(data stored in SCRATCH3701 zone)

HOGENOM6: DESMR_2_PE4

ID   DESMR_2_PE4                          STANDARD;      PRT;   813 AA.
AC   DESMR_2_PE4; C4XT13;
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; (DESMR_2.PE4).
GN   Name=gyrA; OrderedLocusNames=DMR_00040;
OS   DESULFOVIBRIO MAGNETICUS RS-1.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=573370;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DESMR_2.PE4.
CC       Desulfovibrio magneticus RS-1, complete genome.
CC       complete genome.
CC   -!- ANNOTATIONS ORIGIN:C4XT13_DESMR
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; C4XT13; -.
DR   EMBL; AP010904; BAH73495.1; -; Genomic_DNA.
DR   RefSeq; YP_002951381.1; NC_012796.1.
DR   STRING; C4XT13; -.
DR   GeneID; 7981600; -.
DR   GenomeReviews; AP010904_GR; DMR_00040.
DR   KEGG; dma:DMR_00040; -.
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: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; DESMR_2.PE4; -.
DR   PRODOM; DESMR_2_PE4.
DR   SWISS-2DPAGE; DESMR_2_PE4.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   813 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDLIQIEEE LKKSYLEYSL SVIIGRAIPD VRDGLKPVHR RILYAMHDLS NTYNRPYKKS
     ARVVGDVIGK YHPHGDQSVY DALVRMAQDF SMRDAIVDGQ GNFGSIDGDA AAAMRYTEVR
     MSRLAGEFLA DIEKETVDFR PNYDNSLEEP AVLPTKVPNL LLNGSSGIAV GMATNIPPHN
     LGELCDGLLH LLDTPSCPVT DIIGLVKGPD FPTGAAIYGG KGLTEAYTTG RGTIKIRGRA
     EVEERKKDYV SVVIREIPYA LNKSSLVEKI AALINDGRIE GVSDLRDESD RKGIRIVLDL
     KKGVIPDIVI NALYKYTPLE TSFGINMLVV ADNRPALLNI KQVLEHFLTH RRDVILRRTR
     FDLRKSEERA HILEGLRIAL DNIDEVVSII RASKNAVEAR ERLMERFGLS ERQAQAILDM
     RLQRLTNLER QKLIDEYNEL IKLIEYLRSI LENDEVLRGV IRDEIKEIQD RYATPRKTEI
     LEDLEGINIL DLIPDEDVVI TLSRRGYIKR TKIDNYQQQK RGGKGIAGVA TAGDDFVQSF
     CATTNHQQLL LFTNLGRMFM LPVHQIPEGQ RTAKGAHIAN LLPMDKEEFV ATALSIREFS
     EERYFLFVTR KGMVKRTCTD LYKNCRSTGI IAVGLKENDE LLTVKEIDDE TEVLLATQQG
     LSNRFHISGV RPTGRGAAGV KGIALKGNDR VAAGVVITSV SRSEVLTVSA NGYGKRTSIE
     HYPIRNRGGS GVINMRVTPK TGQVIGAVMV GDDDELLLLT SANKIIRLSV SGISSVGRAT
     QGVMLVRMDE NDTVMGFDLV DPSDLDRCAP SGE
//

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