ID A0A218NZL0_THECE Unreviewed; 1709 AA. AC A0A218NZL0; DT 27-SEP-2017, integrated into UniProtKB/TrEMBL. DT 27-SEP-2017, sequence version 1. DT 02-JUN-2021, entry version 25. DE RecName: Full=Reverse gyrase {ECO:0000256|HAMAP-Rule:MF_01125}; DE Includes: DE RecName: Full=Helicase {ECO:0000256|HAMAP-Rule:MF_01125}; DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_01125}; DE Includes: DE RecName: Full=Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01125}; DE EC=5.6.2.2 {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. It cleaves transiently a single CC DNA strand and remains covalently bound to the 5' DNA end through a CC tyrosine residue. May be involved in rewinding the DNA strands in the CC regions of the chromosome that have opened up to allow transcription or CC replication. {ECO:0000256|HAMAP-Rule:MF_01125, CC ECO:0000256|RuleBase:RU004026}. 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; EC=3.6.4.12; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01125, CC ECO:0000256|RuleBase:RU004026}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-dependent breakage, passage and rejoining of double- CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01125, CC ECO:0000256|RuleBase:RU004026}; CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP- CC Rule:MF_01125}. CC -!- DOMAIN: Both the DNA unwinding and positive supercoiling activities CC require the cooperation of both domains. The cooperative action between CC the helicase-like and the topoisomerase domains is specific. The CC helicase-like domain probably does not directly unwind DNA but acts CC more likely by driving ATP-dependent conformational changes within the CC whole enzyme, functioning more like a protein motor. The 'latch' region CC of the N-terminal domain plays a regulatory role in the enzyme, CC repressing topoisomerase activity in the absence of ATP and therefore 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 discovered so far. It appears to be CC essential for adaptation to life at high temperatures. CC {ECO:0000256|HAMAP-Rule:MF_01125}. CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic type CC I/III 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|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 EnsemblBacteria; ASI98103; ASI98103; A3L02_00210. DR KEGG; tce:A3L02_00210; -. DR Proteomes; UP000197156; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC. DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule. 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; cd03361; TOPRIM_TopoIA_RevGyr; 1. DR Gene3D; 1.10.290.10; -; 2. DR Gene3D; 1.10.460.10; -; 2. DR Gene3D; 3.10.28.10; -; 1. 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 PANTHER; PTHR43505; PTHR43505; 1. DR Pfam; PF00270; DEAD; 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; SSF51294; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF55608; SSF55608; 1. DR SUPFAM; SSF56712; SSF56712; 2. DR TIGRFAMs; TIGR01443; intein_Cterm; 1. DR TIGRFAMs; TIGR01445; intein_Nterm; 1. DR TIGRFAMs; TIGR01054; rgy; 1. 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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01125}; Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_01125}; KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01125}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, 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|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01125}; 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_TER" FT /evidence="ECO:0000259|PROSITE:PS50818" FT ZN_FING 9..30 FT /note="C4-type 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01125" FT NP_BIND 106..113 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01125" FT ZN_FING 725..744 FT /note="C4-type 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01125" FT REGION 648..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="For DNA cleavage activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01125" FT BINDING 89 FT /note="ATP" 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 //