(data stored in SCRATCH3701 zone)

HOGENOM6: ASEXC1_2_PE702

ID   ASEXC1_2_PE702                       STANDARD;      PRT;   918 AA.
AC   ASEXC1_2_PE702; E8RTB5;
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; (ASEXC1_2.PE702).
GN   ORFNames=Astex_3101;
OS   ASTICCACAULIS EXCENTRICUS CB 48.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=573065;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ASEXC1_2.PE702.
CC       Asticcacaulis excentricus CB 48 chromosome 2, complete sequence.
CC       by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:E8RTB5_9CAUL
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; E8RTB5; -.
DR   EMBL; CP002396; ADU14736.1; -; Genomic_DNA.
DR   RefSeq; YP_004088887.1; NC_014817.1.
DR   GeneID; 10054703; -.
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; ASEXC1_2.PE702; -.
DR   PRODOM; ASEXC1_2_PE702.
DR   SWISS-2DPAGE; ASEXC1_2_PE702.
KW   ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW   Topoisomerase.
SQ   SEQUENCE   918 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTDTPASGLP TPHGISHVTI EDELKRSYLD YAMSVIVSRA LPDARDGLKP VHRRIVYAMY
     EEGRTHDKKY VKSANIVGDV MGRYHPHGDG AIYDALVRMA QPFSMRLLLV DGQGNFGSVD
     GDPPAAMRYT ESRMTRAAES LIADIDKNTV DFNDNYDGAR QEPSVLPSRI PNLLVNGAGG
     IAVGMATNIP PHNLGEIIEA CLAMLDDPEV STETLLGIVP GPDFPTGGEI LGRSGARQAL
     LTGRGSVIMR GKASVETIRK DREAIIVTEL PYQVNKATLI EHIAEMVREK RIEGISDIRD
     ESDRQGMRMV IELKRDASGD VILNQLYRYS ALQTSFGVNM LALNHGRPQQ MGLRKLLEIF
     LDFREEVVVR RTRFELNKAR DRGHVLVGLA IAVANIDEII HIIRSSVDPT EARERLTAKN
     WPAGDMSPLI ELIADPRSIV FEGGEVRLTE EQARAILALT LSRLTGLGRD EIFGEARTLA
     ASIAEYLAIL SSRERILGIV REELEEVKAL YAEPRRSLIV DGEADIEDED LIPREDMVVT
     VTHSGYVKRT PLSAYRTQHR GGKGRSGMAM KDEDAITGIY AASTHQPMLF FSSTGKAYKL
     KVWRLPLGTP QSKGKAFVNL LPLDKHETVT NILTLPEDEA AWDRLDIVFA TRSGDVRRNK
     LSDFVNVNRA GKIAMKLEEG DAIVGVALCT EDQDVLLSTA SGRSIRFAVD EVRVFKGRDS
     TGVRGVRLGE DDTVISMAIL RRVEATPAER AAYLKHAASL RAAVTGEGEE ATVVVEEEAE
     EGAEDASLSV ERIAELGAAE EFILTIADTG FGKRTSSYDY RRTGRGGQGI VAIDLSKRGG
     KLVASFPVED TDQLLLVTDG GQLIRTPVSQ IRVAGRNTQG VTIFRTSGEK VVSVERLAET
     AEEDGPDEAE LASGGDAG
//

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