(data stored in SCRATCH3701 zone)

HOGENOM6: COMT2_1_PE1431

ID   COMT2_1_PE1431                       STANDARD;      PRT;   898 AA.
AC   COMT2_1_PE1431; D0J3Y4;
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; (COMT2_1.PE1431).
GN   OrderedLocusNames=CtCNB1_1431;
OS   COMAMONAS TESTOSTERONI CNB-2.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=688245;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS COMT2_1.PE1431.
CC       Comamonas testosteroni CNB-2, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D0J3Y4_COMT2
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; D0J3Y4; -.
DR   EMBL; CP001220; ACY32177.1; -; Genomic_DNA.
DR   RefSeq; YP_003277473.1; NC_013446.1.
DR   STRING; D0J3Y4; -.
DR   GeneID; 8564169; -.
DR   GenomeReviews; CP001220_GR; CtCNB1_1431.
DR   KEGG; ctt:CtCNB1_1431; -.
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; COMT2_1.PE1431; -.
DR   PRODOM; COMT2_1_PE1431.
DR   SWISS-2DPAGE; COMT2_1_PE1431.
KW   DNA gyrase, A subunit;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   898 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTQFAKETLP ISLEEEMRRS YLDYAMSVIV GRALPDARDG LKPVHRRVLY AMHELNNDWN
     RPYKKSARIV GDVIGKYHPH GDSAVYDTIV RMAQDFSLRH MLVDGQGNFG SVDGDSAAAM
     RYTEIRLSKI AHEMLGDIDK ETVDFGPNYD GSEQEPLVLP SRLPNLLVNG SSGIAVGMAT
     NIPPHNLNEV VDGCLHLLQN PEASIDELME IIPAPDFPTA GIIYGINGVK EGYRTGRGRV
     VMRAKCHFED IDKGQRQSII VDELPYQVNK KTLQERMAEL VHEKKIEGIS HIQDESDKSG
     MRLVIELKRG EVPEVVLNNL YKLTQLQDTF GMNMVALVNG QPKLCNLKDL IQVFLEHRRE
     VVTRRTVFEL RKARDRGHVL EGLAVALANI DDFIAIIRNA PTPPVAKAAL MEKSWDSKLV
     REMLTRTRTD GGVVNADDYR PEGLEVEFGM QQNGLYRLSE TQAQEILQMR LQRLTGLEQD
     KIVAEYKDVM SVIEDLLDIL AKPERVSIII GEELNAVKAE FGQSKKGERR STVEYSAQDL
     STEDLITPTD MVVTLSHTGY IKSQPLSEYR SQKRGGRGKQ ATATKEDDWI DQLFIANTHD
     YLLCFSNRGR MYWLKVWEVP SGSRGSRGRP IVNMFPLQEG EKINVVLPLT GENRSFPEDH
     FVFMATSMGT VKKTALTEFS NPRKAGIIAV GLDEGDYLIG AALTDGKHDV MLFSDGGKAV
     RFDENDVRPM GRNARGVRGM NIEEHQNVIA MLVAEADDGT GNVVAGSQSV LTATENGYGK
     RTAISEYTRH GRGTKGMIAI QQSERNGKVV AATLVAPEDE IMLITDTGVL VRTRVAEIRE
     LGRATQGVTL INLDEGAKLI GLQRIVENDA NDNAGEDGEA DDSGSAGAEG AAESGDAS
//

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