(data stored in SCRATCH3701 zone)

HOGENOM6: MARTH_2_PE487

ID   MARTH_2_PE487                        STANDARD;      PRT;   839 AA.
AC   MARTH_2_PE487; E4TPA1;
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; (MARTH_2.PE487).
GN   OrderedLocusNames=Ftrac_0499;
OS   MARIVIRGA TRACTUOSA DSM 4126.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae;
OC   Marivirga.
OX   NCBI_TaxID=643867;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MARTH_2.PE487.
CC       Marivirga tractuosa DSM 4126 chromosome, complete genome.
CC       Genomes
CC   -!- ANNOTATIONS ORIGIN:E4TPA1_MARTH
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; E4TPA1; -.
DR   EMBL; CP002349; ADR20504.1; -; Genomic_DNA.
DR   RefSeq; YP_004052612.1; NC_014759.1.
DR   GeneID; 10010622; -.
DR   GenomeReviews; CP002349_GR; Ftrac_0499.
DR   KEGG; mtt:Ftrac_0499; -.
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; MARTH_2.PE487; -.
DR   PRODOM; MARTH_2_PE487.
DR   SWISS-2DPAGE; MARTH_2_PE487.
KW   DNA gyrase subunit a;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   839 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAEGENEKII PINIEDEMRG AYIDYSMSVI VSRALPDVRD GLKPVHRRIL FGMQELGLAH
     NRPYKKSARI VGEVLGKYHP HGDSAVYDTM VRMAQPWSLR YQMVDGQGNF GSIDGDSPAA
     MRYTEARLKR IAEEMLTDIN KNTVDFQFNF DDSLKEPTVL PAKVPNLLLN GASGIAVGMA
     TNMAPHNLTE VVNGINAYID NNDITVAELM EHISAPDFPT GAAIYGYQGV KAAFETGRGR
     IVMRAKAEIE VLKSGRERVI VTEIPYLVNK ANMIEKTAAL VNEKKIEGIS DIRDESDRNG
     LRIVYEIRKD AIPNVVLNNL YKYTQLQTSF SVNNVALVKG RPETLNLKDM IKHYVEHRHD
     VIVRRTKYEL EEAQKRAHIL EGYLIALDNL DEVIKLIRES RDPEIARNGL MDKFKLSEIQ
     AKAILDMRLQ RLTGLEREKI IQEYEEIKKL IEYLESVLAD EGLRMNIIKD EMQEIQDRYG
     DERRTEIIHS AEEFTDEDMI PNEDVVITLS HQGYIKRTLL NEYKTQGRGG VGSKGAGSKD
     DDFTELLFVA KTHNYLLIFT ELGKVYWIKV YRLPEGSKTS KGRAIQNLIN IESEDSVRAV
     INVENLDDAD YINNNFLVMC TEKGTIKKTT LEAYSRPRAN GINAISINEG DRLLNVKLTN
     GDNNIIIAAR SGRAIRFHES NVRPMGRTAA GVRGITLKDG KDIVVEMVAI TRENANLLVV
     SEKGYGKRSD IEDYRITKRG GKGVKTLNVT EKTGELVAIK EVIDSDDLMI INKSGITIRM
     AVESLRVMGR ATQGVRLIKV NENDSISSVE KVEKIDEIEE EENVEESPEN SSGEDKTES
//

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