ID A0A218NZL0_THECE Unreviewed; 1709 AA. AC A0A218NZL0; DT 27-SEP-2017, integrated into UniProtKB/TrEMBL. DT 27-SEP-2017, sequence version 1. DT 29-MAY-2024, entry version 36. DE RecName: Full=Reverse gyrase {ECO:0000256|HAMAP-Rule:MF_01125, ECO:0000256|RuleBase:RU004026}; DE EC=5.6.2.- {ECO:0000256|HAMAP-Rule:MF_01125}; GN Name=rgy {ECO:0000256|HAMAP-Rule:MF_01125}; GN ORFNames=A3L02_00210 {ECO:0000313|EMBL:ASI98103.1}; OS Thermococcus celer Vu 13 = JCM 8558. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=1293037 {ECO:0000313|EMBL:ASI98103.1, ECO:0000313|Proteomes:UP000197156}; RN [1] {ECO:0000313|EMBL:ASI98103.1, ECO:0000313|Proteomes:UP000197156} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Vu 13 {ECO:0000313|EMBL:ASI98103.1, RC ECO:0000313|Proteomes:UP000197156}; RA Oger P.M.; RT "Complete genome sequence of Thermococcus celer."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Modifies the topological state of DNA by introducing positive CC supercoils in an ATP-dependent process, increasing the linking number CC in steps of +1. Binds to single-stranded DNA, transiently cleaves and CC then rejoins the ends, introducing a positive supercoil in the process. CC The scissile phosphodiester is attacked by the catalytic tyrosine of CC the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)- CC enzyme intermediate. Involved in rewinding DNA strands in regions of CC the chromosome that have opened up to allow replication, transcription, CC DNA repair and/or for DNA protection. {ECO:0000256|RuleBase:RU004026}. CC -!- FUNCTION: Modifies the topological state of DNA by introducing positive CC supercoils in an ATP-dependent process, increasing the linking number CC in steps of +1. Binds to single-stranded DNA, transiently cleaves and CC then rejoins the ends, introducing a positive supercoil in the process. CC The scissile phosphodiester is attacked by the catalytic tyrosine of CC the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)- CC enzyme intermediate. Probably involved in rewinding DNA strands in CC regions of the chromosome that have opened up to allow replication, CC transcription, DNA repair and/or for DNA protection. CC {ECO:0000256|HAMAP-Rule:MF_01125}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000256|ARBA:ARBA00001836, ECO:0000256|HAMAP- CC Rule:MF_01125, ECO:0000256|RuleBase:RU004026}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01125}; CC Note=Binds 1 or 2 zinc ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01125}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01125}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_01125}. CC -!- DOMAIN: Introduction of positive supercoils requires the cooperation of CC both domains. The helicase-like domain probably does not directly CC unwind DNA, but more likely acts by driving ATP-dependent CC conformational changes within the whole enzyme. A beta hairpin in the CC 'latch' region of the N-terminal domain plays a regulatory role in the CC enzyme, repressing topoisomerase activity in the absence of ATP and CC preventing the enzyme from acting as an ATP-independent relaxing CC enzyme; it also helps to coordinate nucleotide hydrolysis by the ATPase CC domain with the supercoiling activity of the topoisomerase domain. CC {ECO:0000256|HAMAP-Rule:MF_01125}. CC -!- MISCELLANEOUS: This enzyme is the only unique feature of CC hyperthermophilic bacteria/archaea known and seems to be essential for CC adaptation to life at high temperatures. It may play a role in CC stabilization of DNA at high temperatures. {ECO:0000256|HAMAP- CC Rule:MF_01125}. CC -!- SIMILARITY: In the C-terminal section; belongs to the type IA CC topoisomerase family. {ECO:0000256|HAMAP-Rule:MF_01125}. CC -!- SIMILARITY: In the N-terminal section; belongs to the DEAD box helicase CC family. DDVD subfamily. {ECO:0000256|ARBA:ARBA00043976, CC ECO:0000256|HAMAP-Rule:MF_01125}. 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; CP014854; ASI98103.1; -; Genomic_DNA. DR KEGG; tce:A3L02_00210; -. DR OrthoDB; 30963at2157; -. DR Proteomes; UP000197156; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR CDD; cd17924; DDXDc_reverse_gyrase; 1. DR CDD; cd00081; Hint; 1. DR CDD; cd18798; SF2_C_reverse_gyrase; 1. DR CDD; cd03361; TOPRIM_TopoIA_RevGyr; 1. DR Gene3D; 2.60.510.20; -; 2. DR Gene3D; 3.40.50.140; -; 1. DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 2. DR Gene3D; 3.10.28.10; Homing endonucleases; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3. DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 2. DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 2. DR HAMAP; MF_01125; Reverse_gyrase; 1. