(data stored in SCRATCH3701 zone)

HOGENOM6: PIRSD_1_PE1336

ID   PIRSD_1_PE1336                       STANDARD;      PRT;   938 AA.
AC   PIRSD_1_PE1336; D2QWS9;
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; (PIRSD_1.PE1336).
GN   OrderedLocusNames=Psta_1356;
OS   PIRELLULA STALEYI DSM 6068.
OC   Bacteria; Planctomycetes; Planctomycetacia; Planctomycetales;
OC   Planctomycetaceae; Pirellula.
OX   NCBI_TaxID=530564;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PIRSD_1.PE1336.
CC       Pirellula staleyi DSM 6068, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:D2QWS9_PIRSD
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; D2QWS9; -.
DR   EMBL; CP001848; ADB16033.1; -; Genomic_DNA.
DR   RefSeq; YP_003369893.1; NC_013720.1.
DR   GeneID; 8705280; -.
DR   GenomeReviews; CP001848_GR; Psta_1356.
DR   KEGG; psl:Psta_1356; -.
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; PIRSD_1.PE1336; -.
DR   PRODOM; PIRSD_1_PE1336.
DR   SWISS-2DPAGE; PIRSD_1_PE1336.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   938 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSSDFDPPSG PSASELPPGD DGTRFLDQPI EDELKESYLT YAMSVIVSRA LPDVRDGLKP
     SQRRILVAMN DLNLTPGAPR VKCAKISGDT SGNYHPHGES VIYPTLVRMA QEWNMRHILI
     DKQGNFGSIA GLPPAAMRYT EARLSPVASM MLEDLNLDTV DFVPTYDERN QEPTVLPCRF
     PNLLVNGAQG IAVGMATSIP PHNLGEVCEA LVKVIDDPEV TLGELCEIIK GPDFPTGGTI
     CGRAGIRRGY RDGRSTIVLR AKTRIEEHKK DRYRIIITEI PYQQARDRVV EKIAELVNEE
     RIKGISGITD LSDLKEPVHL VIDIKRDADP YVVLNQLYQF SPLQDSISII LLALVDGKPR
     ELSLKELLEE FLRHRVTVIR RRTQFLLSKA RRRKHTVEGL LLALANIDEI IRIIRASRTQ
     AEAKVGLMGV ECPAAMMQRA LGEEGFAMFQ SERGASDTYR LTAVQSEAIL RMTLGQLVNL
     EQERLGGEHA ELLKEIAEYL RILADENIIR AMIKEELIAI AAKYGDERRT EISGEEIGDV
     NLEDLITEET MVVSISHRGY IKRTPASTYR AQRRGGKGLK GAKTEDEDPI AHLFVASTHA
     YLLFFTNLGR VYWQKVYDLP ELSRESRGRA IVNLLNLSEG EKIAECIAIR DFDQQGHFLM
     MATRKGLVKK SPLEDYSRPK KGGIIAIKLR EDDEVVDVVV TKPGDEVVLS TSTGMAIRFS
     ESDARPMGRN TSGVKGISLA SGDSLVGMVV ADPDATLLTV CENGYGKRTN FGPNAEVVGP
     PPADDDSIDT GSIDTSSAEA ETVVAEPPAP AEEAAAEDEG DEEGSSGSRY RTQRRGGKGL
     RDIKTTTRNG TVIAVARVDD TEEVLMMTAR GKLQRIAARE IKTIGRNTQG VRIMSLDDDD
     KLVAVVRVPR DEAEVTDLAA LGALPPELPP PAPAGDAS
//

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