(data stored in SCRATCH3701 zone)

HOGENOM6: KOSOT_1_PE18

ID   KOSOT_1_PE18                         STANDARD;      PRT;   812 AA.
AC   KOSOT_1_PE18; C5CHA8;
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   RecName: Full=DNA gyrase subunit A; EC=5.99.1 3; (KOSOT_1.PE18).
GN   Name=gyrA; OrderedLocusNames=Kole_0018;
OS   KOSMOTOGA OLEARIA TBF 19.5.1.
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Kosmotoga.
OX   NCBI_TaxID=521045;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS KOSOT_1.PE18.
CC       Kosmotoga olearia TBF 19.5.1, complete genome.
CC       NRRL Y-1140) chromosome F, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:GYRA_KOSOT
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 (Potential).
CC   -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family.
CC   -!- GENE_FAMILY: HOG000076278 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C5CHA8; -.
DR   EMBL; CP001634; ACR78747.1; -; Genomic_DNA.
DR   RefSeq; YP_002939751.1; NC_012785.1.
DR   STRING; C5CHA8; -.
DR   GeneID; 7968843; -.
DR   GenomeReviews; CP001634_GR; Kole_0018.
DR   KEGG; kol:Kole_0018; -.
DR   ProtClustDB; PRK05560; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   HAMAP; MF_01897; GyrA; 1; -.
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; 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; 2.
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; KOSOT_1.PE18; -.
DR   PRODOM; KOSOT_1_PE18.
DR   SWISS-2DPAGE; KOSOT_1_PE18.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   812 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPEEIISRSI NDEMITSYML YSMSVIVGRA IPDVRDGLKP VQRKILFGML ELGLRHNQSY
     KKSARIVGEV MGKFHPHGDM AIYDALVRMA QPFSMRYPLI QGQGNFGSID RDPPAAMRYT
     EARMQRLAEE LLADIDKNTV KMIPNFDGSL IEPEVLPAKA PNLLMNGASG IAVGMMTNIP
     PHNLSELVEA LTALIDNPDA TIEELMEYVK GPDFPTGGII MGRDGIKKMY ETGRGRMVVR
     GVAEIEEAKG GTRIVISEIP YGVSKADLIQ QIANVAQNVR DIQVRNVRDE SDKRGLRVVI
     ELKRGADPNV VLNLLYKHTQ LQTTFGAHML VIDEKKRPKL MNLKEIFQAF IKHRYEVVKR
     RTEYELEQAS KKAHILEGLT KASRAIDTVV DIIRNSKNIQ EASVNLQETL EITPEQSQAI
     LEMRLGKLTA LEIDKLVTEY AELVEKIKEY REILSDDKNI YQIIKKELQE LEAQYGDARR
     TKISIDGNTD FNVEDVIPDD EVVVTVTKKG YIKATPLEDY RKQGRGGKGI RGVKTTDADF
     VTNVVSTTRL SKTVVITSKG KAYFINNYEL ECTSRSSRGK LLANYVKIEP DETVQAVLSV
     KREEVANKHL IITTRKGKIK RTPFEAFINS RTSGIKAITL NEGDSVVDAG ISTSEEETII
     ISTRKGMVIR FPISQIRPMG RTAAGVKAMA LRGDDEVVSA TIVLPVDERY LFTATERGVG
     KRTPLSEYRP QHRAGMGVKN IYGLERTGYV VGSLVVTNED EIIVITKNGM SIRIPAADIR
     PTGRVTKGVK VVELRDDDTV ASLAVVVDQA EV
//

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