(data stored in SCRATCH3701 zone)

HOGENOM6: RUTMC_1_PE280

ID   RUTMC_1_PE280                        STANDARD;      PRT;   861 AA.
AC   RUTMC_1_PE280; A1AVX7;
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; (RUTMC_1.PE280).
GN   OrderedLocusNames=Rmag_0306;
OS   CANDIDATUS RUTHIA MAGNIFICA STR. CM (CALYPTOGENA MAGNIFICA).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=413404;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RUTMC_1.PE280.
CC       Candidatus Ruthia magnifica str. Cm (Calyptogena magnifica), complete
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:A1AVX7_RUTMC
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; A1AVX7; -.
DR   EMBL; CP000488; ABL02084.1; -; Genomic_DNA.
DR   RefSeq; YP_903555.1; NC_008610.1.
DR   ProteinModelPortal; A1AVX7; -.
DR   SMR; A1AVX7; 37-528, 542-848.
DR   STRING; A1AVX7; -.
DR   GeneID; 4554869; -.
DR   GenomeReviews; CP000488_GR; Rmag_0306.
DR   KEGG; rma:Rmag_0306; -.
DR   eggNOG; COG0188; -.
DR   OMA; TGRGRIY; -.
DR   PhylomeDB; A1AVX7; -.
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; RUTMC_1.PE280; -.
DR   PRODOM; RUTMC_1_PE280.
DR   SWISS-2DPAGE; RUTMC_1_PE280.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   861 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSEHTENPTH FKPNLPVVTI EDEMRNSYLE YAMSVIVGRA LPDVRDGLKP VHRRVLYAME
     VLGNDYNKSY KKSARIVGDV IGKYHPHGDT AVYDTIVRMA QPFSMRNILI DGQGNFGSVD
     GDSAAAMRYT EIRMAKLSHE LLRDLEKNTV DFIDNYDGSE SEPLVLPTRV PNLLANGSSG
     IAVGMATNIP PHNLGEVIEA CLKTIDNEDI TIDELLEIMP GPDFPTAGII NGASGIRQAY
     ETGKGKIYLR SVPHIEGEGE DKQSIVVTEL PYQVNKAKLI GKIAKLVKDK RIDGITGLRD
     ESDKDGMRMV IELRRGEVPE VMLNNLYKLT EMQTVFGINM VAIDKGMPKL MTLKNILEAF
     IAHRRDVVTR RSIFDLNKAR NHAHLLEGLA VALHNIDDII ELIKSASNSI DAKEVLVAKT
     WQGSVIKELI GDRDMVMFKP EDLPTELGLQ MDGDYQLSQK QVQAILDLKL HRLTGLEKNK
     IFDEFNELLE RIKYLLDILQ TPERLMQVIR EELIDIQSNY ANARMTQILE HKIDLTLEDL
     ITQERRVVTL SHGGYVKAQS LSDYQAQRRG GKGKVATKVK DEDFVDQLFI ANSHDTVLCF
     SSLGKVYWLK VYELPMASRI ARGKPIVNLL PLEKEEIINA ILTVSKFDEN HFVFMVTSSG
     TCKKTVLTNF SKPRKGGIIA IELKDNDQLI GVEITSGEHD IMLFSANGKS IRFKESDVRV
     VGRTAIGVRG IKLANADKVV SLIVVNQDNP ILTTTEKGFG KRTRLNEYRS QARGGLGVIS
     IKTSDRNGKV VGAIQITDED EMMLISNKGT LVRARAVDVS IIGRNTQGVT LINIIKGEKL
     VSIAKIAEIE DEESEGENSI E
//

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