(data stored in SCRATCH3701 zone)

HOGENOM6: ACIBL_1_PE4766

ID   ACIBL_1_PE4766                       STANDARD;      PRT;   865 AA.
AC   ACIBL_1_PE4766; Q1IH79;
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; EC=5.99.1 3; (ACIBL_1.PE4766).
GN   OrderedLocusNames=Acid345_4772;
OS   CANDIDATUS KORIBACTER VERSATILIS ELLIN345.
OC   Bacteria; Acidobacteria; Candidatus Koribacter.
OX   NCBI_TaxID=204669;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIBL_1.PE4766.
CC       Candidatus Koribacter versatilis Ellin345, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:Q1IH79_ACIBL
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; Q1IH79; -.
DR   EMBL; CP000360; ABF43771.1; -; Genomic_DNA.
DR   RefSeq; YP_593845.1; NC_008009.1.
DR   ProteinModelPortal; Q1IH79; -.
DR   SMR; Q1IH79; 45-520.
DR   STRING; Q1IH79; -.
DR   GeneID; 4073366; -.
DR   GenomeReviews; CP000360_GR; Acid345_4772.
DR   KEGG; aba:Acid345_4772; -.
DR   NMPDR; fig|204669.6.peg.4748; -.
DR   eggNOG; COG0188; -.
DR   OMA; TGRGRIY; -.
DR   PhylomeDB; Q1IH79; -.
DR   ProtClustDB; PRK05560; -.
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; ACIBL_1.PE4766; -.
DR   PRODOM; ACIBL_1_PE4766.
DR   SWISS-2DPAGE; ACIBL_1_PE4766.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Reference proteome; Topoisomerase.
SQ   SEQUENCE   865 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MADEQNPLLP LPPSGDGGNP QNIQPINIEE EMKRSYLDYS MSVIIGRALP DVRDGLKPVH
     RRILYAMHDM GLLHNRKHVK CAKVVGEVLG KYHPHGDSAV YDAMVRMAQD FSLRYPLVDG
     QGNFGSVDGD PPAAYRYTEA RMTAIAEELL ADIDKDTVDF VANFDDTSAE PLLLPTKVPN
     LLINGSNGIA VGMATNIPPH NLTEIVDACI TIVNNPKSTL DDVLKFVQGP DFPTGGFIHG
     KGGIKNAYQN GRGRFMMRAK VAVEHLPNKD AIVVTEIPYQ VNKSTLIKKI ADLVNDKTID
     EISDVRDESD RDGMRIVIEL KRSAQPEIVL NQLYKHTQMQ ESFSMIFLAV VNNQPKEMGL
     VQALNHFIDH RIDVVRRRTF YLLQKAKDRE HILEGYLMAL DHLDNVIAII RGSSNRADAR
     ENLVAYFTGK KITINTTGKA PKVDPEKPFS TRQADAILEL QLHRLTRLSI DEITSELKDV
     RERIAEYESI LASEKKLRSV IVKELEQIRK DYGDERRTII QDEAAELSLE DLIADEQVAV
     TVSHSGYLKR TPISTYRQQR RGGTGRKGMS TRDEDFVEMM FVASTHAYLL IFTNTGRVYW
     LKVYEVPEIA AAGKGKHIGN LVALQPGESV RAILPVKSLE EESRYVFFTT RKGTVKKTAL
     VDFSNVMARG IIAIGIDKDD ELVAAQLTDS NQIVFLASHE GLAIRFDEAD VRIMGRPAYG
     VRGMDIGAKD YIVGMAITPK ERKKGKNGGA DTANLILSVT ENGYGKRTDV DEYRLQTRGG
     KGVINVKTTE RNGKVVAIML VTEDAEAMVI SQYGKIIRTS TDSIREAGRS TQGVRLLHLE
     PGDKVAAAVV IPDDEKAEAE PTLLQ
//

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