(data stored in SCRATCH3701 zone)

HOGENOM6: SHESW_1_PE1924

ID   SHESW_1_PE1924                       STANDARD;      PRT;   917 AA.
AC   SHESW_1_PE1924; A1RJD2;
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; (SHESW_1.PE1924).
GN   OrderedLocusNames=Sputw3181_1942;
OS   SHEWANELLA SP. W3-18-1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=351745;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SHESW_1.PE1924.
CC       Shewanella sp. W3-18-1, complete genome.
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:A1RJD2_SHESW
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; A1RJD2; -.
DR   EMBL; CP000503; ABM24777.1; -; Genomic_DNA.
DR   RefSeq; YP_963331.1; NC_008750.1.
DR   ProteinModelPortal; A1RJD2; -.
DR   SMR; A1RJD2; 30-520, 535-860.
DR   STRING; A1RJD2; -.
DR   GeneID; 4659812; -.
DR   GenomeReviews; CP000503_GR; Sputw3181_1942.
DR   KEGG; shw:Sputw3181_1942; -.
DR   eggNOG; COG0188; -.
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; SHESW_1.PE1924; -.
DR   PRODOM; SHESW_1_PE1924.
DR   SWISS-2DPAGE; SHESW_1_PE1924.
KW   DNA gyrase, A subunit;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   917 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTDLASSISP INIEDELKNS YLDYAMSVIV GRALPDVRDG LKPVHRRVLF AMSELKNDWN
     KPYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY TLVDGQGNFG SVDGDSAAAM
     RYTEIRMDKL AHQLLADLEK ETVDFVPNYD GTEQIPAVLP TRVPNLLING SSGIAVGMAT
     NIPPHNLTEV VKGCLALIEE PSLSIEQLME YIPGPDFPTA AIINGRKGII DAYKTGRGRA
     IMRALADIET EDNGRERIIV TEIPYQVNKA RLIEKIAELV KDKKLEGISG LRDESDKDGM
     RIVIEIKRGE VGEVVLNNLY AQTQMQCSFG INMVALTNGQ PKLFNLKEML ECFILHRREV
     VTRRTVFELR KARERAHILE ALAVALANID PIIALIKASP TPADAKVKLV EQGWELGHVQ
     GMLEKAGDDA ARPEWLEPQY GIRDGQYFLT EQQAQAILEL RLHRLTGLEH DKIIAEYEEL
     LEFIAGLLFI LRSPERLMEV IKEELEEILT EYGDARRTVI NANEIDMSLE DLINEEDVVV
     TLSHLGYAKY QPLSDYQAQR RGGKGKAATK VKDEDFVEKL LVANTHDTIL CFSDFGKMYW
     LKVYQLPLAS RTARGRPIVN LLPLSDGERI TAILPVREYA ADKYIIMATS NGTVKKTALT
     AYSNPRANGI IAVNLKDGDQ LIGVDITNGD DEIMLFSNEG KVVRFGEKVR DSETGEVKTD
     PETGEEVLSL RPMGRTATGV RGIRLEEGQK VVSLIVPKGD GAILTVTENG YGKRTQLSEY
     PAKSRATKGV VSIKVSERNG AVVGAVQVGS NDEIMLISDK GTLVRTPAKG VSIIGRNTQG
     VTIIRTASDE KVVGLQRIDE IQTDEDDEVE LDENGLPIVP AIIEGELANN EPLDDDIDED
     ELDDDEDDEL ADEQDED
//

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