(data stored in SCRATCH3701 zone)

HOGENOM6: DENA2_1_PE2815

ID   DENA2_1_PE2815                       STANDARD;      PRT;   828 AA.
AC   DENA2_1_PE2815; D4H6E8;
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; (DENA2_1.PE2815).
GN   OrderedLocusNames=Dacet_2872;
OS   DENITROVIBRIO ACETIPHILUS DSM 12809.
OC   Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae;
OC   Denitrovibrio.
OX   NCBI_TaxID=522772;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DENA2_1.PE2815.
CC       Denitrovibrio acetiphilus DSM 12809 chromosome, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:D4H6E8_DENA2
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; D4H6E8; -.
DR   EMBL; CP001968; ADD69622.1; -; Genomic_DNA.
DR   RefSeq; YP_003505578.1; NC_013943.1.
DR   GeneID; 8877254; -.
DR   GenomeReviews; CP001968_GR; Dacet_2872.
DR   KEGG; dap:Dacet_2872; -.
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; DENA2_1.PE2815; -.
DR   PRODOM; DENA2_1_PE2815.
DR   SWISS-2DPAGE; DENA2_1_PE2815.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   828 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDTSKTIDI SIEESVKNSY LDYAMSVIIG RALPDVRDGL KPVHRRALFS MSEMGVHYNK
     AYKKSARIVG DVIGKFHPHG DSAVYDTIVR MAQDFSLRYP LVDGQGNFGS VDGDSAAAMR
     YTEIRLSKIS DDLLADLDKD TVDFSENYDG TMVEPTVLPT RIPALLVNGT SGIAVGMATN
     IPPHNITEII SALNYMIDEP GYDTEGILRH VSGPDFPTAG IIMGSKDIQT AYRTGRGSIT
     IRARVLIEET KTGKPVIIVR EIPYLVNKAS MIEKIADLVQ EKKITGITDL RDESDKDGIR
     VVIELKKGEN VDVVLNRLYK FTQLQTSFGF NMVAIVDGKP QTLSLREILE EFLKHRVTVV
     TRRTQFLLRK AEARLHILEG LIKAVENIDE VIKTIKASKD TPAAKANLCA QFGFTEIQAQ
     SILEMRLQKL TGLEIEKLKE EYENILKDIE YYKSILGNRS VMMSVIKDEL QDVLDKYGDD
     RRTEIAPGLT EFEDEDLIPN NEKVVTMTHN GYIKATLLSS YVAQKRGGKG KTGAGSKDED
     FVERLIVTTN HTRLMFFTNT GKVHYLKVYA LPEAQRDAKG RHISNLLTLE PEEFVASVLA
     LPAETDGKYL FFATKSGTIK KTSLEEFKSG RSGIVAIKLR DGDEILTADI TTDEDTVILS
     TKAGKTIQFS STDARPMGRS TSGVRGITLE ARDELMSMEV LTGAPYILSV TSAGYGKRTP
     VDEYRVQTRG GKGLKLCRVS PKTGFVVGAK QVTDNDDVMI ITRSAKTIRT EVQGISKMGR
     DTMGVKLMDT GDDDIIAFAV IKEGTIHEDS DNNEREGTGS EGQGGTED
//

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