(data stored in SCRATCH3701 zone)

HOGENOM6: PARD8_1_PE1058

ID   PARD8_1_PE1058                       STANDARD;      PRT;   870 AA.
AC   PARD8_1_PE1058; A6LAY9;
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; (PARD8_1.PE1058).
GN   OrderedLocusNames=BDI_1090;
OS   PARABACTEROIDES DISTASONIS ATCC 8503.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PARD8_1.PE1058.
CC       Parabacteroides distasonis ATCC 8503, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:A6LAY9_PARD8
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; A6LAY9; -.
DR   EMBL; CP000140; ABR42853.1; -; Genomic_DNA.
DR   RefSeq; YP_001302475.1; NC_009615.1.
DR   ProteinModelPortal; A6LAY9; -.
DR   SMR; A6LAY9; 29-485.
DR   STRING; A6LAY9; -.
DR   GeneID; 5306243; -.
DR   GenomeReviews; CP000140_GR; BDI_1090.
DR   KEGG; pdi:BDI_1090; -.
DR   eggNOG; COG0188; -.
DR   OMA; TGRGRIY; -.
DR   ProtClustDB; PRK05560; -.
DR   BioCyc; PDIS435591:BDI_1090-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: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; PARD8_1.PE1058; -.
DR   PRODOM; PARD8_1_PE1058.
DR   SWISS-2DPAGE; PARD8_1_PE1058.
KW   DNA gyrase A subunit;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   870 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVDQDRIIKI NIEEEMKSAY IDYSMSVIVS RALPDVRDGF KPVHRRILFG MNELGNTSDK
     PYKKSARIVG EVLGKYHPHG DSSVYFAMVR MAQTWSMRYP LVDGQGNFGS VDGDSPAAMR
     YTEARLSKLA EEMLRDIDKD TVDFQLNFDD TLKEPTVLPT RVPNLLVNGG SGIAVGMATN
     MPTHNLSEVL DGCIAYIDAK GDIEVEGLMQ YIKAPDFPTG ATIYGYAGVK DAFETGRGRI
     ILRGKAEIEV ENNHEKIIIT EIPYLVNKAE LIKYIADLVN EKRIDGISNV NDESDRSGMR
     IVVDVKRDAN SSVVLNKLYK LTALQSSFSV NNIALVNGRP RLLNLKDLIK AFVEHRHEVV
     IRRTKYELRK AEERAHILEG LIIASDNIDE VIAIIKSSKS PQEAIERLIE RFSLSELQAR
     AIVEMRLRQL TGLEQDKLRA EYEEIEKLIA YLNEILENED LCMKVIKDEL LEIKDKFGDE
     RKTDIVYASE ELNPEDFYAD DEMIITVSHM GYIKRTPLSE FRAQGRGGVG AKGSETRDED
     FVEYIYPASM HATLLFFTAK GKCYWLKVFE IPEGAKNAKG RAIQNLLNIE PDDKVQAFIR
     VKKLTTDTEF INSHYLLFCT KKGVIKKTLL EAYSRPRQNG VNAITLREDD GLIQVCMTNG
     NNEVIIANRN GRAIRFHESA VRVMGRTASG VKGMTLDEDN TDEVVGMICI KDKEKETVLV
     VSEQGYGKRS SIEDYRITNR GGKGVKTINI TEKTGKLVAI KNVTDENDLM IINKSGIAIR
     MKVADLNVIG RATQGVRLIN LEKRNDEIAS VCKVLSESEE EIAEQKAEQE ARQENEGREF
     SENQASLGTD VDLPESEEDN EQNDNEEITE
//

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