(data stored in SCRATCH3701 zone)

HOGENOM6: ARTAR_3_PE6

ID   ARTAR_3_PE6                          STANDARD;      PRT;   875 AA.
AC   ARTAR_3_PE6; E1VRK1;
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; (ARTAR_3.PE6).
GN   Name=gyrA; OrderedLocusNames=AARI_00060;
OS   ARTHROBACTER ARILAITENSIS RE117.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=861360;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ARTAR_3.PE6.
CC       Arthrobacter arilaitensis Re117 chromosome, complete genome.
CC       by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:E1VRK1_ARTAR
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; E1VRK1; -.
DR   EMBL; FQ311875; CBT74255.1; -; Genomic_DNA.
DR   RefSeq; YP_003915226.1; NC_014550.1.
DR   GeneID; 9793944; -.
DR   GenomeReviews; FQ311875_GR; AARI_00060.
DR   KEGG; aai:AARI_00060; -.
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; ARTAR_3.PE6; -.
DR   PRODOM; ARTAR_3_PE6.
DR   SWISS-2DPAGE; ARTAR_3_PE6.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   875 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDEQTPENA PMDGEIIEPI HEGGRVDQID LQTEMQRSYL DYAMAVIVGR ALPDVRDGLK
     PVHRRVLYAM YDGGYRPERS YNKCARVVGE VMGQYHPHGD TAIYDALVRL IQDWVMRYPL
     ALGQGNFGSP GNDGAAAQRY TETKMAPLAM EMVRDINENT VDFQDNYDGK NQEPTVLPAR
     FPNLLVNGSS GIAVGMATNI PPHNLREVAE GVQWYLQNPE ASREELLAEL MLRVKGPDFP
     SGAMILGTKG ISDAYRTGRG SITMRAVVNV EEIQGRTCLV VTELPYMANP DNLAVKIAEL
     VRDGKISGIA DMRDETSGRT GQRLVIVLKR DAVAKVVLNN LYKHTELQSN FSANMLAIVD
     GVPRTLPLDG FIRHWVTHQI EVIVRRTEYR LKKAEEEAHI LRGLLKALDA LDEVIALIRR
     SATTEAARDG LMELLDIDED QARAILDMQL RRLAALERQK IQDRHAELDR MIAEFKAIIA
     DPARQRQIVS EELQEIVAKH GDDRRTKVLM GYDGDMSVED LIPEEEMVVT ITRGGYVKRT
     RIDNYRSQAR GGKGIKGANL RGDDVVEHFF VTSTHNWLLF FTNHGRVYRT KCYELAEAGR
     DAKGQHVANV MAFQPDEHIA QVLDLRTYQD AAYLMLATRN GLVKKTRLED YDTNRTAGVI
     AINLREDDEL VSAQLVSESD DVMLVSRKGQ SVRFTATDTA LRPMGRATSG VTGMKFREGD
     ELLAADVVRD DSYVFTVTNE GYAKRTTVAE YRVQSRGGLG IKVAKLNEER GELVGALIVD
     ETDEVLVVMG SGKVVRSAVS QVPSKGRDTM GVIFAKPDKK DHIIAVAKNS ETELEENLEE
     DAVTLDAENT IDESSAAPET ESGAENDDDT NGGNA
//

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