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Database: UniProt
Entry: A0A0D8ZQ90_9CYAN
LinkDB: A0A0D8ZQ90_9CYAN
Original site: A0A0D8ZQ90_9CYAN 
ID   A0A0D8ZQ90_9CYAN        Unreviewed;      1081 AA.
AC   A0A0D8ZQ90;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=UH38_24330 {ECO:0000313|EMBL:KJH69361.1};
OS   Aliterella atlantica CENA595.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Chroococcidiopsidales;
OC   Aliterellaceae; