(data stored in SCRATCH3701 zone)

HOGENOM6: NOCDD_1_PE7

ID   NOCDD_1_PE7                          STANDARD;      PRT;   870 AA.
AC   NOCDD_1_PE7; D7B607;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=DNA gyrase, A subunit; EC=5.99.1 3; (NOCDD_1.PE7).
GN   OrderedLocusNames=Ndas_0007;
OS   NOCARDIOPSIS DASSONVILLEI SUBSP. DASSONVILLEI DSM 43111.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptosporangineae; Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=446468;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS NOCDD_1.PE7.
CC       Nocardiopsis dassonvillei subsp. dassonvillei DSM 43111 chromosome,
CC       complete genome.
CC   -!- ANNOTATIONS ORIGIN:D7B607_NOCDD
CC   -!- FUNCTION: DNA gyrase negatively supercoils closed circular double-
CC       stranded DNA in an ATP-dependent manner and also catalyzes the
CC       interconversion of other topological isomers of double-stranded
CC       DNA rings, including catenanes and knotted rings (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA.
CC   -!- SUBUNIT: Made up of two chains. The A chain is responsible for DNA
CC       breakage and rejoining; the B chain catalyzes ATP hydrolysis. The
CC       enzyme forms an A2B2 tetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- GENE_FAMILY: HOG000076278 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D7B607; -.
DR   EMBL; CP002040; ADH65460.1; -; Genomic_DNA.
DR   RefSeq; YP_003677966.1; NC_014210.1.
DR   GeneID; 9243833; -.
DR   GenomeReviews; CP002040_GR; Ndas_0007.
DR   KEGG; nda:Ndas_0007; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase (ATP-hydrolyzing) activity; IEA:EC.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   InterPro; IPR020899; Arg_repress_C.
DR   InterPro; IPR005743; GyrA.
DR   InterPro; IPR006691; GyrA/parC_pinwhl.
DR   InterPro; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a.
DR   InterPro; IPR013760; Topo_IIA_cen.
DR   Gene3D; G3DSA:3.30.1360.40; Arg_repress; 1.
DR   Gene3D; G3DSA:3.90.199.10; Topo_IIA_A/C_ab; 1.
DR   Gene3D; G3DSA:1.10.268.10; Topo_IIA_A_a; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF56719; Topo_IIA_cen; 1.
DR   TIGRFAMs; TIGR01063; GyrA; 1.
DR   HOGENOMDNA; NOCDD_1.PE7; -.
DR   PRODOM; NOCDD_1_PE7.
DR   SWISS-2DPAGE; NOCDD_1_PE7.
KW   DNA gyrase, A subunit;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   870 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTDANNPDAP EGGDSTVEAP PRVTDRIEPV DIQVEMQRSY LDYAMSVIVG RALPDVRDGL
     KPVHQRVLYA MYDGGYRPDR GYFKCARVVG DVMGNYHPHG DSAIYDTLVR LAQWWSMRMP
     LVDPNGNFGS AGNDPAAAMR YTECKLAPLA MEMLRDIDKD TVDFRPNYDG RSSEPVVLPA
     RFPNLLVNGS SGIAVGMATN IPPHNLREVA DGVNWYLDNP EAQDEELLDA LIARVKGPDF
     PTRGLIVGKR GIEEAYRTGR GSITMRAVVE VEEDKRGRQT LVVTELPYQV NPDNLALKIA
     DLVKDGKITG IADVRDESSG RTGQRLVIVL KRDAVAKVVL NNLYKHTQLQ ETFGANMLAL
     VDGVPRTLRL DQMIRHWVKH QVEVIVRRTR YLLRKAEERA HILRALLRAM DRIDEVINLI
     RASASADQAR TGLMDLLEID DIQARAILDM QLRKLAALER NALTAEYDEL MAQIADYNDI
     LESDTRQRSI IREELGEIVE KYGDERRTHI IPFEGDMRME DFIAEEDVVV TISRGGYAKR
     TRIDNYRAQK RGGKGVRGAQ LKQDDIVQHF FVTTTHNWIL CFTNQGRVYR TKAYELPEAA
     RDARGQHVAN LLPFQPGEEI AQIMALRDYE AAPYLVLATR EGLVKKSRLE DFDSARAAGI
     IAINLREGDE LIAARLVFPD DDLLLISSDA QAIRFPASDE SLRPMGRATS GVIGMRFLED
     DYLLSMDVIR PGDGSTDVLV TTENGYAKRT PSDQYPVQNR GGKGVLTAKV VEARGKLVGA
     LMIDPEVDEV FAITSAGGVI RTGADEVKRS GRTTMGVRLM NLAKGNKIVA VARNAEAAEE
     EAVETAEDAG EANADTAEDV NANAEGNPEA
//

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