(data stored in SCRATCH3701 zone)

HOGENOM6: ACIC5_1_PE1981

ID   ACIC5_1_PE1981                       STANDARD;      PRT;   861 AA.
AC   ACIC5_1_PE1981; C1F921;
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; (ACIC5_1.PE1981).
GN   Name=gyrA; OrderedLocusNames=ACP_2084;
OS   ACIDOBACTERIUM CAPSULATUM ATCC 51196.
OC   Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC   Acidobacterium.
OX   NCBI_TaxID=240015;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIC5_1.PE1981.
CC       Acidobacterium capsulatum ATCC 51196, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C1F921_ACIC5
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; C1F921; -.
DR   EMBL; CP001472; ACO34051.1; -; Genomic_DNA.
DR   RefSeq; YP_002755139.1; NC_012483.1.
DR   STRING; C1F921; -.
DR   GeneID; 7698960; -.
DR   GenomeReviews; CP001472_GR; ACP_2084.
DR   KEGG; aca:ACP_2084; -.
DR   OMA; QRENVIV; -.
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; ACIC5_1.PE1981; -.
DR   PRODOM; ACIC5_1_PE1981.
DR   SWISS-2DPAGE; ACIC5_1_PE1981.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   861 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNLVPINIEE EMRRSYLDYS MSVIIGRALP DVRDGFKPVH RRILYAMHEM GLQHNKKYTK
     CAKVVGQAMG VYHPHGDSAI YDTLVRLAQP FSLRYPMIDG QGNFGSVDGD PPAAMRYTEC
     RMMRIAGEML ADIDMETVDF TPNYDESTLE PTVLPTKIPN LIVNGSNGIA VGMATNIPPH
     NLTEVINATI EMVNNPHAGL AEVLQHVQGP DFPTGGFIYG RSGIANAYRT GRGRFLMRAK
     ASIEQLPQGR SAIIVTEIPY QVNKAKLIER VADLVNDKVI DEISDIRDES DRDGMRIVIE
     LKRGAEAQIV LNQLYKHTQM QESFSMIFLA VVNGQPRELP LPDAIRHFID HRVDVVRRRT
     AYLLRKARER EHILLGYQIA LDHLDHVIKI IRGSSSRADA RENLFQFFSG RTITVRDEAL
     AGVKLDPQKY AIDPATMIEA TLTLSYRQID AILELQLYRL TQLSIDELLK ELAEVRERIA
     EYESILASEK KLRSVIVKEL EDVRKAYGDE RRTQIVDETA ELQLEDLIAD EQVAVTVSHS
     GYLKRTPIST YRQQKRGGTG RMGMKTREED FVQQLLVDST HAYLLCFTNT GRVYWLKIYE
     IPDVGAAGKG KSIASLLNLQ PGEQVRAIMA VRDLTEEGKF IFFATRNGTV KKTPLKDFSN
     VMARGIIAIG IDEEDELMGA TITDGSQIVF LATHEGMAIR FDENDVRSMG RPARGVRGID
     LGKKDHVVGM AATPKDRGVG DDGKACACLI LSVTQNGYGK RTDVDEYRLQ TRGGKGVINV
     KTTAKNGKVV SIQLVDDTSE LMVISQYGKI IRIDTKGVRA AGRSTQGVRL LNLDTEDKVA
     AAVVIPPEEA KEEPETGTLL Q
//

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