(data stored in SCRATCH3701 zone)

HOGENOM6: THISK_2_PE163

ID   THISK_2_PE163                        STANDARD;      PRT;   823 AA.
AC   THISK_2_PE163; D3SGL4;
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_2.PE163).
GN   ORFNames=TK90_2770;
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_2.PE163.
CC       Thioalkalivibrio sp. K90mix plasmid pTK9001, complete sequence.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:D3SGL4_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; D3SGL4; -.
DR   EMBL; CP001906; ADC73255.1; -; Genomic_DNA.
DR   RefSeq; YP_003494722.1; NC_013930.1.
DR   GeneID; 8829182; -.
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_2.PE163; -.
DR   PRODOM; THISK_2_PE163.
DR   SWISS-2DPAGE; THISK_2_PE163.
KW   ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW   Plasmid; Topoisomerase.
SQ   SEQUENCE   823 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTEVIDPEAG ASNAPLELEI GNVMRSSFAD YAMSVITDRA LPDARDGLKP VHRRILYSMH
     QLGITHMVAH KKSARVVGDV LGKYHPHGDS ACYDSAVRMA QHWAMRHPLI DGQGNFGSID
     GDNAAAMRYT EMRLSKLGTR LFADIQKNTV DFRDNFDGTE REPEVLPLTY PNLLVNGSEG
     IAVGMATSVP PHNLRETADA FLAWLDNPEI TTREIAQHMP GPDFPTGGIL HDLDGYIQAL
     DTGRGAVKLR SQWTVEDRPR GGSRLVIDQI PYAVNKAKLV EQIAELVREK KIEGVADLRD
     ESNKKGIRIV LEIKREFEAE AIAFQLVTMT QLETSVRYNI MALVGQTPMQ LGVRDLFEHF
     RAHRIEVIQR RTQFDLDRAL DRLHILEGLL MALDRLDETI ATIRASADAD EARGGLIDLL
     GIDVTQAQAI LDMKLQKLTG LQIQDIRDEH DRLTAEVADL RDILARSERQ VEIMRTELLD
     LCDQHANERC TEIDTSLSKV SAADLIPEED VMLIGTQQGY LKRIAAKDMN RQNRGTKGRS
     IMSVGEDDLV TTFHAGHSHD TLIALTDSGQ VHAIKAYDIP DTGLGNKGRH YRNVFEGVEG
     NVVAMLTVDG LESVTHSLVI FTAQGLVKRT PLSAYSNATR RGGIQGISLV EGDSIVCARV
     SKDEPNESVI VAADNAKAIR FGMEEARAIG RTSRGVRAMN LSEDARVVAG DIIHADDLEK
     AHLMVVSEKG LGKATPASEF RLQSRGGKGV TSYTPNKRSG PVVAATVLFE GADVVLFNDQ
     GGANRIAGSD VPHNGRATTG SAIIRNGSVR NVLAVPPPVE EDQ
//

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