(data stored in SCRATCH3701 zone)

HOGENOM6: CLOCE_1_PE3381

ID   CLOCE_1_PE3381                       STANDARD;      PRT;   840 AA.
AC   CLOCE_1_PE3381; B8I2A6;
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; (CLOCE_1.PE3381).
GN   OrderedLocusNames=Ccel_3482;
OS   CLOSTRIDIUM CELLULOLYTICUM H10.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=394503;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CLOCE_1.PE3381.
CC       Clostridium cellulolyticum H10, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:B8I2A6_CLOCE
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; B8I2A6; -.
DR   EMBL; CP001348; ACL77769.1; -; Genomic_DNA.
DR   RefSeq; YP_002507749.1; NC_011898.1.
DR   STRING; B8I2A6; -.
DR   GeneID; 7312501; -.
DR   GenomeReviews; CP001348_GR; Ccel_3482.
DR   KEGG; cce:Ccel_3482; -.
DR   OMA; TGRGRIY; -.
DR   ProtClustDB; PRK05560; -.
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: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; CLOCE_1.PE3381; -.
DR   PRODOM; CLOCE_1_PE3381.
DR   SWISS-2DPAGE; CLOCE_1_PE3381.
KW   DNA gyrase, A subunit;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   840 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MADEIREQKI IPIDIESEMK KSFIDYAMSV IIDRALPDVR DGLKPVHRRI LYTMFTSGFT
     PEKPYRKSVA TVGEALKSYH PHGDAAVYDS LVRMAQDFSL RHPLVDGHGN FGSRDGDSAA
     AMRYTEARLA KISMEMLADI NKDTVDFKPN FDEHEVEPVV LPSRFPNLLV NGSSGIAVGM
     ATNIPPHNLG ETIDGICAVL DNPEITIDEL MKYIKGPDFP TAAKIIGKRG IREAFKTGRG
     KLVVRSEAVI EEMHGNRHRI IITEIPYLVN KARLVEKIAQ LVKDKRIDGI SFIQDESGRE
     EPVRIVIDLK RDANPNVVLN QLYKNTQLQE SFSVNMVAIV PTEDKMYEPR VLNLRQIIDY
     YIAHQEDVIR RRTKFELDKA EARAHILEGL KKALDHLDEV IKTIRNSKTE AIAKENLSER
     FGFSDKQAQA IVDMRLGRLT GLEREKLETE YNELLEKIKY YKDVLANEIL VHQIIKDELS
     VIKNKYADER RTKIEIDEDE IDIEDLIQEE ESVITMTHFG YIKRLPADTY KSQRRGGKGI
     IGLSTREEDF VKNLFVTSTH HFIMFFTNKG RVYRLKAYEI PESGRQAKGT AIVNLLQLDG
     DEKVTTVIPI QEYKEGLYLI MATKNGLVKK TDLMEYDNIR KGGLAAVSLR ENDQLIDVQL
     TDGNQDIILS TVNGMAIRFR ETDARPIGRV SQGVKGIELD EGDFVIGMEV CTDNTTLLVV
     TENGFGKRTE LDEYKVQTRG GKGVLTYRIT EKTGKSIGML LVSEEDDIML ISSDGSIIRM
     KVSEISILGR ATQGVTLMRM SEGNNVVSVA RMVNEESEEN EEMEENEEME ENEESENTEL
//

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