ID HJC_SULSO Reviewed; 143 AA. AC Q7LXU0; Q9UWX8; DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot. DT 31-MAY-2011, sequence version 1. DT 07-JAN-2015, entry version 25. 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 Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / OS P2). OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. 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., RA Gaasterland T., Garrett R.A., Gordon P., Jeffries A.C., Kozera C., RA Kushwaha N., Lafleur E., Medina N., Peng X., Penny S.L., She Q., RA St Jean A., van der Oost J., Young F., Zivanovic Y., Doolittle W.F., RA Ragan M.A., Sensen C.W.; RT "Gene content and organization of a 281-kbp contig from the genome of RT the 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., RA Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., RA De Moors A., Erauso G., Fletcher C., Gordon P.M.K., RA Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X., RA Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., RA 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 RT resolving 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, ENZYME 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 RT components 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 RT resolving enzyme Hje."; RL Nucleic Acids Res. 32:5442-5451(2004). RN [7] RP FUNCTION, ENZYME 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 CC some degree of sequence preference in a mobile junction. Cleaves CC 4-way DNA junctions introducing paired nicks in opposing strands, CC leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group CC that are ligated to produce recombinant products. Can cleave all 4 CC strands 3 bases 3' of the junction center. Cleaves both mobile and CC immobile junctions. Modifies the structure of the 4-way DNA CC junction, a model Holliday junction structure. The protein forms CC multiple complexes with 4-way DNA, suggesting more than 1 CC homodimer can bind to each junction. {ECO:0000269|PubMed:10701121, CC ECO:0000269|PubMed:10736227, ECO:0000269|PubMed:10940317, CC ECO:0000269|PubMed:11709558, ECO:0000269|PubMed:17011573}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage at a junction such as CC a reciprocal single-stranded crossover between two homologous DNA CC duplexes (Holliday junction). {ECO:0000255|HAMAP-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- CC Rule:MF_01490, ECO:0000269|PubMed:11709558}; CC -!- ENZYME REGULATION: Autoinhibits at very high concentrations, CC possibly because of extreme junction distortion. Inhibition (and CC activity at low concentrations of enzyme) is stimulated by dsDNA CC and Sso7d (PubMed:11709558). Activity stimulated by PCNA subunit CC PCNA1 (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, CC with 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; NP_342099.1; NC_002754.1. DR PDB; 1HH1; X-ray; 2.15 A; A=1-143. DR PDBsum; 1HH1; -. DR ProteinModelPortal; Q7LXU0; -. DR SMR; Q7LXU0; 9-140. DR EnsemblBacteria; AAK40889; AAK40889; SSO0575. DR GeneID; 1454856; -. DR KEGG; sso:SSO0575; -. DR HOGENOM; HOG000222547; -. DR InParanoid; Q7LXU0; -. DR KO; K03552; -. DR OMA; EVFYAIE; -. DR BioCyc; SSOL273057:GCH2-551-MONOMER; -. DR Proteomes; UP000001974; Chromosome. DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR Gene3D; 3.40.1350.10; -; 1. DR HAMAP; MF_01490; HJ_Resolv_Hjc; 1. DR InterPro; IPR002732; Resolv_Hlld_junc. DR InterPro; IPR014428; Resolv_Hlld_junc_arc. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR011856; tRNA_endonuc-like_dom. DR Pfam; PF01870; Hjc; 1. DR PIRSF; PIRSF004985; Hlld_jn_rslvs_ar; 1. DR ProDom; PD015874; PD015874; 1. DR SUPFAM; SSF52980; SSF52980; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA damage; DNA recombination; KW DNA repair; DNA-binding; Endonuclease; Hydrolase; Magnesium; KW Metal-binding; Nuclease; Reference proteome. FT CHAIN 1 143 Holliday junction resolvase Hjc. FT /FTId=PRO_0000429158. FT ACT_SITE 32 32 {ECO:0000255|HAMAP-Rule:MF_01490}. FT METAL 12 12 Magnesium. {ECO:0000305}. FT METAL 42 42 Magnesium. {ECO:0000305}. FT METAL 55 55 Magnesium. {ECO:0000305}. FT SITE 57 57 Transition state stabilizer. FT {ECO:0000255}. FT MUTAGEN 12 12 E->Q: No cleavage of 4-way junction DNA. FT Binds junction DNA normally. FT {ECO:0000269|PubMed:10940317}. FT MUTAGEN 32 32 S->A: No cleavage of fixed 4-way junction FT DNA. Binds junction DNA normally. FT {ECO:0000269|PubMed:15479781}. FT MUTAGEN 42 42 D->N: No cleavage of 4-way junction DNA. FT Binds junction DNA normally. FT {ECO:0000269|PubMed:10940317}. FT MUTAGEN 55 55 E->Q: No cleavage of 4-way junction DNA. FT Binds junction DNA normally. FT {ECO:0000269|PubMed:10940317}. FT MUTAGEN 57 57 K->A: 1000-fold less cleavage of 4-way FT junction DNA. Binds junction DNA FT normally. {ECO:0000269|PubMed:10940317}. FT MUTAGEN 137 143 Missing: No interaction with PCNA1. FT {ECO:0000269|PubMed:17011573}. FT HELIX 10 21 {ECO:0000244|PDB:1HH1}. FT STRAND 25 28 {ECO:0000244|PDB:1HH1}. FT STRAND 42 47 {ECO:0000244|PDB:1HH1}. FT STRAND 50 56 {ECO:0000244|PDB:1HH1}. FT STRAND 66 68 {ECO:0000244|PDB:1HH1}. FT HELIX 70 83 {ECO:0000244|PDB:1HH1}. FT STRAND 86 92 {ECO:0000244|PDB:1HH1}. FT STRAND 97 101 {ECO:0000244|PDB:1HH1}. FT HELIX 102 104 {ECO:0000244|PDB:1HH1}. FT STRAND 105 107 {ECO:0000244|PDB:1HH1}. FT HELIX 124 139 {ECO:0000244|PDB:1HH1}. SQ SEQUENCE 143 AA; 16010 MW; 22099074AECF1279 CRC64; MNAKKRKGSA VERNIVSRLR DKGFAVVRAP ASGSKRKDPI PDIIALKNGV IILIEMKSRK DIEGKIYVRR EQAEGIIEFA RKSGGSLFLG VKKPGVLKFI PFEKLRRTET GNYVADSEIE GLDLEDLVRL VEAKISRTLD NFL //