(data stored in SCRATCH3701 zone)

HOGENOM6: CITRI_1_PE2253

ID   CITRI_1_PE2253                       STANDARD;      PRT;   878 AA.
AC   CITRI_1_PE2253; D2TSD3;
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; (CITRI_1.PE2253).
GN   Name=gyrA; OrderedLocusNames=ROD_23531;
OS   CITROBACTER RODENTIUM ICC168.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=637910;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CITRI_1.PE2253.
CC       Citrobacter rodentium ICC168, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:D2TSD3_CITRI
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; D2TSD3; -.
DR   EMBL; FN543502; CBG89099.1; -; Genomic_DNA.
DR   RefSeq; YP_003365897.1; NC_013716.1.
DR   GeneID; 8714522; -.
DR   GenomeReviews; FN543502_GR; ROD_23531.
DR   KEGG; cro:ROD_23531; -.
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; CITRI_1.PE2253; -.
DR   PRODOM; CITRI_1_PE2253.
DR   SWISS-2DPAGE; CITRI_1_PE2253.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   878 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDLAREITP VNIEEELKSS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMNVLGNDWN
     KAYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY MLVDGQGNFG SIDGDSAAAM
     RYTEIRLAKI AHELMADLEK ETVDFVDNYD GTEKIPDVMP TKIPNLLVNG SSGIAVGMAT
     NIPPHNLTEV INGCLAYIDD EDISIEGLME HIPGPDFPTA AIINGRRGIE EAYRTGRGKV
     YIRARAEVEA DAKTGRETII VHEIPYQVNK ARLIEKIAEL VKDKRVEGIS ALRDESDKDG
     MRIVIEVKRD AVGEVVLNNL YSQTQLQVSF GINMVALHHG QPKIMNLKDI ISAFVRHRRE
     VVTRRTIFEL RKARDRAHIL EALAIALANI DPIIELIRRA PTPAEAKAAL IARPWDLGNV
     AAMLERAGDD AARPEWLEPE FGVRDGQYYL TEQQAQAILD LRLQKLTGLE HEKLLDEYKE
     LLEQIAELLH ILGSADRLME VIREELELIR DQFGDARRTE ITANSADINI EDLINQEDVV
     VTLSHQGYVK YQPLTDYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDTI LCFSSRGRLY
     WMKVYQLPEA SRGARGRPIV NLLPLEADER ITAILPVREY EEGVNVFMAT ASGTVKKTAL
     TEFSRPRSAG IIAVNLNEGD ELIGVDLTSG SDEVMLFSAA GKVVRFKEDA VRAMGRTATG
     VRGIKLAGED KVVSLIIPRG EGAILTVTQN GYGKRTAAEE YPTKSRATQG VISIKVTERN
     GSVVGAVQVD DCDQIMMITD AGTLVRTRVS EISVVGRNTQ GVILIRTAED ENVVGLQRVA
     EPVDDEELDS IDGSVAEGED DIAPEAETDD DAADDADE
//

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