(data stored in SCRATCH3701 zone)

HOGENOM6: DESHD_1_PE2633

ID   DESHD_1_PE2633                       STANDARD;      PRT;   808 AA.
AC   DESHD_1_PE2633; B8FW91;
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; (DESHD_1.PE2633).
GN   OrderedLocusNames=Dhaf_2677;
OS   DESULFITOBACTERIUM HAFNIENSE DCB-2.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=272564;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DESHD_1.PE2633.
CC       Desulfitobacterium hafniense DCB-2, complete genome.
CC       complete genome.
CC   -!- ANNOTATIONS ORIGIN:B8FW91_DESHD
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; B8FW91; -.
DR   EMBL; CP001336; ACL20703.1; -; Genomic_DNA.
DR   RefSeq; YP_002459139.1; NC_011830.1.
DR   ProteinModelPortal; B8FW91; -.
DR   STRING; B8FW91; -.
DR   GeneID; 7259684; -.
DR   GenomeReviews; CP001336_GR; Dhaf_2677.
DR   KEGG; dhd:Dhaf_2677; -.
DR   OMA; PEENITQ; -.
DR   ProtClustDB; CLSK2465865; -.
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; 4.
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; DESHD_1.PE2633; -.
DR   PRODOM; DESHD_1_PE2633.
DR   SWISS-2DPAGE; DESHD_1_PE2633.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   808 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSIPEENITQ RSLEEVLPES YLGYSKHVIL QRAVPDVRDG LKPVHRRIIY AMDELGMTPD
     KPYSKSARLV GDCMGKYHPH GDSSIYDAAV RMAQPWATRY PLIDGQGNFG SIDGDGAAAM
     RYTEMRMTHL SQLMTQDIEK DVIPFKPNYD QREKEPIVLP SPFPNLLVNG GSGIAVGMAS
     NIPPHNLREV VAALILQIDN PHVTLEQLME KVKGPDFPTG GLIIGSQGFT EAYRSGRGKV
     TMRGKAIIES GKNGKSLIVI TEIPFQVSKS TLAAKIEAQS ENGKIEGISE VRDESDREGI
     RLVVECKKDA DPKRILKLLY KYTQLQETFG IINLVISEEG TPRVLGLKEI NHSYLQHRRE
     VVLRRTEYEL AKAKARAHIL EGLVIAINNL DEVLQIIRSS KTPALAKAGL ITRFEFSEVQ
     AQAILDMKLQ HLTNLELDGI RKEYAEILKL IAELESILAD INKVYTIIKN ELKQIADQYG
     DERRTLILPE DVGDEVDYSA FEEPEKPMEV LLTRKGFIKQ IPTPTRRSQI NAIAFAFKDG
     DVLLEHVSCT SKDTLYFFTH SGKYYDAKAK LVAEAGAKEK GRAVNNLFPL PEEERIVAMV
     SLREEKEGQY FVFVTKDGQV MRSPVKDFLN ARTAEAMGLK EQDEIVKVFL SAGEGELFLA
     SLQGQAIRFA EAEVNPMGRK SRGVKGMTLN EGDYVVDALL IQPGADGETG DLITVTEQGY
     VKRTSLEEYK PQGRAGRGIA IAKIDAEKTG YLVSLIQVGP KEDKLLHIIQ AGGAVTGVEA
     QSLKRESRVK SGAGLVNVII NDYIVHVL
//

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