(data stored in SCRATCH3701 zone)

HOGENOM6: RHOFD_2_PE1541

ID   RHOFD_2_PE1541                       STANDARD;      PRT;   880 AA.
AC   RHOFD_2_PE1541; Q21Y50;
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; (RHOFD_2.PE1541).
GN   OrderedLocusNames=Rfer_1571;
OS   RHODOFERAX FERRIREDUCENS T118.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Albidiferax.
OX   NCBI_TaxID=338969;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RHOFD_2.PE1541.
CC       Rhodoferax ferrireducens T118, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:Q21Y50_RHOFD
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; Q21Y50; -.
DR   EMBL; CP000267; ABD69303.1; -; Genomic_DNA.
DR   RefSeq; YP_522834.1; NC_007908.1.
DR   ProteinModelPortal; Q21Y50; -.
DR   SMR; Q21Y50; 30-525, 547-858.
DR   STRING; Q21Y50; -.
DR   GeneID; 3960907; -.
DR   GenomeReviews; CP000267_GR; Rfer_1571.
DR   KEGG; rfr:Rfer_1571; -.
DR   NMPDR; fig|338969.3.peg.3546; -.
DR   eggNOG; COG0188; -.
DR   OMA; TGRGRIY; -.
DR   PhylomeDB; Q21Y50; -.
DR   ProtClustDB; PRK05560; -.
DR   BioCyc; RFER338969:RFER_1571-MONOMER; -.
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; RHOFD_2.PE1541; -.
DR   PRODOM; RHOFD_2_PE1541.
DR   SWISS-2DPAGE; RHOFD_2_PE1541.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   880 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTQFAKETLP VSLEEEMRRS YLDYAMSVIV GRALPDARDG LKPVHRRVLF AMHELNNDWN
     RPYKKSARIV GDVIGKYHPH GDQSVYDTIV RMAQDFSMRH MLVDGQGNFG SVDGDNAAAM
     RYTEIRLSKI AHELLADLDK ETVDFGPNYD GSEKEPLVLP TRLPNLLVNG SGGIAVGMAT
     NIPPHNLNEV VDACLHLLRN PEASIDELME IIPAPDFPTA GIIYGIQGVK DGYRTGRGRV
     VMRAKVHFED IDKGQRQSII VDELPYQVNK KTLQERMAEL VHEKKIEGIS HIQDESDKSG
     MRLVIELKRG EVPEVVLNNL YKQTQLQDTF GMNMVALIDG QPKLCNLKDL IKVFLQHRRE
     VVTRRTVFNL RKARERGHVL EGLAVALANI DEFIAIIRNA PTPPVAKVEL MAKPWDSKLV
     REMLTRTRAD GGVINADDYR PDGLEKMYGM GSDGLYRLSD TQAQEILQMR LQRLTGLEQD
     KIVAEYKEVM GEIEDLLDIL AKSERVSTII YEELTAIKTE FGQTKLGARR SLVEHSSFDL
     STEDLITPTD MVVTLSHSGY IKSQPLSEYR AQKRGGRGKQ ATATKEDDWV DQLFIANTHD
     YILCFSNRGR LYWLKVWEVP QGSRGSRGRP IVNMFPLQEG EKINVVLALT GEKRSFPADQ
     YVFMATSMGT VKKTPLDEFS NPRKGGIIAV GLDEGDYLIG AALTDGKHDV MLFSDGGKAV
     RFDENDVRPM GRNARGVRGM MLEDGQGVIA MLVAEDELQS VLTATVNGYG KRTSITEYTR
     HGRGTKGMIA ITQSERNGKV VAATLVHADD EIMLITDKGV LVRTRVSEIR ELGRATQGVT
     LIGLDEGSKL SGLQRIVEND ANPVADETPG DDQDDTSSTD
//

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