(data stored in SCRATCH3701 zone)

HOGENOM6: SANKS_1_PE7

ID   SANKS_1_PE7                          STANDARD;      PRT;   883 AA.
AC   SANKS_1_PE7; D1BI12;
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; (SANKS_1.PE7).
GN   OrderedLocusNames=Sked_00070;
OS   SANGUIBACTER KEDDIEII DSM 10542.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Sanguibacteraceae; Sanguibacter.
OX   NCBI_TaxID=446469;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SANKS_1.PE7.
CC       Sanguibacter keddieii DSM 10542 chromosome, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:D1BI12_SANKS
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; D1BI12; -.
DR   EMBL; CP001819; ACZ19986.1; -; Genomic_DNA.
DR   RefSeq; YP_003312820.1; NC_013521.1.
DR   GeneID; 8631646; -.
DR   GenomeReviews; CP001819_GR; Sked_00070.
DR   KEGG; ske:Sked_00070; -.
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:InterPro.
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; SANKS_1.PE7; -.
DR   PRODOM; SANKS_1_PE7.
DR   SWISS-2DPAGE; SANKS_1_PE7.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   883 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTDDLTPEPS TPEILGENGL AIEHGRIQSV DLQLEMQRSY LDYAMSVIVG RALPEVRDGL
     KPVHRRVLYA MYDGGYRPDR AFSKCSRVVG DVMGKFHPHG DTAIYDALVR LVQDWSLRYP
     LVAGQGNFGS PGNDPAAAPR YTECRMAPIA MEMVRDIDKD TVDFQDNYDG RTQEPSILPS
     RFPNLLVNGS SGIAVGMATN IPPHNLREVA EGVQWYLDHP DASPEEVLDS LIRIIKGPDF
     PTGATILGHR GIEDAYRTGR GSITMRAIVN VEEIQNRICL VVTELPYQVN PDTLALKIAE
     LVKDGRVQGI ADIRDETSGR TGQRLVIVLK RDAVAKVVLN NLYKHTQLQD NFGANMLALV
     DGVPRTLSID AFIRHWVAHQ LEVIVRRTAF LLREAESKIH IFRGYLKALD RLDDVIALIR
     RSPDADRARQ GLIEMLDIDE IQATAILNMQ LRRLAALQRQ EIIDEHDKLE KEILEYQDIL
     AKESRQRQIV SDELNELVAK YGDERRTTVL PHAGEVSMED LIAEEEMVVT ITRGGYAKRT
     RSDNYRAQKR GGKGVRGAQL REDDIVDHFF VTTTHHWLLF FTNLGRVYRA KAYELPEGGR
     DAKGQHVANL LAFQPGEKIA QVLDLRDYDV ADYLVLATRR GTVKKTRLSE YDSNRSGGVI
     AINLREDADG QPDELVSARL VDATDDLILV SRKGQSIRFT ASDEAMRPLG RATSGVTGMK
     FREDDELLAM DVVRDGAHLF VVTEGGFAKR TSVDEYRVQG RGGLGIKVAN LVEARGDLVG
     ALVTDEDDEV LVIMERGKIV RSAVNQVHLT GRTTQGVTFA KPDKNDRIIA VARNVERNLG
     DDIDSEESGE GSDGGAVTTS DDQQHPDDAV VTPDLSTGSE EDA
//

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