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 17-JUN-2020, entry version 55. DE RecName: Full=Holliday junction resolvase Hjc {ECO:0000255|HAMAP-Rule:MF_01490}; DE Short=Hjc {ECO:0000255|HAMAP-Rule:MF_01490}; DE EC=3.1.22.4 {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=3.1.22.4; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 eggNOG; COG1591; LUCA. DR HOGENOM; CLU_139546_1_0_2; -. DR InParanoid; Q7LXU0; -. DR KO; K03552; -. DR OMA; WYFFHPG; -. DR BioCyc; SSOL273057:G1FZF-608-MONOMER; -. DR BRENDA; 3.1.22.4; 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 METAL 12 FT /note="Magnesium" FT /evidence="ECO:0000305" FT METAL 42 FT /note="Magnesium" FT /evidence="ECO:0000305" FT METAL 55 FT /note="Magnesium" 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:0000244|PDB:4TKD" FT STRAND 25..28 FT /evidence="ECO:0000244|PDB:4TKD" FT STRAND 42..47 FT /evidence="ECO:0000244|PDB:4TKD" FT STRAND 50..57 FT /evidence="ECO:0000244|PDB:4TKD" FT STRAND 65..68 FT /evidence="ECO:0000244|PDB:4TKD" FT HELIX 70..83 FT /evidence="ECO:0000244|PDB:4TKD" FT STRAND 86..91 FT /evidence="ECO:0000244|PDB:4TKD" FT STRAND 94..96 FT /evidence="ECO:0000244|PDB:4TKD" FT STRAND 98..101 FT /evidence="ECO:0000244|PDB:4TKD" FT HELIX 102..104 FT /evidence="ECO:0000244|PDB:4TKD" FT STRAND 105..107 FT /evidence="ECO:0000244|PDB:4TKD" FT STRAND 113..115 FT /evidence="ECO:0000244|PDB:4TKD" FT HELIX 124..135 FT /evidence="ECO:0000244|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 //