(data stored in SCRATCH3701 zone)

HOGENOM6: CORP2_1_PE9

ID   CORP2_1_PE9                          STANDARD;      PRT;   854 AA.
AC   CORP2_1_PE9; D9QD64;
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; (CORP2_1.PE9).
GN   Name=gyrA; OrderedLocusNames=CpC231_0009;
OS   CORYNEBACTERIUM PSEUDOTUBERCULOSIS C231.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=681645;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CORP2_1.PE9.
CC       Corynebacterium pseudotuberculosis (strain C231) chromosome, complete
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D9QD64_CORP2
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; D9QD64; -.
DR   EMBL; CP001829; ADL09508.1; -; Genomic_DNA.
DR   GenomeReviews; CP001829_GR; CpC231_0009.
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:0006265; P:DNA topological change; IEA:InterPro.
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:3.90.199.10; 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; CORP2_1.PE9; -.
DR   PRODOM; CORP2_1_PE9.
DR   SWISS-2DPAGE; CORP2_1_PE9.
KW   ADL09508.1000011385old_1320000031;
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   854 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDDLLGGEG FDRIHPIDLN EEMETSYIDY AMSVIVGRAL PEVRDGLKPV HRRILYAMYD
     SGYRPERGYV KSARPVSDTM GQFHPHGDSA IYDTLVRLAQ DWNMRYPLVD GQGNFGSRGN
     DGPAAMRYTE CRLTPLAMEM VRDIRENTVD FSPNYDGKTQ EPDVLPSRVP NLLMNGSNGI
     AVGMATNIPP HNLNELADAI FWLLENPDAD EAAALEACMS YVKGPDFPTS GQIVGSQGIN
     DAYTTGRGSI RMRGVTSIEE EGSRQIIVIT ELPYQVNPDN MISNIAEQVR DGKLAGISKI
     EDESSDRVGM RIVVTLKRDA VPRVVLNNLY KHSQLQTNFG ANMLSIVDGV PRTLRLDQML
     RYYVTHQIEV IVRRTQHRLE EAEKRAHILR GLVKALDMLD EVIALIRRSA TVDVARSGLI
     DLLTIDEIQA DAILAMQLRR LAALERQKII DELAEIEIEI ADYKDILAKP ERQRAIVRDE
     LKEIVTKYGD ERRTQIIAAT GDVTEEDLIA RENVVVTITS TGYAKRTKVD AYKSQRRGGK
     GVRGAELKQD DVVRHFFVCS THDWILFFTN FGRVYRLKAY ELPEASRTAR GQHVANLLEF
     QPEERIAQVI QLQSYEDAPY LVLATAQGRV KKSRLSDYES NRSGGLIAIN LGEEDKLIGA
     ALCSNDDELL LVSEEGQSIR FSADDDQLRP MGRATAGVKG MRFRGDDQLL AMTVVRSDAY
     LLVATSGGYG KRTSLEEYSQ QGRGGLGVVT FKYTPKRGKL IAAVVVDEDD QIFAITSAGG
     VIRTEVNQIR PSSRATMGVR LVNLEDGVEL LAIDRNVEGE GEETAEAVAT GAIDGPADRG
     RQTEVNIEPE GADQ
//

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