(data stored in SCRATCH3701 zone)

HOGENOM6: ANACI_1_PE708

ID   ANACI_1_PE708                        STANDARD;      PRT;   902 AA.
AC   ANACI_1_PE708; D1ASI5;
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; (ANACI_1.PE708).
GN   Name=gyrA; OrderedLocusNames=ACIS_00926;
OS   ANAPLASMA CENTRALE STR. ISRAEL.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=574556;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ANACI_1.PE708.
CC       Anaplasma centrale str. Israel, complete genome.
CC       Missing 5 prime End;
CC   -!- ANNOTATIONS ORIGIN:D1ASI5_ANACI
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; D1ASI5; -.
DR   EMBL; CP001759; ACZ49438.1; -; Genomic_DNA.
DR   RefSeq; YP_003328752.1; NC_013532.1.
DR   GeneID; 8651790; -.
DR   GenomeReviews; CP001759_GR; ACIS_00926.
DR   KEGG; acn:ACIS_00926; -.
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; ANACI_1.PE708; -.
DR   PRODOM; ANACI_1_PE708.
DR   SWISS-2DPAGE; ANACI_1_PE708.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   902 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSGGVLPVSI EQELESSYLS YAMSVIVSRA IPDIRDGLKP VHRRILYSMY KSGYDHNKPY
     KKAARVVGDV MGRYHPHADT AIYDALVRMA QDFSLLVPLI DSQGNFGSID GDPPASMRYT
     EARLSEAAHF LLNDIDEDTV DFRPNYDENE EEPVILPAEF PNLLVNGAGG VAVGMSTNIP
     SHNLGEVVDA CVAYIERPEI TLDELMAIIP GPDFPTGGVI MGDAGIRSAF ASGRGTIVVR
     GRTHTEELPS GRQAIIIDEI PYQVNKAKLV ERIHELVKEK KIEGVADLRD ESNKSGVRVA
     IELKRQVDSQ VVLNQLLGLT PLRTSFSINT LVLENNKPRV MSLPEIIATF VDFRKEVIVR
     RTRFRLKKIR EKAHLYIGMY IAVLNIDEVV SIIKSSKDSA EASAALRERR WAPSADIRNM
     IELVSDSTGV VEGGMYQLTV PQVKAILEMR LQRLTGLEKE KLEAELESMV ALITEYTKIL
     STDSLLMDIV KQGLLDAKAK LAKPRNTAIE QSVDEIDAES LIPKEEMVVT VTMNGFVKRV
     KLSNYRAQKR GGKGRVAQGI KEEDVTTKLF VVDTHTSVLF FSNVGKVYKL KVYKLPLGEP
     SSRGRSLVNI FPLSDGETIT SVMPLPSCDD EVGIANLDVV FATASGNIRR NALSDFQYVP
     SSGKIAMVLT PGDQLISAHV CGYADHVLLS SRLGKSIRFA VSNVRQFRGR TSDGVRAIRL
     SAGDQVISMS VLHGIEASSE LKESYLKIPV EARVAASHSG VVSDEVAPML EEHAIEREQF
     LEMACSEQFI LTVTENGFGK RTSAYEYRIT SRGGVGVVNI LTTVRNGNVV ASFPVSQTDQ
     VMLITDKGKL IRIAVTDIRV VGRSTQGVTL FKTEKGEKVV SVATVVDGSK EEDEERPSGD
     EE
//

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