(data stored in SCRATCH3701 zone)

HOGENOM6: CAUST_1_PE2539

ID   CAUST_1_PE2539                       STANDARD;      PRT;   918 AA.
AC   CAUST_1_PE2539; D5VKQ0;
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; (CAUST_1.PE2539).
GN   OrderedLocusNames=Cseg_2622;
OS   CAULOBACTER SEGNIS ATCC 21756.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=509190;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CAUST_1.PE2539.
CC       Caulobacter segnis ATCC 21756 chromosome, complete genome.
CC       (1809 nt) ;
CC   -!- ANNOTATIONS ORIGIN:D5VKQ0_CAUST
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; D5VKQ0; -.
DR   EMBL; CP002008; ADG11073.1; -; Genomic_DNA.
DR   RefSeq; YP_003593691.1; NC_014100.1.
DR   GeneID; 9104131; -.
DR   GenomeReviews; CP002008_GR; Cseg_2622.
DR   KEGG; cse:Cseg_2622; -.
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; CAUST_1.PE2539; -.
DR   PRODOM; CAUST_1_PE2539.
DR   SWISS-2DPAGE; CAUST_1_PE2539.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   918 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDEHTTIPA DGSRGDIAPI NIEDELRRSY LDYAMSVIVS RALPDARDGL KPVHRRVLFS
     MHEQGQTPER PYVKSARVVG DVMGKYHPHG DASIYFTLVR MTQPFSMGLV LIDGQGNFGS
     VDGDMPAAMR YTECRMAPPA MALLADLDKD TVDFVDNYDG KEQEPTVLPA RIPNLLVNGA
     GGIAVGMATN IPPHNLGEVI DACLLLIDEP EITTDQLLDL VPGPDFPTGG EIIGRAGPRQ
     ALLTGRGSVI MRGVASVEDL RAGREAIIVT EIPYQVNKAN LVEHIAELVR DKKLEGIADI
     RDESNRDGMR IVIELKRDAS GEVILNQLYR FTALQSSFGV NMLALNRGRP EQMGLHKLLQ
     LFVEFREEVV VRRTKFELGK ARDRGHVLVG LTIAVANIDE FIHIIRSSKD PTEARERLVA
     KSWPAGDMLP LVELIADPRT IQEEGGLIRL TDEQARAILA LTLSRLTGLG REEIGNEAET
     LADAIRGYLE LLSDRANIMA VVREELVEVR EKFAVPRRCQ IVDGDADMED EDLIVREDMV
     ITVTMGGYVK RTPLANYRTQ HRGGKGKSGM ATKNEDAVTR VFSASTHAPL LFFTSGGKVY
     KMKVWRLPLG VANSRGKAFV NLLPIESGET ITSILALPED EATWSGLDVM FATRSGSVRR
     NKLSDFVDVR RNGKIAMKLD EGDGIVGVAV CNADQDVLLT TAAGRCIRFS VDEVRVFASR
     DSTGVRGVRL AEGDEVISMA VLRSVDATPA ERAAYLKHQR AMLRAAGEEG DDAPVAAEEG
     EEDADETTLS PERIAELGAA EEILLTVSSE GFGKRTSAYD FRRTGRGGQG LAAQDLSKRG
     GRLVGSFPID ESDQILLVTD QGQLIRVPVS QIRVAARNTQ GVTIFRTAQD EHVVSVERLA
     DSGGDDNQGE DSGAEETL
//

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