(data stored in SCRATCH3701 zone)

HOGENOM6: THEAS_1_PE268

ID   THEAS_1_PE268                        STANDARD;      PRT;   816 AA.
AC   THEAS_1_PE268; D1B8A6;
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;Flags: Precursor;
DE   (THEAS_1.PE268).
GN   OrderedLocusNames=Taci_0272;
OS   THERMANAEROVIBRIO ACIDAMINOVORANS DSM 6589.
OC   Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae;
OC   Thermanaerovibrio.
OX   NCBI_TaxID=525903;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS THEAS_1.PE268.
CC       Thermanaerovibrio acidaminovorans DSM 6589, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:D1B8A6_THEAS
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; D1B8A6; -.
DR   EMBL; CP001818; ACZ18509.1; -; Genomic_DNA.
DR   RefSeq; YP_003316791.1; NC_013522.1.
DR   GeneID; 8630082; -.
DR   GenomeReviews; CP001818_GR; Taci_0272.
DR   KEGG; tai:Taci_0272; -.
DR   OMA; QRENVIV; -.
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; THEAS_1.PE268; -.
DR   PRODOM; THEAS_1_PE268.
DR   SWISS-2DPAGE; THEAS_1_PE268.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Reference proteome; Topoisomerase.
SQ   SEQUENCE   816 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MEKGNGSSDL FQKVIPLPLE EEIKHSYIDY AMSVIVGRAL PDARDGLKPV QRRILYAMRE
     LGLRHSQPFK KSARVVGETM GKYHPHGDAA IYETMVRMSQ DFSMRYPLVD GQGNFGSIDG
     DPPAAMRYTE ARLHSLGEEM LADIDEDTVD WLPNFDESLE EPAVLPSRIP NLLVNGSTGI
     AVGMATNMPP HNLREVVDAC CTLLDNPDVE VGELMTHVPG PDFPTGGVIM GRDGIIDAYT
     TGRGKIVVRG CAEIEDAKRG KKAIVITQIP YMVNKSNLIE TIVKGVQAGQ LDGITDVRDE
     SNREGIRLVL ELHRDSDPHL VLRQLYSRTQ LQTTFGVINL ALVDGRPVEL NLKGLLQIFI
     DHRRMVVRRR TQYRLRKAEE RAHILEGLVK ALDMIDMVIA LIRSSEDPLV AKGRLVEELG
     FTEAQAQAIL DMRLQRLTSL EKHKLQEELA ELMAQIARYR LILGDPAELD SVVREELLEV
     KRAYGDERRT VIEDSVDDVS YEDLIPETEV VVAMTRDGFI RRMPLQDYRC QARGGKGVKG
     AAVKGEDEVS LVAVTTTHRS LYLFTDRGRV FSLKCLAIPE PKSGRGKHVS TFISLDEGES
     VVTFRDSALE GARFVFLVTK MGLAKRLPVG ELEGITRAGR RILGLEEDDT IARVRFTGGE
     DQLLLTTAKG QTLRVSETEF RPQGRAAKGV RGIKLDPDDL VVGCDVIMPG RQVLFISQLG
     MGKRTRYEEF TVHHRGGMGV RAMRLGERTG HLVGAWGVAD DDEIMVITSR GRVVRFSARD
     VSSLSRSAMG LTLVRLDEGD QVADVTVIRC SMEEGE
//

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