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR036844; Hint_dom_sf. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR004860; LAGLIDADG_2. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005736; Reverse_gyrase. DR InterPro; IPR003601; Topo_IA_2. DR InterPro; IPR013497; Topo_IA_cen. DR InterPro; IPR013824; Topo_IA_cen_sub1. DR InterPro; IPR013826; Topo_IA_cen_sub3. DR InterPro; IPR023405; Topo_IA_core_domain. DR InterPro; IPR003602; Topo_IA_DNA-bd_dom. DR InterPro; IPR006171; TOPRIM_domain. DR InterPro; IPR034142; TOPRIM_RevGyr. DR InterPro; IPR040569; Znf_Rg. DR NCBIfam; TIGR01443; intein_Cterm; 1. DR NCBIfam; TIGR01445; intein_Nterm; 1. DR NCBIfam; TIGR01054; rgy; 1. DR PANTHER; PTHR43505; REVERSE GYRASE; 1. DR PANTHER; PTHR43505:SF1; REVERSE GYRASE; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF14890; Intein_splicing; 1. DR Pfam; PF14528; LAGLIDADG_3; 1. DR Pfam; PF01131; Topoisom_bac; 2. DR Pfam; PF01751; Toprim; 1. DR Pfam; PF17915; zf_Rg; 1. DR PRINTS; PR00379; INTEIN. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1. DR SUPFAM; SSF55608; Homing endonucleases; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 2. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS50818; INTEIN_C_TER; 1. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01125, KW ECO:0000256|RuleBase:RU004026}; KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01125}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_01125}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_01125}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01125}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01125, KW ECO:0000256|RuleBase:RU004026}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01125, KW ECO:0000256|RuleBase:RU004026}; KW Protein splicing {ECO:0000256|ARBA:ARBA00023000}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP- KW Rule:MF_01125}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01125}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP- KW Rule:MF_01125}. FT DOMAIN 93..318 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 642..805 FT /note="Toprim" FT /evidence="ECO:0000259|PROSITE:PS50880" FT DOMAIN 1160..1287 FT /note="DOD-type homing endonuclease" FT /evidence="ECO:0000259|PROSITE:PS50819" FT DOMAIN 1428..1449 FT /note="Intein C-terminal splicing" FT /evidence="ECO:0000259|PROSITE:PS50818" FT REGION 638..1709 FT /note="Topoisomerase I" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01125" FT COILED 260..287 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 1451 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01125" FT BINDING 89 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01125" SQ SEQUENCE 1709 AA; 195851 MW; 8068FA9939B0A960 CRC64; MKAIYREMCP NCFGRISDER LYLKNPCDDC LDEPVHADSY FDLVTGVRNA LQLKGTLKEW ERIHSLEKGL REVEDFFRKA TGFTFWSAQR TWVKRLLKGR SFSIIAPTGM GKSTFGAVMA VWHATRGKKS YIVVPTTPLV IQTVKKIEAI VERAGVEVNL AYYHGNLRKR EKEEMLAKIQ NGDYDVLVTS AQWLARKYDE VLDGRHFDFI FVDDVDAFLK ASKNIDRSLH LLGFDDEVIA KAWEIIRLKR EMSRYLNGRA KDGEEKLREL NAEISKLQRE IDEFKARNDI GIMIIASATG SARGDRIKLY RELLGFEVGS GRSALRNVVD TYLKPDKGIK EHVEELLARL GKGGIIFTPV DQGLSYAEEL AAYLRERGFR IELVSSKNKK AIERFENGEA DYLIGSATYY GSLVRGLDLP HLIRYAVFTG VPKFRFGMDL ERPTIYRSLG LLSEIMDFLG DEDRKKAERL HARLRRLIRN IPQFELLKIE EALAEGLPME NAFHNHVLDV FRELVDFLRS ALKDEEVLRK LAEDPFVSVK EEGGKWYIEI PDVRTYIQAT GRTSRLFAGG ITKGLSVLIV DNEKVFNGLV RQMRWRFTEF KMLPFEELDL DGVLREIDED REKVRLVMEG KISSKVKDLV KSALMIVESP NKARTIANFF GRPSKTRIGD LVAYEVSIGK VMLTILASGG HMFDLVTNEG YHGVLTEERD GVMRFVPVYD TIKRCRDCGH QFVDWEEKGV CPRCGSRNVR DALENVKAMR ELAQEVDEIL IATDPDTEGE KIAWDIRNVL GPYAPNIKRI EFHEVTRPAI LKAIEEAREV NEGRVNAQIV RRIEDRWIGF ELSQELQRVF ENHNLSAGRV QTPVLGWIIE RYKEFTESEV YFLGLTLENG LQLTVELGKD GKNVELPEYV TVEDVRLEER ELNPMPPYTT DEMLKDASTF LKLSAPETMR LAQDLFEAGL CVTPDTVVSM ADGRIMSIET AVKGGEGNLL GINGLKVKNA EATEFWEINW NGPLKILKLK NGHEIKATPD HGLLVIRDGK LGWVSAKNIK PGDYVAFAYN TGHPGKEEYT LLRMLVELKI TDVMVELEKE YFDSKIAPLI RERIKTSTKY KYLRNRVVPL KKLLEWGVNG YEPHVRSLYR QRTGSKRIPN FKLDENFWYI FGLVLGDGTL RGSKVLISQT PLKGVKESLE QTFPFLHVFE TTNQVGFSNS ILAEVFRRLG ARSGELHPII FTIPENMMNA MMAGYFDTDG TFSLLHDKRG VDLRVILTSK RGDVLKRLSV YLYRIGILNY LRENGRRGGW DLTISNRSLG AFKEKIYPHL RIRRKQFEEA YSAYRGTRKS MESDLIPVGN VIKNLGFPEG VKVKILREEG IDVWNWLKKP GNVPRDKLVR VLSYAEDGEI KEYLRSLVEA NVTWVEVSEV RETRYTGKLY DFTTTTGNFI ANGAVSHNCT YHRTDSTHVS NTGIEVAKEY ITGELGEEYF KPRHWGEEGT HEAIRPTRPI DTGRLMQLIR DGVIQLPKNL TRNHYRLYDM IFRRFMTGQM KAAKLLMEKA LINAGVGKVE LEGYVEVLED GWTKLRSPPF RQLPRLEPGA RLKVVESKRW KAPKVPLYSQ GDVIALMKER GIGRPSTYAK IVETLVRRYY VIETRGRKKL VPTEQGIKVY HYLISKYKDL VSEEKTRELE ETMDLIEDGK ADYQEVLGRL YGEIREYLG //