(data stored in SCRATCH3701 zone)

HOGENOM6: DEPRO1_1_PE3225

ID   DEPRO1_1_PE3225                      STANDARD;      PRT;   829 AA.
AC   DEPRO1_1_PE3225; E8RH59;
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; EC=5.99.1 3;Flags: Precursor;
DE   (DEPRO1_1.PE3225).
GN   ORFNames=Despr_3292;
OS   DESULFOBULBUS PROPIONICUS DSM 2032.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobulbaceae; Desulfobulbus.
OX   NCBI_TaxID=577650;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DEPRO1_1.PE3225.
CC       Desulfobulbus propionicus DSM 2032 chromosome, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:E8RH59_9DELT
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; E8RH59; -.
DR   EMBL; CP002364; ADW19419.1; -; Genomic_DNA.
DR   RefSeq; YP_004196710.1; NC_014972.1.
DR   GeneID; 10176046; -.
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; DEPRO1_1.PE3225; -.
DR   PRODOM; DEPRO1_1_PE3225.
DR   SWISS-2DPAGE; DEPRO1_1_PE3225.
KW   DNA gyrase subunit A;
KW   ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW   Topoisomerase.
SQ   SEQUENCE   829 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTEPSIESNQ QPTIAISREL RKSYLDYAMS VIIGRALPDV RDGLKPVHRR TLFAMRELGN
     TYNRPYIKSA RIVGDVIGKY HPHGDTAAYD TLVRMAQDFS MRYPLVDGQG NFGSMDGDSA
     AAMRYTEARM TRLDQELVAD LDKETVDFVP NYDNSLQEPA VLPSRIPNIL INGSEGIAVG
     MATKIPPHNL TEVINGLIAL VDNPEITVHQ LMEIITGPDF PTGGFICGRA GIREAYETGR
     GVIVMRSKTH IEQRGSHGEA IVITEIPFQQ NKAALVEKIA LLMKEKRITS IAEIRDESDR
     HGVRVVLDLR KDEIPDIVIN QLYKMTPLQK SFGIILLCIV NNKPEILNLK QILQHFLAHR
     KTVVYRRTAF ELRKAEERAH ILEGLKIAIT HLDEVVELIR GSANPAEAKE GLILRFELSE
     IQAQTILDMR LQRLTGLERD KIISDYNEIQ AKISWLKQVL ADDNLVVQII REEFEKIREE
     YGDDRRTEII DAPDEILPED LITPEEMVVT VSHTGYIKRN PLTLYRAQRR GGKGVKGMVT
     LEDDFVTSLY TASSLDTFLF FTNKGRVFWR KVYELPLAGR TARGKAIVNL LELGEDEKVA
     AILPVADLAN MDDTVSVLTV TKQGRVKKTF ISEYKRPLRK GKFGLTIRDD DEILSAAITS
     GDDEIFLVTK KGLSIHFHES DVRAMGRLAA GVKGITLGDD DEVVGVAVLK SDASILTVTE
     NGYGKRTAVS EYKLQSRGGK GVFTIKTSER NGNVVGVLPV VDEDQVMLVA NSGKVIRMPM
     DTVRIIGRNT QGVRLINLDE GELVVDMSML AREEGVDLEE DDGEGEYED
//

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