(data stored in SCRATCH3701 zone)

HOGENOM6: THEYD_1_PE41

ID   THEYD_1_PE41                         STANDARD;      PRT;   826 AA.
AC   THEYD_1_PE41; B5YGW5;
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; (THEYD_1.PE41).
GN   Name=gyrA; OrderedLocusNames=THEYE_A0041;
OS   THERMODESULFOVIBRIO YELLOWSTONII DSM 11347.
OC   Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Thermodesulfovibrio.
OX   NCBI_TaxID=289376;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS THEYD_1.PE41.
CC       Thermodesulfovibrio yellowstonii DSM 11347, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:B5YGW5_THEYD
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; B5YGW5; -.
DR   EMBL; CP001147; ACI20689.1; -; Genomic_DNA.
DR   RefSeq; YP_002247895.1; NC_011296.1.
DR   STRING; B5YGW5; -.
DR   GeneID; 6943235; -.
DR   GenomeReviews; CP001147_GR; THEYE_A0041.
DR   KEGG; tye:THEYE_A0041; -.
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; THEYD_1.PE41; -.
DR   PRODOM; THEYD_1_PE41.
DR   SWISS-2DPAGE; THEYD_1_PE41.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Reference proteome; Topoisomerase.
SQ   SEQUENCE   826 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPNVLKVNIE EEMKTSYLDY AMSVIIGRAL PDVRDGLKPV QRRILYAMFR EGLLAGKKYS
     KCAGVVGEVL KKYHPHGDQA VYDALVRLAQ DFNMRYPLID GQGNFGSIDG DPPAAYRYTE
     ARLTKIAEEL LQDIDKETVP FAPNFDATTQ EPLVLPARIP NLLINGSSGI AVGMATNIPP
     HNLNEIVDAL IKLLENPQIS MEELLEFVKG PDFPTGGTIY GIEGIRDLYL TGRGLIRIRA
     KVKIERETKG KKSKEVPLFE IEPEGKAFKE KIIITEIPYQ VNKAKLIEKI AELVREKKIE
     GITEIRDESN REGIRVVLEL KKGEMPEVVL NNLYKHTQME TTFGGILLAI VDGQPRILNL
     KEALWEFLKH RKDVVIKRTA FDLKKAEHQA HILLGLKIAV ENLDEVISII RKSQNPEEAK
     MKLMNRFPLT EIQAQAILDM RLQRLTGLER EKIIQDYETI LKEIERLKAI LESEELVRNI
     IKDELIEIKQ KYGDERKTEI VTETKEINIE DLITQEDMVI TLTHLGYIKR TSLSDYRSQK
     RGGKGLTPME TVTDDYLESV LIGSTHDHIM FFSNFGRVYC LKVYQIPEAG RVSKGKAIVN
     LLPLQEGEKI TTALVCKDIE EGYLMMFTKK GFVKKTSLEE FKNIRQKGVI AIDLEEGDEL
     ISVRKTTGNN QLIIATKMGM AVRFSEIDVR PMGRTARGVI GIRFSEPEDE VVSADVVSEG
     SFVLTITEKG IGKKTPIEEY RLQHRGGTGV KNIKLSLKTG NVVSSLQVKE DDEIIICSSS
     KMIRLKVSQI RPQGRATTGV RLIDLSADDT VVSMGRILEG EDDVNL
//

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