(data stored in SCRATCH3701 zone)

HOGENOM6: RHPAL2_1_PE2810

ID   RHPAL2_1_PE2810                      STANDARD;      PRT;   913 AA.
AC   RHPAL2_1_PE2810; E6VK85;
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; (RHPAL2_1.PE2810).
GN   OrderedLocusNames=Rpdx1_2872;
OS   RHODOPSEUDOMONAS PALUSTRIS DX-1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=652103;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RHPAL2_1.PE2810.
CC       Rhodopseudomonas palustris DX-1 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:E6VK85_RHOPX
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; E6VK85; -.
DR   EMBL; CP002418; ADU44455.1; -; Genomic_DNA.
DR   RefSeq; YP_004109188.1; NC_014834.1.
DR   GeneID; 10065094; -.
DR   GenomeReviews; CP002418_GR; Rpdx1_2872.
DR   KEGG; rpx:Rpdx1_2872; -.
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; RHPAL2_1.PE2810; -.
DR   PRODOM; RHPAL2_1_PE2810.
DR   SWISS-2DPAGE; RHPAL2_1_PE2810.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   913 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDKDDEKPG EPLAPSDIRP VSILDEMKRS YLDYAMSVIV ARALPDARDG LKPVHRRILY
     GMYENGFEWN KPYRKSARTV GDVIGKYHPH GDQSVYDALV RMAQDFSMRV PLIDGQGNFG
     SVDGDMPAAM RYTESRLTKI AQTLLDDIDK DTVDFQPNYD NSEREPQVLP AKFPNLLVNG
     AGGIAVGMAT NIPPHNLGEV IDACVALIDD PALTIDDLNK IVPGPDFPTG GIILGRSGIR
     SAYQTGRGSI VMRGKVEIET VRKDREAIIV SEIPYQVNKA TMVERIAELV REKKIEGISD
     LRDESDRDGF RVVIELRRDA VPEVVLNQLY KFTPLQTNFG ANMVALEGGR PQLMNLKDLL
     TVFVAFREQV VTRRTKFLLN KARDRAHILV GLAIAVANID EIIRVIRNSP DPNTARETLM
     SRDWPAADVA AMITLIDDPR HKLNEDGTAR LSFEQAKAIL DLRLQRLTAL GREEISDELD
     KLAVEIADYL EILRSRARVQ TIVKDELGAV KAEFATPRKT VIVEQEGEVE DEDLIQREDM
     VVTVSHAGYV KRVPLSTYRA QRRGGKGRSG MATREEDFVS RLFVASTHTP VLFFSSRGQV
     YKEKVWRLPL APPNGRGKAL INILPLEQGE RITTIMPLPE DEASWSELDV MFATTGGNVR
     RNKLSDFVDV RRSGIIAMKL DDGEAIVDVQ ICTERDDVLL TAAGGQCIRF PVPDVRVFSG
     RTSMGVRGIA LSSGDKVISL SILRHFEATP AERSTYLKQS GAIRRAATGE ESEPIETPEV
     EAEEGDTSAA LSQERYAEMS ASEQFVLTIS ENGYGKRTSS FEYRTTGRGG KGIVAMSVNG
     RNGKLVASFP VEDSDQIMLV TDNGQLIRCP VEGIRVAGRS TQGVIVFNTA DDEKVVSVER
     IPETDDGDNG NGG
//

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