(data stored in SCRATCH3701 zone)

HOGENOM6: DESHD_1_PE6

ID   DESHD_1_PE6                          STANDARD;      PRT;   828 AA.
AC   DESHD_1_PE6; B8FXX1;
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; (DESHD_1.PE6).
GN   OrderedLocusNames=Dhaf_0006;
OS   DESULFITOBACTERIUM HAFNIENSE DCB-2.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=272564;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DESHD_1.PE6.
CC       Desulfitobacterium hafniense DCB-2, complete genome.
CC       complete genome.
CC   -!- ANNOTATIONS ORIGIN:B8FXX1_DESHD
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; B8FXX1; -.
DR   EMBL; CP001336; ACL18076.1; -; Genomic_DNA.
DR   RefSeq; YP_002456512.1; NC_011830.1.
DR   ProteinModelPortal; B8FXX1; -.
DR   SMR; B8FXX1; 32-490.
DR   STRING; B8FXX1; -.
DR   GeneID; 7256950; -.
DR   GenomeReviews; CP001336_GR; Dhaf_0006.
DR   KEGG; dhd:Dhaf_0006; -.
DR   OMA; TGRGRIY; -.
DR   ProtClustDB; PRK05560; -.
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; DESHD_1.PE6; -.
DR   PRODOM; DESHD_1_PE6.
DR   SWISS-2DPAGE; DESHD_1_PE6.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   828 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSTEIQGGKI LPIEISEELK KSFIDYSMSV IVSRALPDVR DGLKPVHRRI IYTLHELGMT
     PNKPYSKSAR LVGDCMGKFH PHGDSSIYDA VVRLAQDFST RYPLIDGHGN FGSVDGDSAA
     AMRYTEARMA KITQYMLADI DKDTVDFQPN YDEREQEPKV MPAKFPNLLV NGSAGIAVGM
     ATNIPPHNLT EVIEGTIAQI DNPEIEIKEL MNYIKGPDFP TGASIMGTEG IISAYRTGKG
     SFRTRAKAHV EEMEKSGKMR IIVTEIPYMV NKARLVEKIA ELVREKRIEG ITDLRDESDR
     TGMRIVMELR RDVNPQVLLN QLYKHTQMEE SFGVNILALV DGQPKVLNLK QIIHYFIEHQ
     KDVIVRRTRF ELNKAEAEAH ILEGLRIALD YIDEVISIIR TSADEQSAKD NLMSRFGLSD
     KQSQAIVDMR LKRLTGLERE KIEEQYQKIQ ETIAYLKAVL NSEQMVLNII KQELQEVKEK
     FGDERRTEIS FDATHMNIED LIDDEEVVIT MSHRGYIKRM PLNTYKSQRR GGKGVHGMAT
     REEDFVEKIF TTSTHQYILF FTTRGKVYRL KAHEIPEAGR TGKGTALVNL LSINPSEEKI
     TAVLSIRKYN EDFHLFMATR KGIVKKTLLK EYDSPRKDGL IAISLSGDDE LIDVRLTKPD
     EHIIIATKNG LCIRFLESDV RQMGRTAHGV KGISLEKEDL VVSMDVIYEE EAEILSMTEL
     GFSKRTSLSE YRVQGRGGKG IIATKLNAKT GKLVGLKVMR PENDMMIITE DGIIIRQEVS
     GISKQGRSAQ GVMAMRIGES KVVAIAVVDN KEDAEESDLE LVEIESEE
//

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