ID A0A418V7B5_9DEIO Unreviewed; 689 AA.
AC A0A418V7B5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=D3875_10940 {ECO:0000313|EMBL:RJF71998.1};
OS Deinococcus cavernae.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=2320857 {ECO:0000313|EMBL:RJF71998.1, ECO:0000313|Proteomes:UP000286287};
RN [1] {ECO:0000313|EMBL:RJF71998.1, ECO:0000313|Proteomes:UP000286287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K2S05-167 {ECO:0000313|EMBL:RJF71998.1,
RC ECO:0000313|Proteomes:UP000286287};
RA Zhu H.;
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RJF71998.1}.
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DR EMBL; QYUJ01000014; RJF71998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418V7B5; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000286287; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd16928; HATPase_GyrB-like; 1.
DR CDD; cd00329; TopoII_MutL_Trans; 1.
DR CDD; cd03366; TOPRIM_TopoIIA_GyrB; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR000565; Topo_IIA_B.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034160; TOPRIM_GyrB.
DR PANTHER; PTHR45866:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00986; DNA_gyraseB_C; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00433; TOP2c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000286287};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 463..582
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 689 AA; 76210 MW; 5A0D72F0FBDCB3B5 CRC64;
MTQTEELTAT LENETDTQEQ VSEISQITEA ERQKAKADYT AADIQVLEGM DAVRKRPGMY
VQGGTGIDGY HQLLTEIIDN AIDEGLAGYA TEVHITMHED GSATVIDNGR GVPVDIMKGK
NRPAIEVIYS ELHAGGKFGG GAYKVSGGLH GVGSTVVNAL STFLDVVVNK GGKLHHVRFE
QGNLVQPLEV LGDTPRDVKW STKLTFHPDP GIFKEFKNEF DYNRIRNRMR ELAYLTGLKI
VLRDERKELH GGEIKEEVLH EKGGIANFAR ALVTDTDKLL YDQPVTMNGN HSDVNVRVAF
IHANTYASDN ILTYANMIRT RDGGTPITGF KMAYTRVLNK YAKEKNLIKA GNPLPSGDDL
LEGIYCVVSV EVGDPQFESQ AKVKLLNSEA QTAVNAIVGE KFAEFLEENP KVGKTIVEKA
AEAARARDAA RKARDLVRRA NPLENDDLPG KLADCSSQDP SESELFIVEG NSAGGSAKGG
RERRFQAILP LRGKILNVEK AELNKILKNA EIRSLIGAIG AGVEGTGDRM HFDLSNLRYH
KIVIMTDADM DGGHITTLLL TFFFRYMRPI VEHGYLYIAQ PPLYKITVGA QTKNNKGTYL
FTNEELKVHV AQANKDGKKY EIQRFKGLGE MNAEQLWETT MNPETRVLKK VSIDDLIIAN
EIFDALMGSD VAPRKEFIRE NARFAEISV
//
