(data stored in SCRATCH3701 zone)

HOGENOM6: RHOM4_1_PE2162

ID   RHOM4_1_PE2162                       STANDARD;      PRT;   853 AA.
AC   RHOM4_1_PE2162; D0MDS7;
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; (RHOM4_1.PE2162).
GN   OrderedLocusNames=Rmar_2192;
OS   RHODOTHERMUS MARINUS DSM 4252.
OC   Bacteria; Bacteroidetes; Sphingobacteria; Sphingobacteriales;
OC   Rhodothermaceae; Rhodothermus.
OX   NCBI_TaxID=518766;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RHOM4_1.PE2162.
CC       Rhodothermus marinus DSM 4252, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D0MDS7_RHOM4
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; D0MDS7; -.
DR   EMBL; CP001807; ACY49071.1; -; Genomic_DNA.
DR   RefSeq; YP_003291459.1; NC_013501.1.
DR   STRING; D0MDS7; -.
DR   GeneID; 8568855; -.
DR   GenomeReviews; CP001807_GR; Rmar_2192.
DR   KEGG; rmr:Rmar_2192; -.
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; RHOM4_1.PE2162; -.
DR   PRODOM; RHOM4_1_PE2162.
DR   SWISS-2DPAGE; RHOM4_1_PE2162.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   853 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MEAEKPRIIP VNIEEEMKSS YIDYSMSVIV GRALPDVRDG LKPVHRRVLY GMYELGLTAS
     APYKKSARIV GEVLGKYHPH GDAAVYDTMV RMAQDFAMRY PLVDGQGNFG SIDGDSPAAM
     RYTEARLTRL AEEMLRDIDK DTVDFQDNFD GSLKEPVVLP AALPNLIVNG ADGIAVGMAT
     KIPPHNLGEA VDALVAMIDN PDISLDELLK HLPAPDFPTG GIIYGYSGVK EAYATGRGRI
     LIRARIHEEE IRPGRMALVI TEIPYQVNKS SLIEKIAHLV RERRIDGITD IRDESDREGL
     RVVLELRKDA VPLVIQNQLY KYTPCQQTFG VNMVALVNGR PRTLTLKELM RHYLDHRHEV
     VTRRTRFELR KAEERAHILE GLKIALDHLD LVINIIRYSA DPDEARQRLM EGVLPERLTP
     EQRERLGLPV EQISHFTLTE AQANAILALR LSRLTGLERQ KLEEEYRALL QEIERLRSIL
     ASEPLRWQII REELLELKQK YADARRTEID YAGGGDFAIE DLIEDEQVVV TLSHQGLIKR
     TPVHIYRQQG RGGVGMKASG MREDDYIEHL FACKNHDYLL FFTDHGRCYW LRVYDIPEGS
     RTSLGRSIRN LIQIAPDDRV RAVLNIRKED FENPEFLRTH YVLMATRQGL VKKTELEAFS
     RPRADGIIAI AFAEGDELIE AVLTDGRAHV LLASSGGRVV RFDESDVRPM GRNTRGVRGI
     ALETGEQVVG MVAVSPEASP CILSISANGY GKRTPLEEYP VHRRGGKGVW TMKITPRTGR
     LIAIKAVQDT DDLMIITQNG LMIRIHVADI SRMGRHTQGV RLIQLKPGDA IADVTRLVTE
     AQEDEAAAAP AIA
//

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