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Database: UniProt
Entry: D7B319_NOCDD
LinkDB: D7B319_NOCDD
Original site: D7B319_NOCDD 
ID   D7B319_NOCDD            Unreviewed;       828 AA.
AC   D7B319;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   OrderedLocusNames=Ndas_3303 {ECO:0000313|EMBL:ADH68709.1};
OS   Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS   7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS   (Actinomadura dassonvillei).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH68709.1, ECO:0000313|Proteomes:UP000002219};
RN   [1] {ECO:0000313|EMBL:ADH68709.1, ECO:0000313|Proteomes:UP000002219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC   NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC   {ECO:0000313|Proteomes:UP000002219};
RX   PubMed=21304737; DOI=10.4056/sigs.1363462;
RA   Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA   Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT   509).";
RL   Stand. Genomic Sci. 3:325-336(2010).
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   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000256|ARBA:ARBA00008263}.
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DR   EMBL; CP002040; ADH68709.1; -; Genomic_DNA.
DR   RefSeq; WP_013154316.1; NC_014210.1.
DR   AlphaFoldDB; D7B319; -.
DR   STRING; 446468.Ndas_3303; -.
DR   KEGG; nda:Ndas_3303; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_6_1_11; -.
DR   OrthoDB; 9806486at2; -.
DR   Proteomes; UP000002219; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd00187; TOP4c; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR   Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR   Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR   InterPro; IPR006691; GyrA/parC_rep.
DR   InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   InterPro; IPR002205; Topo_IIA_dom_A.
DR   PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 3.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ADH68709.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002219};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          19..474
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   REGION          784..805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          446..473
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        786..803
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   828 AA;  89884 MW;  6C8213BB1D0C8CB1 CRC64;
     MARTTSRPPE DLAEKIIDID VSEEMRGSFL EYAYSVIYQR ALPDARDGMK PVQRRILYQM
     NEMGLRHDRG HVKCARVVGD VMGRLHPHGD TAIYDALVRL SQPFAMRVPL VDGHGNFGSL
     GGDDAPAAMR YTEARLDRAA EQLVASIDEN VVDFRPNYDG QETEPEVLPA AFPNLLVNGA
     SGIAVGMATN MAPHNLGEVV AAARHLIAHP EATLEELTEF VPGPDLPTGG TIVGLDGIRD
     AYRSGRGTFK TRATVSIEKV SARRTGLVVT ELPYSVGPEK VISRIKELVQ SKKLQGISDL
     KDLTDRTQGL RLVIELKNGF NPEAVLEELY RLTPMEESFG INNVALVDGQ PQTLGLRELL
     EVYVNHRLDV VRRRSEFRRA KRQERLHLVD GLLVALLDID RVISLIREAE DTAAARESLM
     GAYDLSEIQA RYILETPLRR LTRFDRMELE TERDKLNKEV DALTAVLESD KKLRRLVSKE
     MGDVAKEFAT PRRTQLRESD GVARSAVIPL EMADQPCHVL MGVHGAIGRS KGPSVPRVYE
     GLRTRHDAVH VSVPTTSRSA VGLVTDLGRM IRVPVVELPE LPDEGGDSPP LASGLDVSEF
     VQLDGDERVV SVVSMDASGP GFALGTRGGV VKRVSPDYPP NKDDFEVVAL KDDDRVVGVT
     QLSTGEEDLA FITSEAQLLR FSASAVRPQG RPAGGVAGVR LSEGARVLWF GAVPSPQDSV
     VVTVSGSSGA LEGTQAGSAK VTPFEAYPVK GRATGGVRCH RYLKGEDTLL FGWIGRSPAR
     AARADGKPVR LPDPIDRRDG SGDALPRAIV TVGSGQTDSG ITVPGAKA
//
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