(data stored in SCRATCH3701 zone)

HOGENOM6: DEMAR1_1_PE2373

ID   DEMAR1_1_PE2373                      STANDARD;      PRT;   818 AA.
AC   DEMAR1_1_PE2373; E8UAE8;
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; (DEMAR1_1.PE2373).
GN   OrderedLocusNames=Deima_2399;
OS   DEINOCOCCUS MARICOPENSIS DSM 21211.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=709986;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DEMAR1_1.PE2373.
CC       Deinococcus maricopensis DSM 21211 chromosome, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:E8UAE8_DEIML
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; E8UAE8; -.
DR   EMBL; CP002454; ADV68037.1; -; Genomic_DNA.
DR   RefSeq; YP_004171702.1; NC_014958.1.
DR   GeneID; 10151760; -.
DR   GenomeReviews; CP002454_GR; Deima_2399.
DR   KEGG; dmr:Deima_2399; -.
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; DEMAR1_1.PE2373; -.
DR   PRODOM; DEMAR1_1_PE2373.
DR   SWISS-2DPAGE; DEMAR1_1_PE2373.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   818 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSSTLPVDIT NEVKTNFINY AMNVIVDRAL PDVRDGLKPV HRRIMYAMLQ EGLFSNQKHA
     KSAAVVGEVM KKYHPHGDSP IYDAMVRLGQ WWNMRYPMVD PQGNFGSIDG DMAAAMRYTE
     ARMTKLAEEL LADLEKETVD LKPNYDETTT EPSVLPSAVP NLLVNGSAGI AVGMATNIPP
     HNLTEIVNGL ISIIDKPGRT AEEKAAQVSL DELMVHVQGP DFPTGGRISR SGIRDAYATG
     HAGLKVRGKA RIDEKNGRTQ IIISEIPYQV NKTNLIQTIS AMYKAGKIPD ISALRDESDR
     KEPVRIVVEL KRGAIPTLVL NQLYKYTQLQ TTFTVINLSI VNGEPKVLPL LDTMRYFLEH
     RADVVTRRTA YELRKAQERA HILEGLLKAL DHIDEVIALI RRSQTGAEAR DGLMTRFQLT
     DVQAQAILDM RLQRLVGLER EKLQGEYNEL MTLIDRLKAI LGDEKLLWRE IKKELKDIRD
     RYGDERRSTI TQLEEDISKE DLIAVEDMVI TMTRAGYLKR TKLDAYRAQS RGGRGSSGGK
     LREEDVNTRV FVGSTHDYLL FFTDQGRLFH EKIYDLPEAG RDAKGTHIKN LLPGLRENES
     VASVLAIKDF DEAGSFVFAT KRGMIKKTQI RDYGNITSAG LIALNLQDDD GLIGVGIQRD
     GDHIVLATSD GQAMRFGANE VRDTGRATQG VIGIRLRDGD HVVSMAVVPG DDEDSELLAI
     SECGLGKRTP VSDYPSKGRG GLGVITLDVT EKTGKLVALA RVAGDEELMV LTQKGTVIRT
     RVEEVRVTGR NAQGVKIINL GDGDCVISAF PIRKEDEL
//

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