(data stored in SCRATCH3701 zone)

HOGENOM6: CATAD_1_PE7

ID   CATAD_1_PE7                          STANDARD;      PRT;   875 AA.
AC   CATAD_1_PE7; C7QFM3;
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; (CATAD_1.PE7).
GN   OrderedLocusNames=Caci_0007;
OS   CATENULISPORA ACIDIPHILA DSM 44928.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Catenulisporineae; Catenulisporaceae; Catenulispora.
OX   NCBI_TaxID=479433;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CATAD_1.PE7.
CC       Catenulispora acidiphila DSM 44928, complete genome.
CC       (1809 nt) ;
CC   -!- ANNOTATIONS ORIGIN:C7QFM3_CATAD
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; C7QFM3; -.
DR   EMBL; CP001700; ACU68962.1; -; Genomic_DNA.
DR   RefSeq; YP_003110803.1; NC_013131.1.
DR   STRING; C7QFM3; -.
DR   GeneID; 8331330; -.
DR   GenomeReviews; CP001700_GR; Caci_0007.
DR   KEGG; cai:Caci_0007; -.
DR   OMA; TGRGRIY; -.
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; CATAD_1.PE7; -.
DR   PRODOM; CATAD_1_PE7.
DR   SWISS-2DPAGE; CATAD_1_PE7.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   875 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDETPQGDRI DPVDLQTEMQ RSYLDYAMSV IVGRALPDVR DGLKPVHRRV LYAMYDGGYR
     PEKGYYKCAR VVGEVMGIYH PHGDSPIYDT LVRLAQPWSL RMVLVDGNGN FGSPGNDPAA
     AMRYTECKMA PLAMEMVRDI DEDTVDFRPN YDGRSSEPVV LPARFPNLLV NGSTGIAVGM
     ATNIPSHNLR EVNDGVQWFL QNPEATNEEL LEALIERIKG PDFPTGALIV GRRGIEDAYR
     TGRGSITMRA VVNTEEINGR MCLVVTELPY QVNPDNLALK IAELVKDGKV AGIADVRDES
     SSRTGQRLVI VLKRDAVAKV VLNNLYKHTQ LQDSFGANML ALVDDVPRTL SLDAFIRHWV
     THQIDVIVRR TRFRLRKAQE RAHILVGLLK ALDAIDEVVA LIRRSPTVDE ARSGLIELLT
     IDEIQANAIL EMQLRRLAAL ERQRIEAEHN ELMAKIADYT AILESPERQR RIVSEELQAI
     SDKYGDDRRS QLVPYEGDMS IEDLIPEEDV VVTITRGGYT RRTRTDLYRS QKRGGKGVKG
     AQLKQDDIVD HFFVTTTHHW LLFFTNKGRV YRAKAHELPD TARDARGQHV ANLLAFLPDE
     KIAQVLDLRD YEQTPYLVLA TKNGLIKKTP LKDYDSPRSA GVIAINLRED DELIAAELVS
     PEDDLLLVSK QAQGLRFTAT DEALRPMGRA TSGVIGMRFR EDDELLSMDV VRPDTFLFTA
     TSGGYGKRTA VEMFPLRGRG GLGVIAAKTV DERGGLVGAA VVDEGDEVMA ITLSGGVIRT
     RVSEVRPTSR DTMGVRVINL GKGDTVLAIA RNGDPGEVED ELGEEAGAPA EAAGADVVAE
     ARENGAVVEA SEGSEVIDES EGSDESDGSE ASSEE
//

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