(data stored in SCRATCH3701 zone)

HOGENOM6: CANIT1_1_PE4

ID   CANIT1_1_PE4                         STANDARD;      PRT;   820 AA.
AC   CANIT1_1_PE4; D8P7F0;
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; (CANIT1_1.PE4).
GN   Name=gyrA; ORFNames=NIDE0004;
OS   CANDIDATUS NITROSPIRA DEFLUVII.
OC   Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Nitrospira.
OX   NCBI_TaxID=330214;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CANIT1_1.PE4.
CC       Candidatus Nitrospira defluvii, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:D8P7F0_9BACT
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; D8P7F0; -.
DR   EMBL; FP929003; CBK39792.1; -; Genomic_DNA.
DR   RefSeq; YP_003795720.1; NC_014355.1.
DR   GeneID; 9486113; -.
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; CANIT1_1.PE4; -.
DR   PRODOM; CANIT1_1_PE4.
DR   SWISS-2DPAGE; CANIT1_1_PE4.
KW   ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW   Topoisomerase.
SQ   SEQUENCE   820 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPPDERLGQI AIEDEMRSSY LDYAMSVIVG RALPDVRDGL KPVHRRILHG MNEMGLAANR
     PYRKSAKIVG EIMGNYHPHG DSAIYDTLVR MAQNFNMRYM LVDGQGNYGS MDGDAAAAMR
     YTEARLTKLA EELLADIEKE TVDFGPNYDE SRVEPLVLPS RVPNLLVNGA GGIAVGYATN
     IPTHNLGEVI EGLLLLLENP EVTIAQLMKK IPGPDFPTAG FIYGTSGIKD AYETGRGLLT
     VRAKVAIETD ERTDRERLII TEIPYQVNKS KLIEKIADLA QEDRVTGISD IRDESDREGV
     RVVIELKRNE IPLVVLNNLY KHSQLQTTFG VNMLALVNNR PEVLNLKRIL EAFVEHRREV
     VVRRTAYDLR KAEERAHILE GLKIALDNLD AVIALIRRSQ SPDVARTGLM QQFRLSEIQA
     NAILEMRLQR LTQLERDKLV EEYREVLKTI EYLRSVLGSE ALVRKIIRDE LTEIKEKYQD
     ERRTKIVKEE AELTLEDLIA EEEVVVTISH AGYIKRNAVT LYRAQRRGGK GKIAMGIKEE
     DFVETLFTAS THDSLLFFTD AGKVYWLKVH EIPEASRAAK GKALVNLLAL SKDEKVTATL
     PVKEYRADRF VIMGTKQGVI KKTELSAYSN PRQGGIIALS LDAGDKLIGV DLTDGQREIL
     LGTKQGITIR FKEEDVRAMG RTAHGVRGIT LEPGDEVIGM ETITPDSTTA ILTVTEGGYG
     KRTPVNEYRV QGRGGKGIIS VKTTERNGPA VGFLQVRDED EIMLMAAQGK VLRCKVDDIR
     EIGRNTQGVR LLDMDGDEDR VVAVVRLVER EEGVPEEGES
//

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