(data stored in SCRATCH3701 zone)

HOGENOM6: SHEDO_1_PE1934

ID   SHEDO_1_PE1934                       STANDARD;      PRT;   908 AA.
AC   SHEDO_1_PE1934; Q12MU5;
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; (SHEDO_1.PE1934).
GN   OrderedLocusNames=Sden_1948;
OS   SHEWANELLA DENITRIFICANS OS217.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SHEDO_1.PE1934.
CC       Shewanella denitrificans OS217, complete genome.
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:Q12MU5_SHEDO
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; Q12MU5; -.
DR   EMBL; CP000302; ABE55231.1; -; Genomic_DNA.
DR   RefSeq; YP_562954.1; NC_007954.1.
DR   ProteinModelPortal; Q12MU5; -.
DR   SMR; Q12MU5; 30-520, 535-860.
DR   STRING; Q12MU5; -.
DR   GeneID; 4018437; -.
DR   GenomeReviews; CP000302_GR; Sden_1948.
DR   KEGG; sdn:Sden_1948; -.
DR   NMPDR; fig|318161.14.peg.1906; -.
DR   eggNOG; COG0188; -.
DR   OMA; TGRGRIY; -.
DR   PhylomeDB; Q12MU5; -.
DR   ProtClustDB; PRK05560; -.
DR   BioCyc; SDEN318161:SDEN_1948-MONOMER; -.
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; SHEDO_1.PE1934; -.
DR   PRODOM; SHEDO_1_PE1934.
DR   SWISS-2DPAGE; SHEDO_1_PE1934.
KW   DNA gyrase, A subunit;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   908 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTDLASSISP INIEDELKNS YLDYAMSVIV GRALPDVRDG LKPVHRRVLF AMSELKNDWN
     KPYKKSARVV GDVIGKYHPH GDSAVYDAIV RLAQPFSLRY TLVDGQGNFG SVDGDSAAAM
     RYTEIRMQKL AHSLLADLEK ETVDFVPNYD GTEMIPAVLP TRVPNLLING SSGIAVGMAT
     NIPPHNLTEV VKGCLALIDE PSLSIEQLME YIPGPDFPTA ASINGRKGII DAYKTGRGRA
     VMRSKAEIET EDNGRERIIV HEIPYQVNKA RLIEKIAELV KDKKIEGISG LRDESDKDGM
     RIVIEIKRGE VGEVVLNNLY AQTQMQCSFG INMVALTNGQ PKLFNLKEML ECFILHRREV
     VTRRTVFELR KARERAHILE ALAIALANID PIIALIKASP TPAEAKLQLV AQGWELGHVQ
     GMLEKAGDDA ARPEWLEPEY GIRDGQYFLT EQQAQAILEL RLHRLTGLEH EKILSEYEEL
     LIVIAGLLLI LRSPERLMEV IKEELEEVLE QYGDVRRTII NENEIDMSLE DLINEEDVVV
     TLSHTGYAKY QPLSDYQAQR RGGKGKAATK VKDEDFVEKL LVANTHDTIL CFSDFGKMYW
     LKVYQLPLAS RTARGRPIVN LLPLSDGERI TAILPVREYA DDKFIIMATA HGTVKKTALT
     AYSNPRANGI IAVNLKDGDQ LIGVDITDGS DDIMLFSNEG KVVRFNEKAR DSETGEVKID
     AETGEEIIAL RPMGRTATGV RGIKLEDGQK VVSLIVPKGD GAILTVTENG YGKRTELNEY
     PAKSRGTKGV VSIKVTERNG AVVGAVQVGE FDEIMLISDK GTLVRTPAEG VSIIGRNTQG
     VTIIRTAEDE KVVGLQRIEE IQTDEILDAD GNVIVPAESV DGDELSTDTR ATATEAPAQT
     DSAEDEQE
//

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