ID A0A218NZL0_THECE Unreviewed; 1709 AA. AC A0A218NZL0; DT 27-SEP-2017, integrated into UniProtKB/TrEMBL. DT 27-SEP-2017, sequence version 1. DT 22-NOV-2017, entry version 3. 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=5.99.1.3 {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. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=2264 {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 CC positive supercoils in an ATP-dependent process. It cleaves CC transiently a single DNA strand and remains covalently bound to CC the 5' DNA end through a tyrosine residue. May be involved in CC rewinding the DNA strands in the regions of the chromosome that CC have opened up to allow transcription or replication. CC {ECO:0000256|HAMAP-Rule:MF_01125, ECO:0000256|RuleBase:RU004026}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000256|HAMAP-Rule:MF_01125}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_01125, CC ECO:0000256|RuleBase:RU004026}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01125}. CC -!- DOMAIN: Both the DNA unwinding and positive supercoiling CC activities require the cooperation of both domains. The CC cooperative action between the helicase-like and the topoisomerase CC domains is specific. The helicase-like domain probably does not CC directly unwind DNA but acts more likely by driving ATP-dependent CC conformational changes within the whole enzyme, functioning more CC like a protein motor. The "latch" region of the N-terminal domain CC plays a regulatory role in the enzyme, repressing topoisomerase CC activity in the absence of ATP and therefore preventing the enzyme CC from acting as an ATP-independent relaxing enzyme; it also helps CC to coordinate nucleotide hydrolysis by the ATPase domain with the CC 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 CC to be 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 CC type I/III topoisomerase family. {ECO:0000256|HAMAP- CC Rule:MF_01125}. CC -!- SIMILARITY: In the N-terminal section; belongs to the DEAD box CC helicase family. DDVD subfamily. {ECO:0000256|HAMAP- CC 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 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:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule. 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; 2.70.20.10; -; 1. 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; IPR013825; Topo_IA_cen_sub2. 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 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 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; 3. DR SUPFAM; SSF52540; SSF52540; 4. 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|HAMAP-Rule:MF_01125, KW ECO:0000256|RuleBase:RU004026}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000197156}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01125, KW ECO:0000256|RuleBase:RU004026}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_01125, KW ECO:0000256|RuleBase:RU004026}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01125, KW ECO:0000256|RuleBase:RU004026}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01125, KW ECO:0000256|RuleBase:RU004026}; 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 Reference proteome {ECO:0000313|Proteomes:UP000197156}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01125, KW ECO:0000256|RuleBase:RU004026}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01125, ECO:0000256|RuleBase:RU004026}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01125, KW ECO:0000256|RuleBase:RU004026}. FT DOMAIN 93 318 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 642 805 Toprim. {ECO:0000259|PROSITE:PS50880}. FT DOMAIN 1160 1287 DOD-type homing endonuclease. FT {ECO:0000259|PROSITE:PS50819}. FT DOMAIN 1428 1449 INTEIN_C_TER. {ECO:0000259|PROSITE: FT PS50818}. FT ZN_FING 9 30 C4-type 1. {ECO:0000256|HAMAP-Rule: FT MF_01125}. FT NP_BIND 106 113 ATP. {ECO:0000256|HAMAP-Rule:MF_01125}. FT ZN_FING 725 744 C4-type 2. {ECO:0000256|HAMAP-Rule: FT MF_01125}. FT REGION 648 1709 Topoisomerase I. {ECO:0000256|HAMAP-Rule: FT MF_01125}. FT COILED 260 287 {ECO:0000256|SAM:Coils}. FT ACT_SITE 1451 1451 For DNA cleavage activity. FT {ECO:0000256|HAMAP-Rule:MF_01125}. FT BINDING 89 89 ATP. {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 //