(data stored in SCRATCH3701 zone)

HOGENOM6: AMYMU_1_PE7

ID   AMYMU_1_PE7                          STANDARD;      PRT;   845 AA.
AC   AMYMU_1_PE7; D8HSV7;
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; (AMYMU_1.PE7).
GN   Name=gyrA; OrderedLocusNames=AMED_0007;
OS   AMYCOLATOPSIS MEDITERRANEI U32.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Pseudonocardineae; Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=749927;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS AMYMU_1.PE7.
CC       Amycolatopsis mediterranei U32 chromosome, complete genome.
CC       Missing 5 prime End;
CC   -!- ANNOTATIONS ORIGIN:D8HSV7_AMYMU
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; D8HSV7; -.
DR   EMBL; CP002000; ADJ41833.1; -; Genomic_DNA.
DR   RefSeq; YP_003762235.1; NC_014318.1.
DR   GeneID; 9434216; -.
DR   GenomeReviews; CP002000_GR; AMED_0007.
DR   KEGG; amd:AMED_0007; -.
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:InterPro.
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; AMYMU_1.PE7; -.
DR   PRODOM; AMYMU_1_PE7.
DR   SWISS-2DPAGE; AMYMU_1_PE7.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   845 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTETLPPAPD HDRIEPVDIQ QEMQRSYIDY AMSVIVSRAL PDVRDGLKPV HRRVLYSMFD
     SGFRPDRGYN KCSRVVGDVM GNYHPHGDSA IYDALVRLAQ PWSMRYPLID GQGNFGSPGN
     DPAAAMRYTE SRLAPLAMQM LADIEEDTVD FSDNYDGRTQ EPDVLPSRFP NLLVNGGSGI
     AVGMATNIPP HNLREVSEGV VWALENPEAT DDELLAALLV RIKGPDFPTK AMILGTSGIE
     DAYRTGRGSV RMRAVVEVEE DAKGRTILVV SELPYQVNPD NLVENIANLV RDGKLTGISD
     IADESNSRSG MRIVVTIKRD AVAKVVLNNL FKHTQLQQNF GVNMLALVDG VPRTLRLDQI
     IRHYVKHQMD VIVRRTRYRL RKKEERAHIL RGLVKALDAL DEVIALIRRS PSADEARPAL
     MTLLDIDEIQ AVAILDMQLR RLAALERQRI IDELAEIEIE IADLKDILEK PERQRAIIRD
     ELMAIVDKYG DDRRTKIIGF SGDVTDEELI AVEDVVVTIT RTGYAKRTKT DLYRSQKRGG
     KGVQGATLKQ DDIVQHFFVC STHDWILFFT NKGRVYRTKA YELPEANRNA RGQHVANLMA
     FQPDEQIAQV IQIKNYEVAP YLVLATKRGL VKKTKLTDFD SNRSGGLIAI NLREGDELVG
     AVLAAAEDDL LLVSAEGQSI RFHATDEALR PMGRPTSGVM GMRFNDGDEL LGISVVKEGK
     FLLVATDGGY SKRTAIEDYP VQGRGGKGVL TIQHDRKRGR LVGALIVDAE DELYAITSSG
     GVIRTPAGDV RKAGRQTKGV RLMNLGEGTT LLAVARNADE PSDVANGEAP EAPEAGEETT
     APSEQ
//

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