(data stored in SCRATCH3701 zone)

HOGENOM6: DESDG_1_PE4

ID   DESDG_1_PE4                          STANDARD;      PRT;   811 AA.
AC   DESDG_1_PE4; Q317S1;
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 subunit A; EC=5.99.1 3; (DESDG_1.PE4).
GN   OrderedLocusNames=Dde_0004;
OS   DESULFOVIBRIO ALASKENSIS G20.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=207559;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DESDG_1.PE4.
CC       Desulfovibrio desulfuricans subsp. desulfuricans str. G20 chromosome,
CC       complete genome.
CC   -!- ANNOTATIONS ORIGIN:Q317S1_DESDG
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; Q317S1; -.
DR   EMBL; CP000112; ABB36805.1; -; Genomic_DNA.
DR   RefSeq; YP_386500.1; NC_007519.1.
DR   ProteinModelPortal; Q317S1; -.
DR   SMR; Q317S1; 24-480.
DR   STRING; Q317S1; -.
DR   GeneID; 3755946; -.
DR   GenomeReviews; CP000112_GR; Dde_0004.
DR   KEGG; dde:Dde_0004; -.
DR   NMPDR; fig|207559.3.peg.510; -.
DR   eggNOG; COG0188; -.
DR   OMA; TSIPPHR; -.
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; DESDG_1.PE4; -.
DR   PRODOM; DESDG_1_PE4.
DR   SWISS-2DPAGE; DESDG_1_PE4.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   811 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSNQVTIEDE LKKSYLEYSL SVIIGRAIPD VRDGLKPVHR RIMFAQHELG NGYNRAPKKS
     ARVVGDVIGK YHPHGDFAVY DALVRMAQDF SMRDPLVTGQ GNFGSIDGDS AAAMRYTEVR
     MSRLASEFMA DIDKETVEFR PNYDNTLQEP AVLPTKVPNL LLNGSSGIAV GMATNIPPHN
     LGELVDGLLL ELDSPECTVA DLAGLVKGPD FPTGGFCYAG RGLRDAYETG RGTVKIRGRV
     EVEERKKGFQ SIVIREIPYA LNKSSLVEKI AALANERRIE GITDLRDESD RRGIRVVIDL
     KRGTIPEIVI NQLYKYTPLE TSFGINMLAV VGNRPQLLTL KKVFECFLQH RREVIIRRTH
     YDLRKAEARA HILEGLRIAL DNIDEVVELI RASKTPPEAK ERLMQRFSLS EVQAQAILDM
     RLQRLTNLEH EKLIEEYREL LKKIEYFKSI LENEEVLRGV IRDELKELKE TYATPRRTEM
     LEDELEGIDI EDLIPDEDVV ITLSRRGYIK RTPLDSYQQQ RRGGKGIAGV HTGDGDFVQD
     FLVTTNHQYL LLFTNKGRMF QLKVHQVPEG SRTAKGMHIN NLLPMEENEW VNTALTIREF
     TEEKYFLFST RKGMVKRSSA SLYAKARRTG LIAVGLREGD ELIMVREVDD NCEVVLTTEK
     GIAIRFGCGD VRPMGRSATG VKGIALSQDD SVVACVTVQG GLESEIMTVS RYGYGKRTLI
     DRYRVQSRGG KGVINFKVTP KTGEVLGAMT VVSNDQLILL TSTNKIIRIG VKEVRSVGRA
     TQGVRLVWLD EGDHVVGFDR VSEQEQEQLD D
//

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