(data stored in SCRATCH3701 zone)

HOGENOM6: CHRSD_1_PE2154

ID   CHRSD_1_PE2154                       STANDARD;      PRT;   907 AA.
AC   CHRSD_1_PE2154; Q1QVI9;
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; (CHRSD_1.PE2154).
GN   OrderedLocusNames=Csal_2168;
OS   CHROMOHALOBACTER SALEXIGENS DSM 3043.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CHRSD_1.PE2154.
CC       Chromohalobacter salexigens DSM 3043, complete genome.
CC       1..43554 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:Q1QVI9_CHRSD
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; Q1QVI9; -.
DR   EMBL; CP000285; ABE59519.1; -; Genomic_DNA.
DR   RefSeq; YP_574218.1; NC_007963.1.
DR   ProteinModelPortal; Q1QVI9; -.
DR   SMR; Q1QVI9; 30-523.
DR   STRING; Q1QVI9; -.
DR   GeneID; 4026662; -.
DR   GenomeReviews; CP000285_GR; Csal_2168.
DR   KEGG; csa:Csal_2168; -.
DR   NMPDR; fig|290398.4.peg.2634; -.
DR   eggNOG; COG0188; -.
DR   OMA; TGRGRIY; -.
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; CHRSD_1.PE2154; -.
DR   PRODOM; CHRSD_1_PE2154.
DR   SWISS-2DPAGE; CHRSD_1_PE2154.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   907 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MGEIAREILP VNIEDELKQS YLDYAMSVII GRALPDVRDG LKPVHRRVLF AMHELGNDWN
     KAYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQEFSMRY VLVDGQGNFG SIDGDSAAAM
     RYTEVRMSRL AHELLADLEK DTVDWVDNYD GTERIPEVLP TKVPNLLVNG ASGIAVGMAT
     NIPPHNMREI IDGCLALIDD YTLSIDDLMA YIPGPDFPTG GIINGRAGIL EAYRTGRGRI
     YVRARHTIEH DEKTGRDHII VTELPYQVNK ARLIEKIAEL VKDKRIEGIA ELRDESDKEG
     LRVVIEVKRG ESGDVVVNNL FAHTQLQTVF GINMVALDNG QPKILNLKEI LEAFVRHRRE
     VVTRRTLFEL KKARDRGHIL EGLAVAISNI DEVIELIKAS PSAAEAKEKL VARAWRPGQV
     TDMLERAGAT SCKPEDLEEG YGLAEGQNEY RLSPAQAQAI LELRLHRLTG LETEKLLDEY
     LSILKRIAEL NEILASPERL LDVIREELQA IRDQYGDERK TEIQASHLDL TIEDLINEED
     MVVTISRSGY AKTQPLSDYQ AQRRGGRGKS ATTMKDEDII EHLLVASTHD TVLLFSNRGK
     VYWLKVYEMP NASRGSRGKP LINLLPLDEG EAINAILPVR EYREDSYIFF ATAKGTVKRT
     SLEQFSRPRS VGLIAIDLEE DDRLVGAAIT SGNDHAMLLS SNGKAIRFEE GNVRAMGRTA
     RGVRGMRLQG GAEVISLIIP QSLTIDAETD DDAEERPVET VGEDQVYILT ASENGYGKRT
     RLDEFPLRGR GGQGVIAMQT SQRNGALVAA IQVRDSDEMM LITDKGTLVR TRVGEVSVSS
     RNTQGVTLIR TGEGEHLVAT VRVDEPDAVE DDALDAEALD SEEGAATAEA TPTPDDGAPS
     DEAPQDD
//

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