(data stored in SCRATCH3701 zone)

HOGENOM6: BURRH_2_PE699

ID   BURRH_2_PE699                        STANDARD;      PRT;   867 AA.
AC   BURRH_2_PE699; E5ANP4;
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 (BURRH_2.PE699) (EC 5.99.1.3);
DE   EC=5.99.1 3; .
GN   OrderedLocusNames=RBRH_01710;
OS   BURKHOLDERIA RHIZOXINICA HKI 454.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=882378;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BURRH_2.PE699.
CC       Burkholderia rhizoxinica HKI 454 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:E5ANP4_BURRH
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; E5ANP4; -.
DR   EMBL; FR687359; CBW74226.1; -; Genomic_DNA.
DR   RefSeq; YP_004028370.1; NC_014722.1.
DR   GeneID; 9987998; -.
DR   GenomeReviews; FR687359_GR; RBRH_01710.
DR   KEGG; brh:RBRH_01710; -.
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; BURRH_2.PE699; -.
DR   PRODOM; BURRH_2_PE699.
DR   SWISS-2DPAGE; BURRH_2_PE699.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   867 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDQFAKETLP ISLEEEMRRS YLDYAMSVIV GRALPDARDG LKPVHRRVLY AMHELNNDWN
     RAYKKSARIV GDVIGKYHPH GDSAVYETIV RMAQDFSLRY MLVDGQGNFG SVDGDNAAAM
     RYTEIRLAKI GHELLADIDK ETVDFEPNYD GSETQPQVLP ARIPNLLING SSGIAVGMAT
     NIPPHNLNEV VDACQHLLNH PQASIDELIE IVPAPDFPTA GIVYGVQGVR DGYRTGRGRV
     VMRAKTHFEE IDRGQRMAII VDELPYQVNK RSLLERIAEL VNEKKIEGIS DIRDESDKSG
     MRVVIELKRG EVPEVVLNNL YKNTQLQDTF GMNMVALIDG QPKLLNLREL LECFLSHRRE
     VVTRRTLYEL RRARERGHVL EGLAVALANI DEFIAIIKAA PTPPIAKQAL MTRAWDSALV
     RDMLSRAQGE TPGGRDAFRP DGLAPIFGMQ SDGLYKLSDT QAQEILQMRL QRLTGLEQDK
     ITAEYREVMA QIADLLDILA KPERIRTIIA DELVAIKAEF GDPRRSQIEL NATELGTEDL
     ITPQDMVVTM SHAGYIKSQP LSEYRAQKRG GRGKQAIVMK DDDWIETLFI ANTHDYILCF
     SNRGRVYWLK VYEVPQGSRN SRGRPIVNMF PLQEGEKINV VLPVKEFSAD KFVFLATSLG
     TVKKTPLEAF SRPLRKGIIA VGLDDGDFLI GAQITDGQHD VMLFSDAGKA VRFDENDVRP
     MGREARGVRG MQLEEGQQVI ALLVAGGESQ SVLTATENGY GKRTPIAEYT RHGRGTKGMI
     AIQTSERNGR VVAATLVEPD SEIMLITTAG VLIRTRVSEI REMGRATQGV TLISLDEGTK
     LSGLQQIAET DAEADAESDA DTGGADE
//

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