(data stored in SCRATCH3701 zone)

HOGENOM6: DESAT_1_PE2060

ID   DESAT_1_PE2060                       STANDARD;      PRT;   837 AA.
AC   DESAT_1_PE2060; D6Z5P0;
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; (DESAT_1.PE2060).
GN   OrderedLocusNames=DaAHT2_2106;
OS   DESULFURIVIBRIO ALKALIPHILUS AHT2.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobulbaceae; Desulfurivibrio.
OX   NCBI_TaxID=589865;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DESAT_1.PE2060.
CC       Desulfurivibrio alkaliphilus AHT2 chromosome, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:D6Z5P0_DESAT
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; D6Z5P0; -.
DR   EMBL; CP001940; ADH86777.1; -; Genomic_DNA.
DR   RefSeq; YP_003691396.1; NC_014216.1.
DR   GeneID; 9258085; -.
DR   GenomeReviews; CP001940_GR; DaAHT2_2106.
DR   KEGG; dak:DaAHT2_2106; -.
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; DESAT_1.PE2060; -.
DR   PRODOM; DESAT_1_PE2060.
DR   SWISS-2DPAGE; DESAT_1_PE2060.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   837 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVETDKPALP PTISIEKELR KSYLDYAMSV IIGRALPDVR DGLKPVHRRV LFAMRELNNY
     YNRPFLKSAR IVGDVIGKYH PHGDSAVYDT LVRMAQSFSM RYPLVDGQGN FGSVDGDPPA
     AMRYTEARMT RIDQDLISDL DKETVDFVPN YDNSMTEPLV LPARIPNLLI NGAAGIAVGM
     ATNIPPHNLR EVIDGLIAMI EDPNITVSAL MEHISGPDFP TGAYICGRAG IREAYETGRG
     SLMLRSRCEV EKQKNGRESI IITEIPYQQN KTTLIERIAL LVKEKKIESI SEVRDESDRQ
     GMRIVLDLKK DENAEVVINQ LYKMTPLQRG YGIILLSIVN NRPEILNLRQ ILEHFILHRK
     TVVYRRTAHD LRKAEEKAHI LEGLKIAITN LDEVVELIKS SANPNEAREG LINRFALSAI
     QAQAILEMRL HRLTGLEREK IIEEYQALMK EIEWLRRVLA DESLVLQIIR QEFEAIREQY
     GDERRTEIIE APDEILPEDM IAREDMVVTV THAGYIKRNP VDLYRAQRRG GKGIRGAGGI
     DDDFISWMHV ASTHDTLLFF TNRGRVFWRK VYEIPQAGRL ARGKAVVNLL DLAPEEKLAA
     ILPVQSFEVP EGRECYILMA TRKGVVKKTT IQEFSRPVRR GKIALTFRED DEILAAALTY
     GDNEILLLSR KGMAVRFHEG DIRPMGRGAT GVRGINLGSA DELVGVSVLS GDPETSILVV
     TENGYGKRTL VDEYRLIRRG GKGVMAIKAS ERNGAVVGML QVTDEDQVMM ITNAGQIIRM
     PMTDLRVIGR NTQGVRLFNL GAEEKVVALD RLAESVNGED EDEPETEPEN EPENGEK
//

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