(data stored in SCRATCH3701 zone)

HOGENOM6: LEAB4_1_PE845

ID   LEAB4_1_PE845                        STANDARD;      PRT;   837 AA.
AC   LEAB4_1_PE845; E4RR46;
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; (LEAB4_1.PE845).
GN   OrderedLocusNames=Lbys_0895;
OS   LEADBETTERELLA BYSSOPHILA DSM 17132.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Leadbetterella.
OX   NCBI_TaxID=649349;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LEAB4_1.PE845.
CC       Leadbetterella byssophila DSM 17132 chromosome, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:E4RR46_LEAB4
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; E4RR46; -.
DR   EMBL; CP002305; ADQ16641.1; -; Genomic_DNA.
DR   RefSeq; YP_003996994.1; NC_014655.1.
DR   GeneID; 9954741; -.
DR   GenomeReviews; CP002305_GR; Lbys_0895.
DR   KEGG; lby:Lbys_0895; -.
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; LEAB4_1.PE845; -.
DR   PRODOM; LEAB4_1_PE845.
DR   SWISS-2DPAGE; LEAB4_1_PE845.
KW   DNA gyrase subunit a;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   837 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAENNENAEW GGSIIPINIE DEMRGAYIDY SMSVIVSRAL PDVRDGFKPV HRRVLFGMSE
     LGVYHNRPYK KSARIVGEVL GKYHPHGDSS VYDTMVRMAQ DWSLRYPLVD GQGNFGSVDG
     DSPAAMRYTE ARLRRIAEEM LADINKETVD FRGNFDDSLQ EPTVLPSRIP NLLLNGTSGI
     AVGMATNMAP HNLSEVTEGI TAYIDNPEIT IEELMHFIKA PDFPTGGIIY GYGGVKAAFE
     TGRGRVVIRS VANFEVSKTG KEQIVVTEIP YLVNKAAMIE KTAELVNDKK IEGISGIRDE
     SDRQGLRIVY DLKKDAVPNV VLNNLYKYTQ LQTSFSINNV ALVHGKPETL NLKQLIEHYV
     KHRLDVITRR TQYDLREAEK RAHILEGLLI ALDHLDEVIS LIRSSKDPDE ARNGLMEKFA
     LSEIQARAIL DMRLQRLTGL ERDKITEEYK QIKALIEELN AILASEEKKK DLIKADLLDI
     KTKYGDERRS KIEMVGGEFN IEDMIPDDEM LVTVTSQGYI KRTNLSEYKS QSRGGTGSRG
     VKTKDDDYTE HLFMATNHNY LLFFTEKGRL YWLRVFEVPE GNKTSKGRAI QNLINIESDD
     KIRAVLNVKT LSDEDYIKNN YIVMCTQNGI VKKTLLEMYS RPRQNGIIAI NINEGDQLID
     VALTNGNDYI IIAAGQGKAV RFHESGIRPM GRGATGVKGI SLAEDDKAIG MICVNRPDAQ
     LLVVSEKGYG KRSDIEDYRI TSRGAKGVKT LNMSEKVGNL VAIKEVTDED DLMIITTRGI
     AIRMHVSDLR VMGRNTQGVR LIKLNDKDGI ASITRIIREE DEEENAEEGG ETPTAAE
//

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