(data stored in SCRATCH3701 zone)

HOGENOM6: BIFAV_1_PE6

ID   BIFAV_1_PE6                          STANDARD;      PRT;   920 AA.
AC   BIFAV_1_PE6; D5TER8;
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; (BIFAV_1.PE6).
GN   OrderedLocusNames=BalV_0006;
OS   BIFIDOBACTERIUM ANIMALIS SUBSP. LACTIS V9.
OC   Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=573236;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BIFAV_1.PE6.
CC       Bifidobacterium animalis (subsp. lactis, strain V9) chromosome, complet
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D5TER8_BIFAV
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; D5TER8; -.
DR   EMBL; CP001892; ADG32594.1; -; Genomic_DNA.
DR   GenomeReviews; CP001892_GR; BalV_0006.
DR   OMA; TGRGRIY; -.
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; BIFAV_1.PE6; -.
DR   PRODOM; BIFAV_1_PE6.
DR   SWISS-2DPAGE; BIFAV_1_PE6.
KW   ADG32594.1002479affold_1320000031;
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   920 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MADEPTNNGL DNGPVNDSGD EQHLPDGSLE PLSPQEADNT DYGLMVGQRV QPIDLQDEMR
     QSYLSYALSV IVERALPDVR DGMKPVHRRV VYAMYDGGYR PDRGYNKCSR VVGDVMGKYH
     PHGDSAIYDT LVRMAQSWSM RYLLVDGQGN FGSPGDDPAA AMRYTECRMA PLAMEMVRDI
     DKDTVDFVPN YDGKTQEPTV LPARFPNLLV NGSSGIAVGM ATNIPPHNMR EVADGVHWAL
     DHPEASREEL LDALIERIKG PDFPTGATIL GHKGIEQAYR TGRGLITMRA VVNTEEIKGR
     MCLVVTELPY QVNPDRLVAS IREAVRDGKI TGIADMRDET SGRTGQRLVL VLKRDAVPKV
     VLNNLYKHSQ LQQTFGANML ALVDGVPRTL SLDAFIRHWV SHQLDVIARR TAYLKREAEE
     RDHILQGYLK ALDMIDEVIH LIRSSQTVEI ARTGLMDLLG VDDVQADAIL AMQLRRLAAL
     ERQKILDEHD ELMRRIADYA DILAKPERQR KIVGDELDEI VARYGDDRRT KILPFSGEMN
     VEDLIAEENV VVTVTHAGFI KRTKADEYRA QHRGGKGIKG AKLRDDDVVD HFFLTSTHNW
     LLFFTNKGRV YRCKAYELPE GSRDSKGQHV ANLLQFTPDE SIQTVLSIPD YEVADYLVLA
     TRSGKVKKTR LSEYDSPRQG GLIAVRLMQD ESGETADELI GAALCNATDD IILVSKLGMS
     LKFRADDEQL RPMGRQTAGV QGMKFRAGDE LLAMDVIWGE TDKDLLVVTN QGFAKRTAIS
     EYRLQGRNGF GVKAVQLTDE RGTLVGAVVV SEEDQIMAIM KSGKVIRSNV SEVKLTGRTT
     QGVTLAKPDA GDEIISIARN AETEDEADGD TVVTESSAEA TATQPAQGEP VFEVKSENGM
     PMIEEESAAI DKTKEESREE
//

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