(data stored in SCRATCH3701 zone)

HOGENOM6: CLOSD_1_PE6

ID   CLOSD_1_PE6                          STANDARD;      PRT;   817 AA.
AC   CLOSD_1_PE6; E3PQZ2;
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 (CLOSD_1.PE6) (Type II topoisomerase), subunit
DE   A; EC=5.99.1 3; .
GN   Name=gyrA; OrderedLocusNames=CLOST_0006;
OS   CLOSTRIDIUM STICKLANDII DSM 519.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=499177;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CLOSD_1.PE6.
CC       Clostridium sticklandii DSM 519, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:E3PQZ2_CLOSD
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; E3PQZ2; -.
DR   EMBL; FP565809; CBH20138.1; -; Genomic_DNA.
DR   RefSeq; YP_003935043.1; NC_014614.1.
DR   GeneID; 9856030; -.
DR   GenomeReviews; FP565809_GR; CLOST_0006.
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; CLOSD_1.PE6; -.
DR   PRODOM; CLOSD_1_PE6.
DR   SWISS-2DPAGE; CLOSD_1_PE6.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   817 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSEEKNEMID KIVDIEIEDE MRKSYIDYAM SVIVGRALPD VRDGLKPVHR RILFAMNDLG
     LVPEKSYRKS ATVVGDVLGK YHPHGDTAVY DAMVKLAQDF STRYPLVNGH GNFGSIDGDS
     AAAMRYTEAK MQKLTLELLK DIDKETVDFT LNYDERLKEP SVLPARYPNL LVNGSNGIAV
     GMATSIPPHN LREVIDAVVE LIDNEEATVE DMMKHIKGPD FPTGATIMGK GSIRDAYMTG
     RGKVTVRSKA DIEELPNGKS QIIVTEIPYQ VNKARMIEKI ADLVKDKRIE GITDLRDESN
     RDGIRIVIEV RRDVNPNIVL NNLYKHSQLQ DVFSIIMLSL VNGEPKVLNI RDMLVHYLNH
     QKNVVRRRTE YDLRKAKERA HILEGLIIAL DNIDRVIKII RGSDNGSIAK EKLTEEFGLS
     DIQSQAILDM RLQRLTGLER GKIEEEFAEL MKNIAYYESI LQDQSILLGI IKDEMLKIRE
     KHGDKRRTEI TEAADEINIL DTIPDEEVTV TFTHYGYIKR IPMDTYKAQR RGGKGITSMT
     TRDDDFVEKL LLTTNHSLIL FLTNRGRIYR LNAYEIPQSG RIAKGTNIVN LIPLEKNEKV
     TSFISIRDVP AENYLVMCTK KGVIKKTQIS EFRKSTRNGL IAISLREDDE LINVKTTDGE
     QDFIIVTKKG MAISFDEKQV RDMGRAAMGV RAIRLAPDDE VVAMELVDPN KQLLVISEKG
     YGKRTNTKDY RLQTRGGKGV KTYKISEKTG ILVGAKAVYK DEEIMIINSD GSLIRMSVNQ
     ISILSRVTSG VKVMRTDENS LVVALARIVV PKEDENI
//

If you have problems or comments...

PBIL Back to PBIL home page