(data stored in SCRATCH3701 zone)

HOGENOM6: DESB2_1_PE261

ID   DESB2_1_PE261                        STANDARD;      PRT;   834 AA.
AC   DESB2_1_PE261; E1QGC8;
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;Flags: Precursor;
DE   (DESB2_1.PE261).
GN   OrderedLocusNames=Deba_0263;
OS   DESULFARCULUS BAARSII DSM 2075.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfarculales;
OC   Desulfarculaceae; Desulfarculus.
OX   NCBI_TaxID=644282;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DESB2_1.PE261.
CC       Desulfarculus baarsii DSM 2075 chromosome, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:E1QGC8_DESB2
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; E1QGC8; -.
DR   EMBL; CP002085; ADK83640.1; -; Genomic_DNA.
DR   RefSeq; YP_003806234.1; NC_014365.1.
DR   GeneID; 9492702; -.
DR   GenomeReviews; CP002085_GR; Deba_0263.
DR   KEGG; dbr:Deba_0263; -.
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; DESB2_1.PE261; -.
DR   PRODOM; DESB2_1_PE261.
DR   SWISS-2DPAGE; DESB2_1_PE261.
KW   DNA gyrase, A subunit;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   834 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLPKDARKED VRIEEEIRRS YLDYAMSVIV GRALPDARDG LKPVHRRILF AMRELRNDFN
     KPYKKSARVV GDVIGKYHPH GDSAVYDALV RMAQDFAMRY TLVDGQGNFG SVDGDAAAAM
     RYTEVRMAKL ANELLADIDK DTVDFTDNYD GSLKEPVVLP TKAPALLING SSGIAVGMAT
     NIPPHNLGEV ARALVALLDN PDIGVRELMR HVPGPDFPTR GFIHGAEGIE QAYRDGRGSI
     QIRAKANIET VARTKKTSII VTELPYQVNK ARLLEKVAEL VKDKKIEGIS DLRDESDRDG
     MRVVFDLRRD AVPQVVLNQL FKFTQMQTTF GINMLAIDRG RPRLMGLKDV LELFIEHRRE
     IVLRRTAFDL AKAEARAHIL EGLRIALDNL DEVIELIRAA KNPAEAKDGL MSRFSLSEKQ
     AQAILEMRLQ RLTGLERDKI MAEYREVIKE IARLRHILES DEEVRRIIRE ETLLLAEEFG
     DKRRTEIVGR VSDIELEDMI AEEEMVVTLS HGGYIKRTPT SLYRAQRRGG KGSRGMATKD
     EDFVEDLFTA STHSYLLIFT DAGRLYWLKV HEIPQAGRAS RGKAIVNLVQ MLPDESVSTV
     LAVREFVEGR QVIMATQKGV IKKTELMSFS RPRAGGIIAI NLAEGDHLVS ARLTDGEMEV
     FLATRQGQAI RFHESQVRSM GRAAAGVKGI DVEHDDQVVA MEAVAGAPTM LTITENGFGK
     RTRMDEYPAR NRAGKGVITI KTTTRNGHVV SALVVGDDDE VMLITDVGKV IRMKVGGISV
     IGRNTQGVKL IDLEPGERLV AVARLAEPGD DEVEAGELPD EDDEIVAGPE PEDE
//

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