(data stored in SCRATCH3701 zone)

HOGENOM6: THECD_1_PE7

ID   THECD_1_PE7                          STANDARD;      PRT;   839 AA.
AC   THECD_1_PE7; D1ADA6;
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; (THECD_1.PE7).
GN   OrderedLocusNames=Tcur_0007;
OS   THERMOMONOSPORA CURVATA DSM 43183.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptosporangineae; Thermomonosporaceae; Thermomonospora.
OX   NCBI_TaxID=471852;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS THECD_1.PE7.
CC       Thermomonospora curvata DSM 43183 chromosome, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:D1ADA6_THECD
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; D1ADA6; -.
DR   EMBL; CP001738; ACY95616.1; -; Genomic_DNA.
DR   RefSeq; YP_003297654.1; NC_013510.1.
DR   GeneID; 8601297; -.
DR   GenomeReviews; CP001738_GR; Tcur_0007.
DR   KEGG; tcu:Tcur_0007; -.
DR   OMA; EEYSAQG; -.
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; THECD_1.PE7; -.
DR   PRODOM; THECD_1_PE7.
DR   SWISS-2DPAGE; THECD_1_PE7.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   839 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTEVTTGGSG PGERIEPVDI QVELQRSYLD YAMSVIVARA LPEVRDGLKP VHRRVLYAMY
     DGGYRPDRGY FKCARVVGDV MGNYHPHGDS AIYDTLVRLA QPWAMRYPLV DGNGNFGSRG
     NDPAAAMRYT ECRLAPLAME MLRDIDKETV DFSPNYDGRS TEPDVLPARF PNLLVNGSAG
     IAVGMATNIP PHNLREVTEG VFWYLDNYHV SDEELLDALI ERIKGPDFPT AALIVGRKGI
     EDAYRTGRGS ITMRAVVEIE EIQGRTCLVV TELPYQVNPD NLALKIAELV KEGKLEGIAD
     VRDETSGRTG QRLVIVLKKD AIAKVVLNNL YKHTQLQETF GANMLALVDG VPRTLRLDQF
     IRYWVDHQID VIVRRTRFLL RKAEERAHIL RALLRALDRI EEVIALIRGS ESAQAAQEGL
     MALLQIDEVQ AQAILDMQLR KLAALERQAI TDEYERLMAE IADFNEILAS PERQRRIVRE
     ELEPIVERYG DERRTQIVPF DGDVSYEDLI PEEDIVVTIT RGGYAKRTRV DAYREQKRGG
     KGVRGAQLKQ DDIVEHFFVT TTHHWLLFFT NKGRVYRAKA YELPEGGRDS RGQHVANMLA
     FQPEEHIAEV LDLRDYDVAP YLVLATRQGK VKKTALKDFD SPRTGGIIAI NLAEGDEVIA
     ARLVFPTDDL LLVGTNAQAI RFHADDEQLR PMGRATSGVI GMRFDTGHLL DMHVIRDGDE
     DVLVATEGGY AKRTPVEQYP VQGRGGKGVL TAKIVQARGK LVGALMVRPE DGVFAMTSNG
     GVIRTNAGEI KRSGRQTMGV RLMNLAEGDS VVAIARNVES SMEEEPEAGD PQTAEGKPQ
//

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