(data stored in SCRATCH3701 zone)

HOGENOM6: SPILD_1_PE1973

ID   SPILD_1_PE1973                       STANDARD;      PRT;   838 AA.
AC   SPILD_1_PE1973; D2QCP2;
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; (SPILD_1.PE1973).
GN   OrderedLocusNames=Slin_2002;
OS   SPIROSOMA LINGUALE DSM 74.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Spirosoma.
OX   NCBI_TaxID=504472;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SPILD_1.PE1973.
CC       Spirosoma linguale DSM 74, complete genome.
CC       sequence 1..690592 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:D2QCP2_SPILD
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; D2QCP2; -.
DR   EMBL; CP001769; ADB38047.1; -; Genomic_DNA.
DR   RefSeq; YP_003386846.1; NC_013730.1.
DR   GeneID; 8725740; -.
DR   GenomeReviews; CP001769_GR; Slin_2002.
DR   KEGG; sli:Slin_2002; -.
DR   OMA; TGRGRIY; -.
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; SPILD_1.PE1973; -.
DR   PRODOM; SPILD_1_PE1973.
DR   SWISS-2DPAGE; SPILD_1_PE1973.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   838 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MADETPDLES PSNIIPINIE DEMRGAYIDY SMSVIISRAL PDVRDGLKPV HRRVLFGMAE
     LGVNYNKPHK KSARIVGEVL GKYHPHGDSS VYDTMVRMAQ DWSLRYPLVD GQGNFGSIDG
     DSPAAMRYTE ARLKRIADEL LTDIYKETVD FQGNFDDSLQ EPTVMPAKLP NLLLNGSSGI
     AVGMATNMAP HNLTEVVDGI LAYLENSEIT VEELMQFVKA PDFPTGATIY GMEGVKSAFK
     TGRGRVVMRA HATIEENRGK TQIIVTDVPY MVNKAVMLEK TAELINDKKI EGIMAFRDES
     DRDGLRVVYD LRKDAIPNVV LNNLYKHTAL QSSFSINNVA LVKGRPMMLN LKDMMKYYVE
     HRFEVITRRT QYELREAEKR AHILEGLLIA LDNIDAVIEL IRSSRDPEVA RTGLMERFSL
     SDLQAKAILE MRLQRLTGLE RDKLQAEYDE LMTEIADLKE ILASEERKRQ VIKEELTDIR
     ARYGDERRTE INPLGDGNIS DLSLIADEDM VITISHEGYI KRTPTTEYRS QGRGGVGAKA
     ASTKEEDFTE HLFTATMHNT LLAFTQKGRM YWLPVYELPE GSRTSKGRPL ANFINIESDD
     KVRAVINVTD LKNEDYINNN YIVMCTRKGT IKKTMLEAYS RPRQNGIIAI TIDEDDQLLG
     VCMTNGDNDI VIASSAGKAV RFHESRVRPM GRTAAGVRGI SLDEEDPTDH VIGMVCISSQ
     DAQLLVVSQN GYGKRSDIDG YRITNRGAKG VGTLKITEKV GRLVAVLDVA DNDDLMIINK
     SGIAIRTPVD AINVIGRNTQ GVRLIKLNEG DEISSVTKIK KEEGEEIATA EPEAAVEE
//

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