(data stored in SCRATCH zone)

SWISSPROT: C1E1M3_MICCC

ID   C1E1M3_MICCC            Unreviewed;       703 AA.
AC   C1E1M3;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE            EC=5.6.2.3 {ECO:0000256|RuleBase:RU362094};
GN   ORFNames=MICPUN_79742 {ECO:0000313|EMBL:ACO61766.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO61766.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO61766.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W.,
RA   Gready J.E., John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F.,
RA   Moreau H., Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I.,
RA   Piegu B., Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T.,
RA   Zelensky A., Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W.,
RA   Van de Peer Y., Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the
RT   marine picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
CC   -!- FUNCTION: Control of topological states of DNA by transient
CC       breakage and subsequent rejoining of DNA strands. Topoisomerase II
CC       makes double-strand breaks. {ECO:0000256|RuleBase:RU362094}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.3;
CC         Evidence={ECO:0000256|RuleBase:RU362094};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362094}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC       {ECO:0000256|RuleBase:RU362094}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001324; ACO61766.1; -; Genomic_DNA.
DR   RefSeq; XP_002500508.1; XM_002500462.1.
DR   STRING; 296587.XP_002500508.1; -.
DR   GeneID; 8241699; -.
DR   KEGG; mis:MICPUN_79742; -.
DR   HOGENOM; HOG000075154; -.
DR   InParanoid; C1E1M3; -.
DR   KO; K02470; -.
DR   OMA; IYIACPP; -.
DR   OrthoDB; 514092at2759; -.
DR   Proteomes; UP000002009; Chromosome 3.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd00075; HATPase_c; 1.
DR   CDD; cd03366; TOPRIM_TopoIIA_GyrB; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   InterPro; IPR002288; DNA_gyrase_B_C.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR001241; Topo_IIA.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034160; TOPRIM_GyrB.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF00986; DNA_gyraseB_C; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1E1M3.
DR   SWISS-2DPAGE; C1E1M3.
KW   ATP-binding {ECO:0000256|RuleBase:RU362094};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002009};
KW   DNA-binding {ECO:0000256|RuleBase:RU362094};
KW   Isomerase {ECO:0000256|RuleBase:RU362094};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362094};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002009};
KW   Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT   DOMAIN      481    596       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   COILED      438    458       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   703 AA;  75891 MW;  FB196801CDE1A9F0 CRC64;
     MPSRGASSSV TPREAIAVGD EEAGGAPRDN TGDIIAAKAA AKAAAAAATG GSDAYGASSI
     QVLKGLEPVR KRPGMYIGNT STKGLHHMVW EVLDNGVDEV QAGHASLITV TVEADGSVAV
     EDDGRGIPTD VHPATGTSSL ETVLTVLHAG GKFGGDESGY HVSGGLHGVG ISVVNALSDS
     TEVTVWRGDR EYRQSFSRGA ALAPMTEGSQ DVANVGKKKG TRVRFKPDPS IFKERQDFDP
     NIILARMKEL AFLNSTATDE ASMDEGDVKK TEEYYEEVLS FPGGLKDYVV DLNEGAEPLH
     EPITFRAEVD GVQVEGALQW TKEAYTDTLL GYANSIRTSD GGTHLDGLKQ SLTRAVNTQA
     RKAKLLKEAD ANLGGEHIRE GLSAVIAVWV PQPEFEGQTK TRLGNPEVRK VVESVIGEQV
     SEHLEFYPNT LGSIFSKASQ AQKAAEAAKR ARELVRRKSV LRSGSLPGKL SDCSVSDPES
     TEIFLVEGDS AGGSAKQGRD RRFQAVLPLR GKILNVERKD EASMYKNTEI SSMVTALGLG
     LKGEPFDESQ LRYSKIVILT DADVDGAHIR TLLLTFLFRY QRGLFEQGKV YVAVPPLYKV
     ESGRAGKNNP PTYCYDEAQL QAHLATLPEG ASRSIQRFKG LGEMMPEQLW STTLNPETRL
     LKRLTVDDAA MANKTFQLLM SDKVAPRREF IETEGPKLED IDV
//

If you have problems or comments...

PBIL Back to PBIL home page