(data stored in SCRATCH3701 zone)

HOGENOM6: THIDA_1_PE948

ID   THIDA_1_PE948                        STANDARD;      PRT;   849 AA.
AC   THIDA_1_PE948; Q3SK89;
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; (THIDA_1.PE948).
GN   OrderedLocusNames=Tbd_0948;
OS   THIOBACILLUS DENITRIFICANS ATCC 25259.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Hydrogenophilales;
OC   Hydrogenophilaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS THIDA_1.PE948.
CC       Thiobacillus denitrificans ATCC 25259, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:Q3SK89_THIDA
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; Q3SK89; -.
DR   EMBL; CP000116; AAZ96901.1; -; Genomic_DNA.
DR   RefSeq; YP_314706.1; NC_007404.1.
DR   ProteinModelPortal; Q3SK89; -.
DR   SMR; Q3SK89; 30-522, 537-843.
DR   STRING; Q3SK89; -.
DR   GeneID; 3672740; -.
DR   GenomeReviews; CP000116_GR; Tbd_0948.
DR   KEGG; tbd:Tbd_0948; -.
DR   NMPDR; fig|292415.3.peg.538; -.
DR   eggNOG; COG0188; -.
DR   OMA; TGRGRIY; -.
DR   PhylomeDB; Q3SK89; -.
DR   ProtClustDB; PRK05560; -.
DR   BioCyc; TDEN292415:TBD_0948-MONOMER; -.
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; THIDA_1.PE948; -.
DR   PRODOM; THIDA_1_PE948.
DR   SWISS-2DPAGE; THIDA_1_PE948.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   849 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MEQFAKETLP VSLEEEMRRS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMNELGNDWN
     KAYKKSARVV GDVIGKYHPH GDTAVYDTMV RMAQDFSLRY PLIDGQGNFG SVDGDNAAAM
     RYTEVRMARI AHELLADLDK ETVDFGPNYD GSEQEPLVLP TKIPNLLING SSGIAVGMAT
     NIPPHNLTDI CNALFALLDA PATDIESLIS IVQAPDFPTA GIIYGLSGVR DGYRTGRGRV
     VMRATCHVED LDKSGGKQAI IIDELPYQVN KANLLIRIGE LVRDKQIDGI ADLRDESDKS
     GMRVYIELKR GENADVVLNN LYKQTQMQDT FGMNMVALID GQPRLLNLKE MLDAFLRHRR
     EVVTRRTVFD LRKARERGHI LEGLAVALAN VDEIVELIKS SETPAIAKER LLGRAWKSAM
     VEEMLARIDP EYSRPVNMGP EFGLHADGYH LSEIQAQRIL EMQLQRLTNL ESDKILAEYK
     EIMAKIADLL DILANPARIT QIIREELTQV RDQFGDGRRS TIVENAQDMS MEDLIKPEEM
     VVTLSHGGYM KSQPLDDYRA QKRGGRGKQA AGTKDEDFIE KMFVANTHDY ILCFSNRGRL
     YWLKVYNVPQ GGRAARGKPI VNLLPLEDGE KISALLPVKT FDDEHYVFMA TANGIVKKTP
     LSEFSRPRTA GIIAVGLDDG DVLCGASITD GRHDVMLFSD SGKAVRFDEN DVRPMGRAAR
     GVIGMKLAKG AKLISLLVAE DENDFVLTAT ENGYGKRTPI AEYTRHARAT QGMIAIQTSE
     RNGKVVAANL VKADDEIMLI TTGGVLIRTR VKEIRAMSRA TQGVTLINLD KGEKLISLEK
     VAETDNEEE
//

If you have problems or comments...

PBIL Back to PBIL home page