(data stored in SCRATCH3701 zone)

HOGENOM6: DEAES1_1_PE3277

ID   DEAES1_1_PE3277                      STANDARD;      PRT;   815 AA.
AC   DEAES1_1_PE3277; E6VSG3;
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; (DEAES1_1.PE3277).
GN   OrderedLocusNames=Daes_3318;
OS   DESULFOVIBRIO AESPOEENSIS ASPO-2.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=643562;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DEAES1_1.PE3277.
CC       Desulfovibrio aespoeensis Aspo-2 chromosome, complete genome.
CC       1..112154 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:E6VSG3_DESAO
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; E6VSG3; -.
DR   EMBL; CP002431; ADU64306.1; -; Genomic_DNA.
DR   RefSeq; YP_004123052.1; NC_014844.1.
DR   GeneID; 10097951; -.
DR   GenomeReviews; CP002431_GR; Daes_3318.
DR   KEGG; das:Daes_3318; -.
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; DEAES1_1.PE3277; -.
DR   PRODOM; DEAES1_1_PE3277.
DR   SWISS-2DPAGE; DEAES1_1_PE3277.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   815 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNDTISIESE LKKSYLEYSL SVIIGRAIPD VRDGLKPVHR RILFAMHDLG NYHNRSYKKS
     ARVVGDVIGK YHPHGDSAVY DALVRMAQEF SMRDTLVDGQ GNFGSIDGDA AAAMRYTEVR
     MARLCSEFLG DIEKQTVDFR PNYDNTMQEP TVLPTKVPNL LLNGTTGIAV GMATNIPPHN
     LSELIDGCVH LLDNPGCTVE DMMAFVKGPD FPTGGLVYGG QGLYDAYTTG RGSIKIRGVV
     EIEETGRGKK EAIVIREIPY ALNKSTLVEK IAALVHEKKI DGVADLRDES DRRGIRIVLD
     LKRGAIADII INALYKYTPL ETSFGINMMA VVGKRPMLLN LKSVLDYFLD HRREVVIRRT
     KFDLDKCEKR VHILEGLRIA LDNIDEVVKL IRASKSPDEA KEALMARFSL SEIQAKAILD
     MRLQKLTGLE HDKLLEELAE LLKKIEYFTS ILNNEDVLKS VIRDELKEIK ENYSTPRRSE
     LLTANPDAID IEDLIPDEET VVTLSQRGYI KRTPLSNYTA QRRGGKGISG VQTGDGDFIH
     TFMLTTNHQH LVLFTNLGKM FKIKAHQVPE GSRYAKGGHV ANLLPLDKDE CITTALSLRE
     FDDDRFFLFL TKKGMIKRSS IGLYGNCRST GIRAVNLRDG DELMMVREIE PDVDCILVTR
     DGSAIRFNIN DARPLGRTTA GVKGVALRGD DEVVACVVTG DPERDQLLTV SAGGFGKRTG
     IDQYRQQSRG GKGILNMRLT NKTGKVVGAR MVNESDDVIL LTSANKIIRM SVSEVSQTRG
     RATQGVRLVR MDANNSVIGF ELVMEGEEEL KDVVS
//

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