(data stored in SCRATCH3701 zone)

HOGENOM6: STANL_1_PE7

ID   STANL_1_PE7                          STANDARD;      PRT;   831 AA.
AC   STANL_1_PE7; D3PTX2;
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; (STANL_1.PE7).
GN   OrderedLocusNames=Snas_0007;
OS   STACKEBRANDTIA NASSAUENSIS DSM 44728.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Glycomycineae; Glycomycetaceae; Stackebrandtia.
OX   NCBI_TaxID=446470;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STANL_1.PE7.
CC       Stackebrandtia nassauensis DSM 44728 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D3PTX2_STANL
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; D3PTX2; -.
DR   EMBL; CP001778; ADD39730.1; -; Genomic_DNA.
DR   RefSeq; YP_003508823.1; NC_013947.1.
DR   GeneID; 8881180; -.
DR   GenomeReviews; CP001778_GR; Snas_0007.
DR   KEGG; sna:Snas_0007; -.
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; STANL_1.PE7; -.
DR   PRODOM; STANL_1_PE7.
DR   SWISS-2DPAGE; STANL_1_PE7.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   831 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDPNQPELE VPEVGAGRIE PVGVEVQMQR SYLDYAMSVI VGRALPDVRD GLKPVHRKIL
     YGMYDGGYRP DRGYVKCSRV VGDVMGQYHP HGDSAIYDSL VRMAQPWSMR YPLIDGQGNF
     GSPGNDPAAA MRYTESRLDP LAMEMLRDID EDSVDFGPNY DGKTTEPEVL PARIPNLLVN
     GSEGIAVGMA TKIPPHNLRE VAAAVNWCLD NTEADEEETL EALIKLVQGP DFPTSALIVG
     RAGIEDAYRT GRGSIRMRAV IEVEEDRKGR PCLVVTEMPY QVNPDNLAER IAELVKDGKL
     NGIADIREES SGRTGMRLVL VLKRDAVAKV VLNNLYKHTQ LQETFGANML ALVDGVPRTL
     NLAQFVRHYV AHQIEVIVRR TKFRLRKAEE RAHILRGLQK ALDQLDAVIA LIRSSPSAEE
     SKTGLMNLLE VDEIQATAIL DMQLRRLAAL ERQKILDELA EIEAKIADLE DILAKPERQR
     QIIKDELGAI VAKWGDERRT KIVPFEGEVN MEDLIAREDV VVTITRGGYA KRTKVDLYRS
     QRRGGKGVSG ATLKQDDLVS HFFVCSTHDW MLFFTNKGRV YRAKAYELPE ASRTARGQHV
     ANLLAFQPDE QIAQVMQISG YDVAPYLVLA TRRGLVKKTK LTDFDSPRTG GVIGINLRDG
     DEVVGAALIN PDDDLLLVSK KAQAIRFMAS DESLRPMGRA TSGVIGMRFV EADELLTMEV
     VRGGMDILVA TSGGYAKRTP VEEYPQQGRG GKGVLTAKIT ERRGNLVGAL SVTPDDELFA
     ITSEGGVIRT PVKPVRRTTD RNTMGVKLMD LPEGVSLLAM ARSADEPDEQ D
//

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