje.";
RL Nucleic Acids Res. 32:5442-5451(2004).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH PCNA1, SUBUNIT, AND
RP MUTAGENESIS OF 137-ARG--LEU-143.
RX PubMed=17011573; DOI=10.1016/j.jmb.2006.09.011;
RA Dorazi R., Parker J.L., White M.F.;
RT "PCNA activates the Holliday junction endonuclease Hjc.";
RL J. Mol. Biol. 364:243-247(2006).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), AND SUBUNIT.
RX PubMed=11331763; DOI=10.1073/pnas.091613398;
RA Bond C.S., Kvaratskhelia M., Richard D., White M.F., Hunter W.N.;
RT "Structure of Hjc, a Holliday junction resolvase, from Sulfolobus
RT solfataricus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:5509-5514(2001).
CC -!- FUNCTION: A structure-specific endonuclease that resolves Holliday
CC junction (HJ) intermediates during genetic recombination; may have some
CC degree of sequence preference in a mobile junction. Cleaves 4-way DNA
CC junctions introducing paired nicks in opposing strands, leaving a 5'-
CC terminal phosphate and a 3'-terminal hydroxyl group that are ligated to
CC produce recombinant products. Can cleave all 4 strands 3 bases 3' of
CC the junction center. Cleaves both mobile and immobile junctions.
CC Modifies the structure of the 4-way DNA junction, a model Holliday
CC junction structure. The protein forms multiple complexes with 4-way
CC DNA, suggesting more than 1 homodimer can bind to each junction.
CC {ECO:0000269|PubMed:10701121, ECO:0000269|PubMed:10736227,
CC ECO:0000269|PubMed:10940317, ECO:0000269|PubMed:11709558,
CC ECO:0000269|PubMed:17011573}.
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_01490};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01490,
CC ECO:0000269|PubMed:11709558};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01490,
CC ECO:0000269|PubMed:11709558};
CC -!- ACTIVITY REGULATION: Autoinhibits at very high concentrations, possibly
CC because of extreme junction distortion. Inhibition (and activity at low
CC concentrations of enzyme) is stimulated by dsDNA and Sso7d
CC (PubMed:11709558). Activity stimulated by PCNA subunit PCNA1
CC (PubMed:17011573). {ECO:0000269|PubMed:11709558,
CC ECO:0000269|PubMed:17011573}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with PCNA subunit PCNA1.
CC {ECO:0000255|HAMAP-Rule:MF_01490, ECO:0000269|PubMed:11331763,
CC ECO:0000269|PubMed:17011573, ECO:0000305}.
CC -!- MISCELLANEOUS: A second Holliday junction resolving enzyme, Hje, with
CC different substrate specificity exists in this organism.
CC -!- SIMILARITY: Belongs to the Holliday junction resolvase Hjc family.
CC {ECO:0000255|HAMAP-Rule:MF_01490}.
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DR EMBL; Y18930; CAB57725.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK40889.1; -; Genomic_DNA.
DR PIR; B90204; B90204.
DR RefSeq; WP_009991087.1; NC_002754.1.
DR PDB; 1HH1; X-ray; 2.15 A; A=1-143.
DR PDB; 4TKD; X-ray; 2.01 A; A/B/C/D=1-143.
DR PDB; 4TKK; X-ray; 2.40 A; A/B=1-143.
DR PDBsum; 1HH1; -.
DR PDBsum; 4TKD; -.
DR PDBsum; 4TKK; -.
DR AlphaFoldDB; Q7LXU0; -.
DR SMR; Q7LXU0; -.
DR STRING; 273057.SSO0575; -.
DR EnsemblBacteria; AAK40889; AAK40889; SSO0575.
DR GeneID; 44129578; -.
DR KEGG; sso:SSO0575; -.
DR PATRIC; fig|273057.12.peg.583; -.
DR eggNOG; arCOG00919; Archaea.
DR HOGENOM; CLU_139546_1_0_2; -.
DR InParanoid; Q7LXU0; -.
DR OMA; WYFFHPG; -.
DR PhylomeDB; Q7LXU0; -.
DR BRENDA; 3.1.21.10; 6163.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd00523; archeal_HJR; 1.
DR Gene3D; 3.40.1350.10; -; 1.
DR HAMAP; MF_01490; HJ_Resolv_Hjc; 1.
DR InterPro; IPR002732; Hjc.
DR InterPro; IPR014428; Hjc_arc.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR PANTHER; PTHR39651; PTHR39651; 1.
DR Pfam; PF01870; Hjc; 1.
DR PIRSF; PIRSF004985; Hlld_jn_rslvs_ar; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome.
FT CHAIN 1..143
FT /note="Holliday junction resolvase Hjc"
FT /id="PRO_0000429158"
FT ACT_SITE 32
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01490"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT SITE 57
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT MUTAGEN 12
FT /note="E->Q: No cleavage of 4-way junction DNA. Binds
FT junction DNA normally."
FT /evidence="ECO:0000269|PubMed:10940317"
FT MUTAGEN 32
FT /note="S->A: No cleavage of fixed 4-way junction DNA. Binds
FT junction DNA normally."
FT /evidence="ECO:0000269|PubMed:15479781"
FT MUTAGEN 42
FT /note="D->N: No cleavage of 4-way junction DNA. Binds
FT junction DNA normally."
FT /evidence="ECO:0000269|PubMed:10940317"
FT MUTAGEN 55
FT /note="E->Q: No cleavage of 4-way junction DNA. Binds
FT junction DNA normally."
FT /evidence="ECO:0000269|PubMed:10940317"
FT MUTAGEN 57
FT /note="K->A: 1000-fold less cleavage of 4-way junction DNA.
FT Binds junction DNA normally."
FT /evidence="ECO:0000269|PubMed:10940317"
FT MUTAGEN 137..143
FT /note="Missing: No interaction with PCNA1."
FT /evidence="ECO:0000269|PubMed:17011573"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:4TKD"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:4TKD"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:4TKD"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:4TKD"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:4TKD"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:4TKD"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:4TKD"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:4TKD"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:4TKD"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4TKD"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:4TKD"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:4TKD"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:4TKD"
SQ SEQUENCE 143 AA; 16010 MW; 22099074AECF1279 CRC64;
MNAKKRKGSA VERNIVSRLR DKGFAVVRAP ASGSKRKDPI PDIIALKNGV IILIEMKSRK
DIEGKIYVRR EQAEGIIEFA RKSGGSLFLG VKKPGVLKFI PFEKLRRTET GNYVADSEIE
GLDLEDLVRL VEAKISRTLD NFL
