(data stored in SCRATCH3701 zone)

HOGENOM6: CYAP2_1_PE1927

ID   CYAP2_1_PE1927                       STANDARD;      PRT;   852 AA.
AC   CYAP2_1_PE1927; E0UBN7;
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, A subunit; EC=5.99.1 3; (CYAP2_1.PE1927).
GN   OrderedLocusNames=Cyan7822_1999;
OS   CYANOTHECE SP. PCC 7822.
OC   Bacteria; Cyanobacteria; Chroococcales; Cyanothece.
OX   NCBI_TaxID=497965;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CYAP2_1.PE1927.
CC       Cyanothece sp. PCC 7822 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:E0UBN7_CYAP2
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; E0UBN7; -.
DR   EMBL; CP002198; ADN13981.1; -; Genomic_DNA.
DR   RefSeq; YP_003887256.1; NC_014501.1.
DR   GeneID; 9738479; -.
DR   GenomeReviews; CP002198_GR; Cyan7822_1999.
DR   KEGG; cyj:Cyan7822_1999; -.
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; CYAP2_1.PE1927; -.
DR   PRODOM; CYAP2_1_PE1927.
DR   SWISS-2DPAGE; CYAP2_1_PE1927.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   852 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTTQPERIIP TDLSSEMSQS YLEYAMSVIV GRALPDARDG LKPVHRRILY AMYELGLTPD
     RPFRKCARVV GEVLGKYHPH GDTAVYDALV RMAQNFSMRD PLIEGHGNFG SIDNDPPAAM
     RYTECRLQNL SVNALLRDIE AETVDFIDTF DGSQQEPVVL PARLPQLLLN GSSGIAVGMA
     TNIPPHNLGE LVDGAIAMIH NPEITNIELM KYIPGPDFPT GGQILGRSGI KDAYISGRGS
     ITMRGVAEIE TIQHRGRPDR DAIIVTELPY QTNKAALIEK IAELVNDKRI DGIADIRDES
     DRDGMRIVIE LKRDAYARVV LNNLYKQTPI QANFGANMLA LVNGEPQILN LKDFLGVFLE
     FRVQVIIRRT TYELRKAEER DHILQGLLVA LANLDPIIQL IRQAADTSSA KRELVEQFGL
     SEVQADAILQ MQLRRLTALE SEKIQAEHQE LQRKIADLTD ILQRRERVDQ IIQEELTQLK
     STHATPRRTQ IVEEEGGIVD IDLIANEQAV ILLTEQGYIK RMPVNTFGQQ SRATRGKSGA
     KIKEDDGVEH FLSCCDHDQI LFFSDRGVVY VISAYQIPSS SRTARGVPIV QMLPIPKDEK
     ITSMVAVSEF TEDQYLVMLT RQGYIKKTAL SAYANIRANG LIAITLSEGD QLRWVRLAKE
     EDSIIIGTRQ GMAIHFKADN EQLRPIGRTA RGVRSMKLKG TDEIISVDIL PGQVVANIGT
     SEDEIEDENL ESEELVNEET HVGPWVLAIT TGGYGKRVPV NQFRLQNRAG MGVKAIRFKN
     AQDQLAAIHI VNQEDEMMIV TSRGIIIRQA VDAISPQSRM ATGIRVQRLD DDDAIAAVAL
     VPPAGEDDES EE
//

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