(data stored in SCRATCH3701 zone)

HOGENOM6: ROTMD_1_PE6

ID   ROTMD_1_PE6                          STANDARD;      PRT;   882 AA.
AC   ROTMD_1_PE6; D2NQB2;
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=Type IIA topoisomerase, A subunit; (ROTMD_1.PE6).
GN   OrderedLocusNames=RMDY18_00060;
OS   ROTHIA MUCILAGINOSA DY-18.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Micrococcaceae; Rothia.
OX   NCBI_TaxID=680646;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ROTMD_1.PE6.
CC       Rothia mucilaginosa DY-18, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D2NQB2_ROTMD
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; D2NQB2; -.
DR   EMBL; AP011540; BAI63838.1; -; Genomic_DNA.
DR   RefSeq; YP_003361658.1; NC_013715.1.
DR   GeneID; 8693035; -.
DR   GenomeReviews; AP011540_GR; RMDY18_00060.
DR   KEGG; rmu:RMDY18_00060; -.
DR   OMA; QRENVIV; -.
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:InterPro.
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; ROTMD_1.PE6; -.
DR   PRODOM; ROTMD_1_PE6.
DR   SWISS-2DPAGE; ROTMD_1_PE6.
KW   type IIA topoisomerase, A subunit;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   882 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRNEKVMSEE QQNKSTEVDV VSNGGAENVD HHGHIEQVDL QTEMQRSYLD YAMAVIIGRA
     LPDVRDGLKP VHRRVIYAMY DGGYRPDRSF NKCARVVGDV MGQFHPHGDS AIYDTLVRLI
     QSWIMRYPLA LGQGNFGSPG NDGAAAPRYT ETKMAPIALE MVRDINEDTV DFQPNYDGKS
     LEPTVLPARI PNLLVNGSSG IAVGMATNIP PHNLREVAEG VEWFLKNPHA TNDELLNALM
     ARIKGPDFPT GAQILGTKGI EDAYRTGRGS ITMRAVVNVE EIHGRTCLVV TELPYQANPD
     NLAIKIAELI KDGKVTGIAD LRDETSGRTG QRLVIVLKRD ASPKVVLNNL YKHTQLQENF
     SANMLAIVDG VPRTLSLDAF VRHWVDHQMD VIVRRTRYRL RQAEEEAHIL RGLLKALDAL
     DEVIALIRRS PTADEARSGL MEFLQIDEAQ AQAILNMQLR RLAALERQKI QDRHDELMRM
     IAEYNAIIAS ETRQREIISE ELGEIVNRYG DERRTQIMYG YNGDMSMEDL IPEEEVVVTI
     TRGGYIKRTR SDQYRSQHRG GKGIKGASLR GDDVVEHFFV TTTHSWILFF TNLGRVYRAK
     GYELQEAGRD AKGQHIANLL EFQGGEHIAQ VMELKSYEDA EYLVLATRGG MVKKSRLSDY
     DTNRTAGLIA INLREGDEVV SAFTVSAQDD ILLVSRNGMS LRFHADDASL RPMGRSTSGV
     TGMKFREGDE LISANVVTEG SFVFVVTEGG YAKRTSVDEY RVQGRNGFGI KVAKLVEDRG
     ALVGGLIVDE EDEVLVVMAS GKVVRSNVNE VPAKGRDTMG VIFAKPGKGD SIIGVARNQD
     RQLDDSDDET TENTEASESS EAPGTDNEGE AAAADLTATG GN
//

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