(data stored in SCRATCH3701 zone)

HOGENOM6: HALNC_1_PE1307

ID   HALNC_1_PE1307                       STANDARD;      PRT;   864 AA.
AC   HALNC_1_PE1307; D0L0F0;
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; (HALNC_1.PE1307).
GN   OrderedLocusNames=Hneap_1339;
OS   HALOTHIOBACILLUS NEAPOLITANUS C2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Halothiobacillaceae; Halothiobacillus.
OX   NCBI_TaxID=555778;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HALNC_1.PE1307.
CC       Halothiobacillus neapolitanus c2, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:D0L0F0_HALNC
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; D0L0F0; -.
DR   EMBL; CP001801; ACX96173.1; -; Genomic_DNA.
DR   RefSeq; YP_003263220.1; NC_013422.1.
DR   STRING; D0L0F0; -.
DR   GeneID; 8534495; -.
DR   GenomeReviews; CP001801_GR; Hneap_1339.
DR   KEGG; hna:Hneap_1339; -.
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; HALNC_1.PE1307; -.
DR   PRODOM; HALNC_1_PE1307.
DR   SWISS-2DPAGE; HALNC_1_PE1307.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   864 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSEFAQEIFK VNLEDEMRRS YLDYAMSVIV GRALPDARDG LKPVHRRVLY AMRELGNDWN
     KPYKKSARVV GDVIGKYHPH GDTAVYDALV RMAQNFSMRY MLIDGQGNFG SVDGDAPAAM
     RYTEVRMAKV AHELQADLEK ETVDFIDNYD GSESEPSVFP ARYPNLLVNG SSGIAVGMAT
     NIPPHNLTEI LNATIALIDD PDTDDETLLS HVPGPDFPTA GIINGAAGIR EAYLTGRGRV
     VMRARTHFEE DDRAGKAIII VTELPYQVNK ARLIERIAEL VREKKIEGIT ELRDESDKDG
     MRIVIELRRG ELPDVMLNNL YQQTQMQSVF GINMVAIVGG QPRTLGLRDI LTVFLRHRRE
     VVTRRTIYDL RKARERAHIL EGLAVALANI DAMIALIKAA PTSNEARTAL MAQNWDSGLV
     HALLERADAA ASRPESLTAD FGLQPDRSYR LSQEQAQAIL EMRLNRLTGL EQDKIVEEYR
     SLLEKIIDLL DILRSESRLM QVIRDELVAM IEEFGDARRT EIVFDYEDLS IEDLIAEEDR
     VVTLSREGYI KTQSLSEYQS QRRGGRGKSS TRMKDEDVIE QLMVASTHAW ALMFTNLGRV
     YWRKVYQLPQ GARGARGRPV VNILPLQEGE RVNALLPVRE FVDDHYIFFA TATGQVKKTP
     LVDFSRPRQA GIIAIDLRDD DRLVGARLTD GSRELMLFSN AGKSIRFAEA DVRSMGRTAG
     GVRGIRMDEM QRVVSLLVVG EGQVLTATEH GYGKRTPIDD FPLQGRGGQG VIAIQTSERN
     GALVGAALVQ DEDEVILISD AGTLVRTEIS QISSVSRNTQ GVILIRLSDD EKLVQLAAVS
     AMSVDSDADR DENATEEDGS SETE
//

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