RGYR1_SULTO
ID RGYR1_SULTO Reviewed; 1156 AA.
AC Q971T7; F9VP02;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Reverse gyrase 1 {ECO:0000255|HAMAP-Rule:MF_01125};
DE Includes:
DE RecName: Full=Helicase {ECO:0000255|HAMAP-Rule:MF_01125};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01125};
DE Includes:
DE RecName: Full=Topoisomerase {ECO:0000255|HAMAP-Rule:MF_01125};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01125};
GN Name=rgy1 {ECO:0000255|HAMAP-Rule:MF_01125}; OrderedLocusNames=STK_12900;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP ELECTRON MICROSCOPY (23 ANGSTROMS).
RX PubMed=12359215; DOI=10.1016/s0006-291x(02)02255-6;
RA Matoba K., Mayanagi K., Nakasu S., Kikuchi A., Morikawa K.;
RT "Three-dimensional electron microscopy of the reverse gyrase from
RT Sulfolobus tokodaii.";
RL Biochem. Biophys. Res. Commun. 297:749-755(2002).
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:0000255|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; EC=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01125};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01125};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01125};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_01125};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-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:0000255|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 -!- SIMILARITY: In the N-terminal section; belongs to the DEAD box helicase
CC family. DDVD subfamily. {ECO:0000255|HAMAP-Rule:MF_01125}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic type
CC I/III topoisomerase family. {ECO:0000255|HAMAP-Rule:MF_01125}.
CC -!- CAUTION: Ser-186 is present instead of the conserved Val which is part
CC of the DDVD box. {ECO:0000305}.
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DR EMBL; BA000023; BAK54510.1; -; Genomic_DNA.
DR RefSeq; WP_010979311.1; NC_003106.2.
DR AlphaFoldDB; Q971T7; -.
DR SMR; Q971T7; -.
DR STRING; 273063.STK_12900; -.
DR PRIDE; Q971T7; -.
DR EnsemblBacteria; BAK54510; BAK54510; STK_12900.
DR GeneID; 1459291; -.
DR KEGG; sto:STK_12900; -.
DR PATRIC; fig|273063.9.peg.1449; -.
DR eggNOG; arCOG01526; Archaea.
DR OMA; VMTYIQA; -.
DR OrthoDB; 1837at2157; -.
DR Proteomes; UP000001015; Chromosome.
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: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: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 CDD; cd00186; TOP1Ac; 1.
DR Gene3D; 1.10.290.10; -; 1.
DR Gene3D; 1.10.460.10; -; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR HAMAP; MF_01125; Reverse_gyrase; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
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; IPR040569; Znf_Rg.
DR PANTHER; PTHR43505; PTHR43505; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF17915; zf_Rg; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF56712; SSF56712; 1.
DR TIGRFAMs; TIGR01054; rgy; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Helicase; Hydrolase; Isomerase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Repeat;
KW Topoisomerase; Zinc; Zinc-finger.
FT CHAIN 1..1156
FT /note="Reverse gyrase 1"
FT /id="PRO_0000158094"
FT DOMAIN 90..277
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT DOMAIN 574..736
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT ZN_FING 10..31
FT /note="C4-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT ZN_FING 658..675
FT /note="C4-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT REGION 580..1156
FT /note="Topoisomerase I"
FT MOTIF 184..187
FT /note="DEAD box"
FT ACT_SITE 895
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 103..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 580
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 705
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 705
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 707
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
SQ SEQUENCE 1156 AA; 132084 MW; 5FA00E0E8F2B6FDB CRC64;
MLKVYYTFGC PNCGGPIDDE HLLAGVPCSK CLPGRVENLD YRVIYDLLVK NSTLKGYAEY
FYDNETFEEI VRIFKRVIGN EPWNLQKYWI KRLAKSESFS LSAPTGLGKT TTLLVYSLFF
SNTTLYVVPT NSLKDQICER LRNMGAKVSC NDVKEEYINV ATFNRILRHY DNYVSLQPKL
VIVDDSDMIL KSGKTTEVMA KILGISEEIF QYAISLIRLK RILKFNEDDK ELKNKIVELE
YKIGSWKPFV QFLVASATLR PKGIKQQALR TLIGFEPSTI QTYLRNIADL YYQGVDIEAI
LDKISDNGGL LLVSKEYGRE KMLELKEIIE KRGYSTGLAI SGRKFLNKFT EGKIDYLIGS
ASYYGVAVRG LDEPKRLKYV IFYGIPKIRL NLTDALNNPS LIVKIGELLN IDVKDIRRKL
LFLSPPEFQI LRYSLMKDEE LSGKLKDIKV NLINIKEKIW DVLKSDNIKK LKADTFLVTE
NNGKYYVYIP DTVTYIQASG RSSRIISNGL TFGISIVLVD NIDLLDILSQ KLKKIIPNFM
FKNINEVDIR ELKSLAVSSR EVSTSQKKKI NIKTILLIVE SPTKAKTIAR LFGRPSRREV
HGIPVYETII LVNDEILITN IIATKGHITD LTTENIGYYG VEVGNNEFNA YYSPIYKCYN
CGKTFTIKSN TCPYCGSVFI SSSEKVVSAL RKLSTEVDEI YIASDPDQEG EKIAYDVAML
ISPYNKNIYR IKYHEITRNG ILNAILNKGK INMNLVKSQI VRRIEDRWIG FELSLALKSM
FYERNHGSGR VQGPVLSWIV ERTKEYKKNY GWILYIKLGD YAIKKFFRIK EEANKFIEKL
NIKINLISER KEIQNPLPPF TTDSLLMDAY DKLGIGSQIV MKIAQDLFES GLITYHRTDS
THVSALGISI AKEYLESKNL NDSFSGRSWG NEGTHEAIRP TSSMDTESLI KDIEDNPNKY
FIKFTKYHLR IYDLIFRRFI ASQMKPAEVT YSKFEIFING EKLEVELPTK ISGGFSIIYP
LKTYVVSEKY STYLTKGSII PLFTYAEIIK NMKEKEIGRP STYAKTISAL IRHGYVVESK
RKALLIATNK GIKAYEFLSS CCSDLISENR TKLLLQKIDK IANGDVNVDY VLEDLHKEIT
QISGKLVNSL KLDTNV
