(data stored in SCRATCH3701 zone)

HOGENOM6: THISK_1_PE1196

ID   THISK_1_PE1196                       STANDARD;      PRT;   870 AA.
AC   THISK_1_PE1196; D3S9K8;
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; (THISK_1.PE1196).
GN   OrderedLocusNames=TK90_1204;
OS   THIOALKALIVIBRIO SP. K90MIX.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396595;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS THISK_1.PE1196.
CC       Thioalkalivibrio sp. K90mix chromosome, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:D3S9K8_THISK
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; D3S9K8; -.
DR   EMBL; CP001905; ADC71713.1; -; Genomic_DNA.
DR   RefSeq; YP_003460449.1; NC_013889.1.
DR   GeneID; 8806966; -.
DR   GenomeReviews; CP001905_GR; TK90_1204.
DR   KEGG; tkm:TK90_1204; -.
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; THISK_1.PE1196; -.
DR   PRODOM; THISK_1_PE1196.
DR   SWISS-2DPAGE; THISK_1_PE1196.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   870 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAEFAKEIFP VNLEDEMQQS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMRELGNDYN
     KPYKKSARVV GDVIGKYHPH GDSAVYDAIV RMAQPFSMRY MLADGQGNFG SIDGDSPAAM
     RYTEVRMARI AAELLADIDK ETVDFIDNYD GSETEPAVLP SKFPNLLVNG SAGIAVGMAT
     NIPPHNLREV INACVALIDD PEISIEGLME HVPGPDFPTA GIINGVEGVR EAYRTGRGRV
     LIRARSHVEP LEGGQREAIV VTELPYQVNK ARLTEKIAEL VKEKRIDGIS ELRDESDKDG
     MRLVIELKRG EMAEVVLNHL YMHTQMQNVF GINIVALVDG QPKVLDLRQV LESFLRHRRE
     VVTRRTIFDL RKARERAHIL EGLAIALANI DPVIELIRAA PNPAEAKAGL LARSWPLGVV
     SDMLDRAGAS ASRPEDLAAD YGVGDDGYRL SEAQAQAILD LRLHRLTGLE QDKILDEYRE
     LLDLIEDLLD ILGSGERLQQ EIRNELLAVA EQFGDERRSE IRERQANLTL EDLIGEEDVV
     VTLSHAGYVK YQPVADYRAQ RRGGRGKAAA SFKEEDFVDR LLVANTHDTV LCFSSRGRVY
     WLKVYELPQG SRASRGKPIV NLLPLEADER INAILPVREY DPDHYVFMVT ARGTVKKTPL
     TDFSRRRSTG IIAVDLRDDD YLVDVSLTDG QMDVMLVTTA GKAVRFSEND VRPMGRTACG
     VRGVRMESDH RVIALLNVAE GAALLATENG YGKRTRFDEF PVHRRGGQGV IGIQTEGRNG
     PLVGAARVLE DDEAMLITTG GTLVRTPVDQ IPLIGRNTQG VRLIRLDEGE RLVELARVEK
     LQGEDEDLDD DSDSEDDEST QNTMDNGDPE
//

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