(data stored in SCRATCH3701 zone)

HOGENOM6: THEFY_1_PE7

ID   THEFY_1_PE7                          STANDARD;      PRT;   848 AA.
AC   THEFY_1_PE7; Q47U17;
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; (THEFY_1.PE7).
GN   OrderedLocusNames=Tfu_0007;
OS   THERMOBIFIDA FUSCA YX.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptosporangineae; Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS THEFY_1.PE7.
CC       Thermobifida fusca YX, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:Q47U17_THEFY
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; Q47U17; -.
DR   EMBL; CP000088; AAZ54047.1; -; Genomic_DNA.
DR   RefSeq; YP_288070.1; NC_007333.1.
DR   ProteinModelPortal; Q47U17; -.
DR   SMR; Q47U17; 40-502.
DR   STRING; Q47U17; -.
DR   GeneID; 3579768; -.
DR   GenomeReviews; CP000088_GR; Tfu_0007.
DR   KEGG; tfu:Tfu_0007; -.
DR   NMPDR; fig|269800.4.peg.36; -.
DR   eggNOG; COG0188; -.
DR   OMA; TGRGRIY; -.
DR   ProtClustDB; PRK05560; -.
DR   BioCyc; TFUS269800:TFU_0007-MONOMER; -.
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; THEFY_1.PE7; -.
DR   PRODOM; THEFY_1_PE7.
DR   SWISS-2DPAGE; THEFY_1_PE7.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   848 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTDVNTTPEA PDNTGGRIEP VDLQVEMQRS YLDYAMSVII GRALPDVRDG LKPVHQRVLY
     AMYDSGYRPD RGYFKCARVV GDVMGNYHPH GDSAIYETLV RLAQPWAMRM PLVDGNGNFG
     SPGNDPAAAM RYTECKLAPL AMEMLRDIDK ETVDFRPNYD GRSQEPVVLP ARFPNLLVNG
     SSGIAVGMAT NIPPHNLREV AEGVYWYLDH PDASDEELLD ALIERIKGPD FPTRGRIVGR
     RGIEETYRTG RGSITMRAVV EIEEDKRGRQ CLVVTELPYQ VNPDNLALKI AELVKEGKIS
     GIADVKDESS GRTGQRLVIV LKRDAVAKVV LNNLYKHTQL QETFGANMLA LVDGVPRTLR
     LDQMIRHWVA HQIEVIVRRT RYLLRKAEER AHILRALLKA IDRIDEVIAL IRGSASADDA
     KNGLMELLAI DDVQARAILD MQLRKLAALE RQQLTSEYDE LMAQIADYNE ILESPERQRR
     IIRDELAEIV EKYGDDRRTE IVPYEGDMRM EDFIAEEDIV VTITRGGYAK RTRLDNYRAQ
     KRGGKGVRGA QLKQDDIVQH FFVTTTHHWI LFFTNKGRVY RTKAYELPEL ARDSRGHHVA
     NLVPFLPDEE IAQVLALRDY DAAPYLVLAT RSGLVKKTKL AEFDSARSSG IIAINLREDD
     ELIAARLVYP TDDLLLISSN AQAIRFPASD DSLRPMGRAT SGVIGMRFAE GDYLLSMDVI
     REGEGATDVL VATEGGYAKR TPADQYPVQK RGGKGVLTAR IVESRGKLVG ALMVDPEDEI
     LAITSNGGVI RTKCAEIKQS QRATMGVRLM HLSKGNHVVA IARNTEGMGD DAENGAHGSE
     DAEDTEQD
//

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