(data stored in SCRATCH3701 zone)

HOGENOM6: RASOL3_2_PE2407

ID   RASOL3_2_PE2407                      STANDARD;      PRT;   885 AA.
AC   RASOL3_2_PE2407; D8NWC4;
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   (RASOL3_2.PE2407).
GN   Name=gyrA; ORFNames=RPSI07_2483;
OS   RALSTONIA SOLANACEARUM PSI07.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=859657;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RASOL3_2.PE2407.
CC       Ralstonia solanacearum PSI07, complete genome.
CC       96802056..97720880 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:D8NWC4_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; D8NWC4; -.
DR   EMBL; FP885906; CBJ51849.1; -; Genomic_DNA.
DR   RefSeq; YP_003753116.1; NC_014311.1.
DR   GeneID; 9408888; -.
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; RASOL3_2.PE2407; -.
DR   PRODOM; RASOL3_2_PE2407.
DR   SWISS-2DPAGE; RASOL3_2_PE2407.
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 ETVNFEPNYD GSETEPSILP ARIPNLLING SSGIAVGMAT
     NIPPHNLREV VDGCLHLLRN PDATVDELIE LIPAPDFPTA GIIYGISGVR EGYRTGRGRV
     VMRAKTHFED IDRGQRQAII VDELPYQVNK RTLLERIAEL VTEKRVEGIS DIRDESDKSG
     MRVVIELKRG EVPEVVLNNL YKNTQLQDTF GMNMVALVDG QPRLLNLRQM LECFLLHRRE
     VVTRRTVFDL RKARERGHIL EGLAVALANI DEFIAIIKAA PTPPIAKQEL MGRSWDSGLV
     REMLSRAESD TAGGRAAYRP EGLLPVFGMQ DDGLYKLSDT QAQEILQMRL QRLTGLEQDK
     IVQEYREVME QIADLLDILA RPERITAIIV EELTLIRAEF GDERRSQIEH NATELDTEDL
     ITPQDLVVTL SHSGYMKSQP ISEYRAQKRG GRGKQAAATK EDDWIDTLFV ANTHDYILCF
     SNRGRLYWLK VWEVPQGSRN SRGRPIVNMF PLSPGEKINV ILPVKQFDEQ HFVFMATSKG
     TVKKTALTEF SNPRKAGIIA VDLDEGDFLI GADITDGQHD VMLFSDAGKA VRFDENDVRP
     MGRQARGVRG MNLEEGQQVI AMLVAPAETA GEGEQAVAGS VLTATENGYG KRTPISEYTR
     HGRGTKGMIA IQTSERNGKV VAAALVAPED EIMLITTGGV LIRTRVDEIR EMGRATQGVT
     LIAVGEGNKL SGLQRVVESD AEGEDAADSG AESDGDAPGA DTAET
//

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