(data stored in SCRATCH3701 zone)

HOGENOM6: CLOBJ_1_PE7

ID   CLOBJ_1_PE7                          STANDARD;      PRT;   846 AA.
AC   CLOBJ_1_PE7; C1FPH9;
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; (CLOBJ_1.PE7).
GN   Name=gyrA; OrderedLocusNames=CLM_0007;
OS   CLOSTRIDIUM BOTULINUM A2 STR. KYOTO.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536232;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CLOBJ_1.PE7.
CC       Clostridium botulinum A2 str. Kyoto, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C1FPH9_CLOBJ
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; C1FPH9; -.
DR   EMBL; CP001581; ACO83422.1; -; Genomic_DNA.
DR   RefSeq; YP_002802320.1; NC_012563.1.
DR   STRING; C1FPH9; -.
DR   GeneID; 7768126; -.
DR   GenomeReviews; CP001581_GR; CLM_0007.
DR   KEGG; cby:CLM_0007; -.
DR   OMA; TGRGRIY; -.
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; CLOBJ_1.PE7; -.
DR   PRODOM; CLOBJ_1_PE7.
DR   SWISS-2DPAGE; CLOBJ_1_PE7.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   846 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLNEGKILPV DVSKEMKKCY IDYAMSVIAG RALPDVRDGL KPVHRRIIYS MQGLGLAPEK
     GYRKCARIVG DVLGKYHPHG DTAVYEALVR MAQNFSIRYT LVDGHGNFGS VDGDGAAAMR
     YTEAKMSKIS MELIKDINKN TVDFIPNFDG EEEEPSVLPS RFPNLLVNGS SGIAVGMATN
     IPPHNLTEVI DGIIMLIENE DVNILDLMTK IKGPDFPTSG LIVGTRGIRE AYETGRGKVI
     IRAKAEIEEE KGKNKIIVTE IPYQVNKARL IENMANLVKD KKINGISDLR DESDRDGMRI
     VIELKRDANP NIVLNQLYKH TKLQDTFGII MLALVNNQPQ ILNLKEILVN YVEFQKEVIR
     RRTRFDLDKA LARAHILEGL RIALDHIDEV IKLIRASKNT AEAKEGLMNN FNLSEKQAQA
     ILDMKLQRLT GLEREKIEEE YKELMEKISY FREILDKEEL VLSIIKEELI EIKNKYGDER
     KTEIVKGEHD IDIEDLIEDK KVIVTLTHGG YIKRLDMDTY SSQKRGGKGI QATSTKQDDF
     IENMFVTSTH STILFFTNRG KVYKLKAYEI PEAGRTAKGT NIVNLIPIEN NEKIQTVIGL
     KDIDDMKHFV MCTRNGIIKK TEISKYSSIR KGGLNAINLR EDDELIDVKM TKGNDEIIVV
     TQNGYCIRFN EEDVRPMGRV ATGVKAITLR KTDKAVSMDV VIEDETLLSI SENGFGKRTD
     IEEYPIHRRG GKGVITYKIT DKTGPIVGAR FVKEDDELML VNSGDVAIRI NVSEISKTSR
     NAMGVKLMRT SEEEKIVAIA KIKSEDIIEE EILNEENLNE ENLNEENLNE ENLNEENLNE
     ENLNEE
//

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