(data stored in SCRATCH3701 zone)

HOGENOM6: RUALB1_5_PE11

ID   RUALB1_5_PE11                        STANDARD;      PRT;   836 AA.
AC   RUALB1_5_PE11; E6UB34;
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; (RUALB1_5.PE11).
GN   OrderedLocusNames=Rumal_0011;
OS   RUMINOCOCCUS ALBUS 7.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminococcus.
OX   NCBI_TaxID=697329;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RUALB1_5.PE11.
CC       Ruminococcus albus 7 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:E6UB34_RUMA7
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; E6UB34; -.
DR   EMBL; CP002403; ADU20575.1; -; Genomic_DNA.
DR   RefSeq; YP_004103209.1; NC_014833.1.
DR   GeneID; 10076235; -.
DR   GenomeReviews; CP002403_GR; Rumal_0011.
DR   KEGG; ral:Rumal_0011; -.
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; RUALB1_5.PE11; -.
DR   PRODOM; RUALB1_5_PE11.
DR   SWISS-2DPAGE; RUALB1_5_PE11.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   836 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDEYNLLNQD VESIMKESFL QYSMAVIVSR ALPDVRDGLK PVHRRILYTM HENGLTPDQA
     YRKCADTVGS VLGRYHPHGD ASVYDALVRL AQSFSLRYPL VDGHGNFGSV DGDPPAAYRY
     TEAKMAKMAV NMLTDIKKDT VDFQSNYDDR LQEPCVLPSR FPNILCNGAV GIAVGMATNI
     PPHNLHEVIE GMKIVIQNPD CTLDELMQAI KGPDFPTGGI IMGRSGIRAA YGTGRGKITL
     RSKTSIEEIK GRNCIVVTEI PYMVNKAKLV ESIAGLVKDK RVEGIHDLRD ETSRDGMRIV
     IELKKDANPQ VVLNKLFSYT QLQDSVGVIL LALVNGIPKI LTLKQILQEY IDFQVSVIRR
     RTEFDLKKAK EREHILQGLV IALDNIDEVI EIMKNSKSIP EAKQKLCTRF GLTDVQADHI
     AQMTLGRLTG MERQKIIDEL AEITATVADL EDILANEQRV FDIIIEEVEA IQEKFGDERR
     TQIENVSGEV DIEDLIPVEE SVVTYTNVGY IKRMPISVYK AQNRGGKGVT GMKQREDDCI
     TEMSVCSSHD NILFITTKGI AYKMKCYELP EGSKASRGVN IKNLLELSDD NLIAAMIKVE
     DFDDDKYIVM VTKRGKIKRT PLSAYKNVRK NGLIAIGLDE GDEIAGVRLT GGQNELLIAT
     HNGMAIRISE NDVRVMSRTA HGVRAIKLRE GDYVVSMARI REGATVLTVS ETGLGRRVAL
     ENYPIRHRGG HGVLNYKNGE VCGIKVVDEE DDIIMISSDG IVIRLRACDI SVMGRYSRGV
     RLMKVAGENK VVTFTRTEHD DEAEIAEVEK ASEEDILKAQ EEEKAEVLEE DTVAED
//

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