(data stored in SCRATCH3701 zone)

HOGENOM6: CYAP4_3_PE2540

ID   CYAP4_3_PE2540                       STANDARD;      PRT;   864 AA.
AC   CYAP4_3_PE2540; B8HKE2;
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; (CYAP4_3.PE2540).
GN   OrderedLocusNames=Cyan7425_2787;
OS   CYANOTHECE SP. PCC 7425.
OC   Bacteria; Cyanobacteria; Chroococcales; Cyanothece.
OX   NCBI_TaxID=395961;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CYAP4_3.PE2540.
CC       Cyanothece sp. PCC 7425, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:B8HKE2_CYAP4
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; B8HKE2; -.
DR   EMBL; CP001344; ACL45133.1; -; Genomic_DNA.
DR   RefSeq; YP_002483494.1; NC_011884.1.
DR   STRING; B8HKE2; -.
DR   GeneID; 7288721; -.
DR   GenomeReviews; CP001344_GR; Cyan7425_2787.
DR   KEGG; cyn:Cyan7425_2787; -.
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; CYAP4_3.PE2540; -.
DR   PRODOM; CYAP4_3_PE2540.
DR   SWISS-2DPAGE; CYAP4_3_PE2540.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   864 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTFSQESPQE RIIATDLRNE MSRSYLEYAM SVIVGRALPD ARDGLKPVHR RILYAMHELG
     LTPDRPFRKC ARVVGEVLGK YHPHGDTAVY DALVRMAQDF SMRDPLIDGH GNFGSIDNDP
     PAAMRYTESR LRPLTCDALL QDIEQETVDF GDNFDGSQQE PLVMPARIPQ LLLNGSSGIA
     VGMATNIPPH NLGELINGVI ALIQNPEISS EQLMQYIPGP DFPTGAQILG TTGIREAYTT
     GRGSITMRGV ARIETIEQRG RPDREAIIIT ELPYQTNKAA LIEKIAEMVN EKRLEGISDI
     RDESDRDGMR IVIELKRDAY PRVVLNNLYK QTPLQINFGA NMLALVNGEP QLLTLKEFLH
     EFLKFRIQVI ERRTQYNKRK AEERDHLLQG LLIALSNLDS VIALIRHAAD ATTAKQELID
     SYGLSEPQAD AILQMQLRRL TALEAEKIQR EHEDLVAQIA DFQDILDRPE RILSIIQTEV
     EQLKTRFASP RRTVIEQLEG EIDTTDLIAN QKAVILVTEQ GYIKRMPVDT FEAQSRDGRG
     RKGAQIKEDD AVEHFFACCD HDGILFFSDR GVAYCLKAYQ IPIGSRNARG VPIVQLLPIP
     REEKITSVVP VDEFREDEYL VMLTAGGYIK KTALSAFSNI RANGLIAIAL ETGDQLRWVR
     RAREGDSIII GSRQGMAIHF RTDHEQLRPL GRATRGVRAM ALRAGDELIG MDILPSAIVA
     NLAVATSDAE VESEEGAEEM PLEEIPINAD NPGPWVLVVT TCGFGKRVPV SQFRLQNRAG
     KGITATKFKT RQTQDQLAAL RIVNGEDELM IVTNRGIIIR QSVGAISSQS RAATGVRLQR
     LDEEDSIAAV TIVPSTELTD SEEC
//

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