(data stored in SCRATCH3701 zone)

HOGENOM6: DESAD_1_PE3759

ID   DESAD_1_PE3759                       STANDARD;      PRT;   817 AA.
AC   DESAD_1_PE3759; C6BUN7;
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;Flags: Precursor;
DE   (DESAD_1.PE3759).
GN   OrderedLocusNames=Desal_3786;
OS   DESULFOVIBRIO SALEXIGENS DSM 2638.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=526222;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DESAD_1.PE3759.
CC       Desulfovibrio salexigens DSM 2638, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:C6BUN7_DESAD
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; C6BUN7; -.
DR   EMBL; CP001649; ACS81831.1; -; Genomic_DNA.
DR   RefSeq; YP_002993370.1; NC_012881.1.
DR   STRING; C6BUN7; -.
DR   GeneID; 8093614; -.
DR   GenomeReviews; CP001649_GR; Desal_3786.
DR   KEGG; dsa:Desal_3786; -.
DR   ProtClustDB; PRK05560; -.
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; DESAD_1.PE3759; -.
DR   PRODOM; DESAD_1_PE3759.
DR   SWISS-2DPAGE; DESAD_1_PE3759.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   817 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSQITIEEEL KKSYLEYSLS VIIGRAIPDV RDGLKPVHRR ILYAMHELGN TYNRSYKKSA
     RVVGDVIGKY HPHGDSAVYD ALVRMAQEFS MRDPLVDGQG NFGSIDGDAA AAMRYTEARM
     SKLSSEFLAD LEKKTVDFRD NYDNSLQEPS VLPTKVPNLL LNGTSGIAVG MATNIPPHNL
     GELINGTVHL LDNPECEIED LMDFIKGPDF PTGALCFGGK GLREAYLTGR GSIKIRGVVN
     IEEKKNGRQS IVITEIPYAL NKSSMVEKIA QLVGEGKIEG VSDLRDESDR KGIRVVVDLK
     KGAIADIIIN SLYKFTQLEQ SFGINMMAVN ANRPQLMNLK QILAAFLEHR REVIIRRTRF
     DLDKCEKRAH ILEGLRIALD NIDEVVKIIR GSSNGDEARI GLMDRFELSK VQAQAILDMR
     LQRLTNLEHE KLLEEYAEIL KKIEYFKSIL ANEEVLKGVI RDELVEIKDN YATERKTVLM
     DHNPDDIDIE DLIPDDDAVI TLSRRGYIKR TPLSNYQKQK RGGKGIAGVQ TKDGDFIHTF
     LTTSNHQYLL LFTSKGKMFK IKVHQVPEAS RIARGAHIAN LLPLEKDETI ATAMTMREFE
     EECFFLFVTK SGMIKRSSIA LYRNCRQSGI RAVALKEGDA LITVKEVSAD SEAVLVTRNG
     TSIRFSCQDA RAMGRVASGV KGIALRPGDE VVSGVVTGDE ERVQLLTISE GGYGKRTDID
     QHRIQTRGGK GIISMRVTTK TGKVLGSIMV SPEDEVVLLT SGNKIIRMGV KDVSLVGRAT
     QGVRLVRMDD GDHVVGFDLV QDANEEITSE PEGEESE
//

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