(data stored in SCRATCH3701 zone)

HOGENOM6: VEIPT_1_PE1818

ID   VEIPT_1_PE1818                       STANDARD;      PRT;   822 AA.
AC   VEIPT_1_PE1818; D1BQ50;
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; (VEIPT_1.PE1818).
GN   OrderedLocusNames=Vpar_1833;
OS   VEILLONELLA PARVULA DSM 2008.
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=479436;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS VEIPT_1.PE1818.
CC       Veillonella parvula DSM 2008, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:D1BQ50_VEIPT
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; D1BQ50; -.
DR   EMBL; CP001820; ACZ25507.1; -; Genomic_DNA.
DR   RefSeq; YP_003312787.1; NC_013520.1.
DR   GeneID; 8637337; -.
DR   GenomeReviews; CP001820_GR; Vpar_1833.
DR   KEGG; vpr:Vpar_1833; -.
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:InterPro.
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; VEIPT_1.PE1818; -.
DR   PRODOM; VEIPT_1_PE1818.
DR   SWISS-2DPAGE; VEIPT_1_PE1818.
KW   DNA gyrase, A subunit;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   822 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MADQQWSHGN IHPVQIDKEM KNAYIDYAMS VIVMRALPDV RDGLKPVHRR ILYAMHETGM
     TPNKPYKKSA RIVGDVLGKY HPHGDSSVYD ATVRLAQDFN TRYLLVDGHG NFGSIDGDSA
     AAMRYTEVRM AKITTEMLAD IDKETVDFMP NYDESLQEPT VLPAKIPNLL INGSSGIAVG
     MATNIPPHNL NEVCNGLAML IDNPDVTVDE LMTAIKGPDF PTGALILGRE GIKKAYSTGR
     GSVKMRARAT IEEMSKGKHK IVVTEIPYQV NKARVIETIA NLSRDKVIDG ITALRDESDR
     QGMRIVIELR ADVQPDIVLN KLYKHTQLQE SFGVIMLALV DGHPRVLNLK EVLGYYLDHR
     LDVIVRRTQF ELNKAEARAH ILEGLLIALD HIDEVIATIR SSQTDEIARN ALMQKFGLSE
     KQAVAILDMR LRRLTGLERE KIEEEYKELL ALIEDLKAIL GSEARQRQII KDELDDMKKK
     YGDPRRSEIT IDTSDLDVED LIADEEMVIT LTKQGYIKRM NANVYRNQHK GGAGVIGMKT
     KEDDYVTQIM HVRTHNTLLF FTSAGRAYRL KAYEVPEAGS RNSRGTAMVN VLPLAVGESV
     TTMIDLERVH EDVNLFMVTE FGVVKRTAIE EYRNIRRSGL NAINLDEGDR LISVNVTTGN
     QDILIGTKLG IAIRFSEHDV RLMKRAAHGV RGIKLNAGDV VVGAGVLNTD ESEAQVFTIS
     EEGFGKRNDA EAYTLQKRGG KGSKNFKITN KTGDVVAVEV VHNDDEVMLI SEQGKIIRFN
     MNDIAVKKGK AISGVKTQNL DEGDKVASIA VIPGAEIEEE VE
//

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