(data stored in SCRATCH3701 zone)

HOGENOM6: ACISD_1_PE833

ID   ACISD_1_PE833                        STANDARD;      PRT;   904 AA.
AC   ACISD_1_PE833; D8JE86;
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; (ACISD_1.PE833).
GN   OrderedLocusNames=AOLE_04195;
OS   ACINETOBACTER SP. DR1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=436717;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACISD_1.PE833.
CC       Acinetobacter sp. DR1 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D8JE86_ACISD
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; D8JE86; -.
DR   EMBL; CP002080; ADI89736.1; -; Genomic_DNA.
DR   RefSeq; YP_003731109.1; NC_014259.1.
DR   GeneID; 9381259; -.
DR   GenomeReviews; CP002080_GR; AOLE_04195.
DR   KEGG; acd:AOLE_04195; -.
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:InterPro.
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; ACISD_1.PE833; -.
DR   PRODOM; ACISD_1_PE833.
DR   SWISS-2DPAGE; ACISD_1_PE833.
KW   DNA gyrase, A subunit;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   904 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSVSEIRPIA IEDELKHSYL DYAMSVIVSR ALPDVRDGLK PVHRRVLFAM HELGNDYNKA
     YKKSARVVGD VIGKYHPHGD SAVYETIVRM AQDFSLRYLL VDGQGNFGSI DGDSAAAMRY
     TEVRMTKLAH ELLADLEKDT VDWEDNYDGS ERIPQVLPTR VPNLLINGAA GIAVGMATNM
     APHNMTEVVN ACLAYADNPN ISVEGLMEYI TGPDFPTGGI IYGKSGIVDA YRTGKGRLHI
     RGKYHFEEDE KTGRTTIVFT EIPYQVNKAR VIERIAELVK EKKLEGISEL RDESDKDGMR
     IAIDLKRGEN AEVVVNNLFL NTQLENSFSI NMVCLDNGQP KLMNLKDIIA AFIRHRQEVV
     TRRTMFELRK ARERGHILEG LTVALANIDE IIETIKTSAN PAEARERLLA GEWAGGGVIS
     LLEKAGAISV RPDEIEGENP DRPFGLTESI YRLSPTQVGA ILELRLHRLT GLEQDKLHAE
     YTEILGQIAE LTAILNDFNL LMAVIREELA QVLQQYGDGR RTEIIESRID FSREDLIPEE
     QVVLTVSQTG YAKTQPLSDY QAQRRGGRGK SATSMKDDDF IQHLIVASNH ATVLCFTNVG
     KVYRLRVFEV PQASRGAKGR PIVNLLPLDA NETVTAILPL TEFPENHYVF MATASGTVKR
     VDLEQFANIR SNGLRAIELN EEDTLIGVAI TDGNQQIMLF SNEGKAIRFA ETDVRSMGRT
     AKGVRGMRVS FASSTLSEED AEVENDESDD NEDSADLNVV SRIVSLVVVP ETGEVLCASA
     NGYGKRTPVN DFPTKKRGGK GVIAIKTSER NGELVGAVSI DESKELLLIS DGGTLVRTRA
     AEVAMTGRNA QGVRLIRLSE EETLVGVVSI EAVEDEEEFL EGEVDTSEVD GEDAVSTNDD
     VSEE
//

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