(data stored in SCRATCH3701 zone)

HOGENOM6: RASOL2_1_PE2383

ID   RASOL2_1_PE2383                      STANDARD;      PRT;   885 AA.
AC   RASOL2_1_PE2383; D8NM24;
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, subunit A, type II topoisomerase; EC=5.99.1 3;
DE   (RASOL2_1.PE2383).
GN   Name=gyrA; ORFNames=RCFBP_20580;
OS   RALSTONIA SOLANACEARUM CFBP2957.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=859656;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RASOL2_1.PE2383.
CC       Ralstonia solanacearum CFBP2957 chromosome, complete genome.
CC       96802056..97720880 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:D8NM24_RALSO
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; D8NM24; -.
DR   EMBL; FP885897; CBJ43767.1; -; Genomic_DNA.
DR   RefSeq; YP_003746361.1; NC_014307.1.
DR   GeneID; 9415941; -.
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; RASOL2_1.PE2383; -.
DR   PRODOM; RASOL2_1_PE2383.
DR   SWISS-2DPAGE; RASOL2_1_PE2383.
KW   ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW   Topoisomerase.
SQ   SEQUENCE   885 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDQFAKETLP VSLEEEMRSS YLAYAMSVIV GRALPDVRDG LKPVHRRVLY AMHELNNDWN
     RPYKKSARIV GDVIGKYHPH GDSAVYDTIV RMAQDFSLRY MLVDGQGNFG SVDGDNAAAM
     RYTEIRLSKI AHELLADIDK ETVDFEPNYD GSETEPSILP ARIPNLLING SSGIAVGMAT
     NIPPHNLREV VDGCLHLLRN PEATVDELIE LIPAPDFPTA GIIYGISGVR EGYRTGRGRV
     VMRAKTHFED IDRGQRQAII VDELPYQVNK RTLLERIAEL VTEKRVEGIS DIRDESDKSG
     MRVVIELKRG EVPEVVLNNL YKNTQLQDTF GMNMVALVDG QPRLLNLRQM LECFLLHRRE
     VVTRRTVFDL RKARERGHIL EGLAVALANI DEFIAIIKAA PTPPIAKQEL MGRSWDSGLV
     RDMLSRAESD TVGGRTAYRP EGLLPVFGMQ GDGLYKLSDT QAQEILQMRL QRLTGLEQDK
     IVQEYREVMA QIADLLDILA RPERITAIIV EELTLIRSEF GDERRSQIEH NATELDTEDL
     ITPQDLVVTL SHSGYMKSQP ISEYRAQKRG GRGKQAAATK EDDWIDTLFV ANTHDYILCF
     SNRGRLYWLK VWEVPQGSRN SRGRPIVNMF PLSPGEKINV ILPVKQFDEQ HFVFMATSKG
     TVKKTALTEF SNPRKAGIIA VDLDEGDFLI GADITDGQHD VMLFSDAGKA VRFDENDVRP
     MGRQARGVRG MNLEDGQQVI AMLVAPAETA GEGEQAVAGS VLTATENGYG KRTPISEYTR
     HGRGTKGMIA IQTSERNGKV VAAALVAPED EIMLITTGGV LIRTRVDEIR EMGRATQGVT
     LIAVGEGNKL SGLQRVVESD AEGEDAADGA TESDGEAPSA DTTET
//

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