(data stored in SCRATCH3701 zone)

HOGENOM6: CHIPD_1_PE5366

ID   CHIPD_1_PE5366                       STANDARD;      PRT;   859 AA.
AC   CHIPD_1_PE5366; C7PUW6;
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; (CHIPD_1.PE5366).
GN   OrderedLocusNames=Cpin_5446;
OS   CHITINOPHAGA PINENSIS DSM 2588.
OC   Bacteria; Bacteroidetes; Sphingobacteria; Sphingobacteriales;
OC   Chitinophagaceae; Chitinophaga.
OX   NCBI_TaxID=485918;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CHIPD_1.PE5366.
CC       Chitinophaga pinensis DSM 2588, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:C7PUW6_CHIPD
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; C7PUW6; -.
DR   EMBL; CP001699; ACU62875.1; -; Genomic_DNA.
DR   RefSeq; YP_003125076.1; NC_013132.1.
DR   STRING; C7PUW6; -.
DR   GeneID; 8361623; -.
DR   GenomeReviews; CP001699_GR; Cpin_5446.
DR   KEGG; cpi:Cpin_5446; -.
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: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; CHIPD_1.PE5366; -.
DR   PRODOM; CHIPD_1_PE5366.
DR   SWISS-2DPAGE; CHIPD_1_PE5366.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   859 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSENTENQQD GRIIQINIEE QMKTAYIDYS MSVIVGRALP DVRDGLKPVH RRVLFGMNEL
     GNNSNKPYKK SARIVGEVMG KFHPHGDASI YDTIVRMAQP WSLRYMLVDG QGNFGSVDGD
     MPAAMRYTEI RLQRMAEAML EDIDKETVDF TLNFDDTLEE PTVLPTRIPN LLINGASGIA
     VGMATNIMPH NLSEVVDGLI AYIDNRDITI EELIKHVKAP DFPTGGIIYG YEGVKQGFET
     GRGRVVVRGK VNVETSKAGR ERLVIYELPY QINKAALHQK IAQLADDKII EGISEARDES
     DRDGMRLVID LKREAIANVV INQLYKYSEL QTSYGINNVA LVKGRPRVLN LKDMLSEFVD
     FRHEVVVRRT RFDLRKAEEK AHILQGYLIA LDHLDEVIAL IRASRTPEEA KEGLMTRFEL
     SEIQSKAILE LRLQRLTGME RDKIKEEYDE VMKLIAYLKE ILSDEGLRFK IIKDELEDVK
     KRFGDERKTE IQYLASEMRM EDIIAEEDVV ITISHLGYIK RTSAYDYRQQ KRGGRGALGG
     KTREEDYIEH LFVASTHHTM LFFTEKGRCY WLKVYEIPEG EKSGKGRAIQ NLINLPTDDK
     IRAIIDIKDL GDKEFISSHY IVLCTANGII KKTLLEDFSR PRQNGVNAIT INEGDQLLEA
     KLTNGNSQIM MAIKSGRAIR FPENTVRDTG RGAIGVRGIE VDNDKDEVVG MICVNKEDET
     RTVLVVSEKG FGKRTDIEEY RITNRGGKGV KTINITEKTG SLIAILDVTE KDDLMITCKS
     GITIRMAVAD IREAGRATQG VRLIRLDDSD EIAAVARLDE QEEQRLDEEA LEGMEGNESN
     QDGSSATQGD APVDETPAE
//

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