(data stored in SCRATCH3701 zone)

HOGENOM6: CORAD_1_PE692

ID   CORAD_1_PE692                        STANDARD;      PRT;   841 AA.
AC   CORAD_1_PE692; D5EPI4;
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; (CORAD_1.PE692).
GN   OrderedLocusNames=Caka_0697;
OS   CORALIOMARGARITA AKAJIMENSIS DSM 45221.
OC   Bacteria; Verrucomicrobia; Opitutae; Puniceicoccales; Puniceicoccaceae;
OC   Coraliomargarita.
OX   NCBI_TaxID=583355;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CORAD_1.PE692.
CC       Coraliomargarita akajimensis DSM 45221 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D5EPI4_CORAD
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; D5EPI4; -.
DR   EMBL; CP001998; ADE53721.1; -; Genomic_DNA.
DR   RefSeq; YP_003547891.1; NC_014008.1.
DR   GeneID; 8957814; -.
DR   GenomeReviews; CP001998_GR; Caka_0697.
DR   KEGG; caa:Caka_0697; -.
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; CORAD_1.PE692; -.
DR   PRODOM; CORAD_1_PE692.
DR   SWISS-2DPAGE; CORAD_1_PE692.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   841 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDNPSDSNT PSHMRAQATS ITDIMQTAYI DYSMSVIVSR ALPDARDGFK PVQRRILYAM
     LREGLLHNRP FDKCAGVVGE VLKNYHPHGD SSVYDTLVRL AQDWVMRYPL IVPQGNFGSI
     DGDSPAAYRY TECKLQAIAE DCLKDIDEDT VDFVPNYKES TTEPSVLPAA LPNLLMNGST
     GIAVGMTTNI PPHNLNEIID AACAIIDNPK IELDELIQFI PGPDFPGGGF IHGKSGIESY
     LKTGRGIVRT RGVAEVVENK GKEEIIISAI PYNVNRASLV MRIAELIKEK AIEGISDLRD
     ESTEETRIVI ELKRGAIPRV IINQLYKSTA LESSFGVILL ALDNRRPKQM NIKEMLTCYI
     DHRREVIYRR TAFRLRKAEA RAHILEGYKI ALDNMDDFVK IIRASKNREE AKVSLMAKYP
     LTEIQTNAIL ELRLYQLTGL ERDKIEEEYR KLMELIGELK DILENESRLL EVIKEELGEM
     KEKYGNPRRS QVIAVDGDIS MEDLVPNEGC MITVTHKGFI KRTSLDEYRS QKRGGKGVIG
     SGQYEDDFVE HLFTASTHDY VMCFMNSGRV YVEKVYHIPE GSRTAKGRAM ANVFELQEGE
     KIAAMICVKD FDESAQSIVL ATENGVTKKT KLSDFRNHRK GGIIGINIDE GDNLVGARLT
     SGEDDIILVT SNAQSIRFPE TDLRDQGRNT RGVRGIKLKS ENDKVVAIEI VDDEAKLLIA
     GANGLGKRTE FSEYRQQSRG GSGIIAIKSD KVAGALSVTD ADEIMMFTLK GQAVRSPIDT
     VRVTGRAASG VKLVNLGNKD ELIGISKVIA SEEDEAGEGE DAVEGEAPDE VATEAPEATE
     E
//

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