(data stored in SCRATCH3701 zone)

HOGENOM6: ERWAC_2_PE2324

ID   ERWAC_2_PE2324                       STANDARD;      PRT;   878 AA.
AC   ERWAC_2_PE2324; D4HWY0;
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; (ERWAC_2.PE2324).
GN   Name=gyrA; OrderedLocusNames=EAMY_2345;
OS   ERWINIA AMYLOVORA CFBP1430.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Erwinia.
OX   NCBI_TaxID=665029;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ERWAC_2.PE2324.
CC       Erwinia amylovora CFBP1430 chromosome, complete genome.
CC       1..42673 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:D4HWY0_ERWAC
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; D4HWY0; -.
DR   EMBL; FN434113; CBA21544.1; -; Genomic_DNA.
DR   RefSeq; YP_003531703.1; NC_013961.1.
DR   GeneID; 8911809; -.
DR   GenomeReviews; FN434113_GR; EAMY_2345.
DR   KEGG; eam:EAMY_2345; -.
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; ERWAC_2.PE2324; -.
DR   PRODOM; ERWAC_2_PE2324.
DR   SWISS-2DPAGE; ERWAC_2_PE2324.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   878 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDLAREITP VNIEEELKNS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMNVLGNDWN
     KAYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY MLVDGQGNFG SVDGDSAAAM
     RYTEVRMSKI AHELLADLEK ETVDFVPNYD GTEQIPEVMP TRIPNLLING SSGIAVGMAT
     NIPPHNITEV INGCLAYIAD ENITVEGLME HIPGPDFPTA AIINGRRGIE EAYRTGRGKI
     YIRARGEVEV DAKTGRETII VHEIPYQVNK ARLIEKIAEL VKEKRLEGIS ALRDESDKDG
     MRIVIEVKRD AVGEVVLNNL YSLTQLQTSF GINMVALHQG QPKIMPLKDI LEAFVRHRRE
     VITRRTIFEL RKARDRAHIL EALAVALANI DPIIELIRAA PTPAEAKAGL IARPWELGNV
     SAMLERAGDN AARPEWLEEQ YGIHNGQYYL TEQQAQAILD LRLQKLTGLE HEKLLDEYKD
     LLAQIAELLR ILASSERLME VIREELELIR DQFGDKRRTE ITANTADINI EDLINQEDVV
     VTLSHQGYVK YQPLSDYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDTI LCFSSRGRLY
     WMKVYQLPEA SRGARGRPIV NLLPLEANER ITAILPVREY AEGWNIFMAT ASGTVKKTAL
     TDFSRPRSAG IIAVNLRDDD ELIGVSLTNG SDEAMLFSAA GKVVRFAESA VRTMGRTASG
     VRGIKLAEGD RVVSLIVPRD DGAIMTVTQN GYGKRTANVE YPTKSRATQG VISIKVTERN
     GPVIGAVQVV DGDQIMMITD AGTLVRTRVS EVSVVGRNTQ GVILIRTAED ENVVGLQRVA
     EPVAEEELDA IDGSAAEGDD DIAPEVDTDD ESPEADDE
//

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