(data stored in SCRATCH3701 zone)

HOGENOM6: THICR_1_PE1192

ID   THICR_1_PE1192                       STANDARD;      PRT;   871 AA.
AC   THICR_1_PE1192; Q31GD7;
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; EC=5.99.1 3; (THICR_1.PE1192).
GN   OrderedLocusNames=Tcr_1191;
OS   THIOMICROSPIRA CRUNOGENA XCL-2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Thiomicrospira.
OX   NCBI_TaxID=317025;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS THICR_1.PE1192.
CC       Thiomicrospira crunogena XCL-2, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:Q31GD7_THICR
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; Q31GD7; -.
DR   EMBL; CP000109; ABB41786.1; -; Genomic_DNA.
DR   RefSeq; YP_391460.1; NC_007520.2.
DR   ProteinModelPortal; Q31GD7; -.
DR   SMR; Q31GD7; 30-521, 537-840.
DR   STRING; Q31GD7; -.
DR   GeneID; 3760609; -.
DR   GenomeReviews; CP000109_GR; Tcr_1191.
DR   KEGG; tcx:Tcr_1191; -.
DR   NMPDR; fig|317025.3.peg.671; -.
DR   eggNOG; COG0188; -.
DR   OMA; TGRGRIY; -.
DR   PhylomeDB; Q31GD7; -.
DR   BioCyc; TCRU317025:TCR_1191-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: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; THICR_1.PE1192; -.
DR   PRODOM; THICR_1_PE1192.
DR   SWISS-2DPAGE; THICR_1_PE1192.
KW   DNA gyrase, A subunit;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   871 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDFAREILP ISLEDEMQQS YLSYAMSVIV GRALPDVRDG LKPVHRRVLY AMNELGNSWN
     KPYKKSARIV GDVIGKYHPH GDTAVYDTIV RMAQPFSLRY MLVDGQGNFG SIDGDSPAAM
     RYTEVRMSKI AHELLADLEK ETVNFTPNYD GSESEPDVLP TRIPNLLVNG SSGIAVGMAT
     NIPPHNLNET VSACIALIDN PELTISELME FLPGPDFPTY GIINGTKGIR EAYETGRGRV
     QMRARTSVET DKNGKSSIIV HEIPYQVNKA KLIERIAELV KEKKIEGISA LRDESDKDGM
     RIVIEVKRGE VPEVLINNLY KQTTMQTVFG INMVALINSQ PKLLNLKDVL EAFIRHRREV
     VTRRTIYDLR KAREKAHILE GLALALNNID EMIELIKASP SPSVAKERML ERDWSIGNVE
     QLLEKVEMKD VRPEDLPEGF GADGSGVYKL SPAQAQAILE MRLHRLTGLE QDKIIAEYRD
     LVLKIAEFLE ILRNPDRLTE VVREELQEVV ENFGDKRRTE IDHSYQDIDA EDLIAVENRI
     VTLSRDGYIK TQPLSDYQAQ RRGGRGKSAT QMKEDDEIGQ MIVASTHDML LCFSNRGKLY
     WQKTWQLPLA SRGSKGKPIV NVLPLETGEH ITSILPVSEF SEGYYVFMAT KQSTVKRVAL
     SDFSRPRANG IIAVDLLDDD ELVGTAITDG EQDIMLFSNI GKAIRFDEND VRVMGRQARG
     VRGMKLKDGM SIISMQVARK DTLILTATEH GYGKCTPVDD YSTINRGGQG VISIKTSDRN
     GNVVYSVAVT PDQEVVLITN KGTLVRTRVS EISVVGRNTQ GVKLINVGKG EIVVGLAVVD
     VQEDELPDID IEDMPESDEA PEIVSEDDTE Q
//

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