(data stored in SCRATCH3701 zone)

HOGENOM6: COXBS_1_PE453

ID   COXBS_1_PE453                        STANDARD;      PRT;   850 AA.
AC   COXBS_1_PE453; Q83E13;
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; (COXBS_1.PE453).
GN   Name=gyrA; OrderedLocusNames=CBU_0524;
OS   COXIELLA BURNETII RSA 493.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Coxiellaceae; Coxiella.
OX   NCBI_TaxID=227377;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS COXBS_1.PE453.
CC       Coxiella burnetii RSA 493, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:Q83E13_COXBU
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; Q83E13; -.
DR   EMBL; AE016828; AAO90070.2; -; Genomic_DNA.
DR   RefSeq; NP_819556.2; NC_002971.3.
DR   GeneID; 1208409; -.
DR   GenomeReviews; AE016828_GR; CBU_0524.
DR   KEGG; cbu:CBU_0524; -.
DR   TIGR; CBU_0524; -.
DR   OMA; TGRGRIY; -.
DR   ProtClustDB; PRK05560; -.
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; COXBS_1.PE453; -.
DR   PRODOM; COXBS_1_PE453.
DR   SWISS-2DPAGE; COXBS_1_PE453.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Reference proteome; Topoisomerase.
SQ   SEQUENCE   850 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVMAEAAHEI IPITIEEELK QSYLDYAMSV IVGRALPDVR DGLKPVHRRV LYAMSELGND
     WNKPNKKSAR IVGDVIGKYH PHGDVAVYDT IVRMAQPFSL RYLLIDGQGN FGSVDGDAPA
     AMRYTEIRLS RFAHALMADL DKETVDFAPN YDETEMAPAV LPTRVPNLLI NGASGIAVGM
     ATNIPPHNLN EIINATLALI ENPDLNVEEL MRHIPGPDFP TAGIINGRNG IVQAYKTGRG
     RIYVRAKTEI ETTKSGRSLI VVHELPYQVN KARLLEKIGE LVREKRIEGI SGLRDESDKR
     GMRMVIEVSR GDNAEIVLNN LYAQTQLQTV FGINMVALDN GQPRVLNLKQ LLSAFLQHRR
     EVVTRRTLFE LRKARERAHI LEGLGVALAN IDEVIALIKK AKTPAIAKEN LLAQAWKPGA
     VADFLKKAGS DRTRPDDLAA EFGLRKEGYY LSPAQAQAIL DLRLHRLTGL ETDKIREEYI
     AIIDKIEELI AIVSDPDKLH EVIREELIAV KEQFGDERRT VIIDDHSDLT HEDLIPEEHR
     VVTLSHEGYI KSQSLSSYQA QHRGGRGKLA AAVKEQDFVK NILVANSHDT ILCFSTQGKV
     YWLKVYQVPQ GSRIARGRPI INLLPLVKDE QISAILPIRA YDGSHFVFMA TAQGAIKKVS
     LAEFSQPRTK GKIALALNEG DRLVGVDITD GKKEIMLVTD AGKAIRFHEK EVREMGRSAR
     GVRGIKLKAK QNVIALIVVK PKGNILTATV HGYGQRTALD DYRSTGRGGQ GVMAIRINSR
     NGKVVSAAQV FDDDDVLLIS DKGTLVRTRV NEISQMGRNT QGVRLIQLSQ DELLVGMEAI
     SAELIEEPSP
//

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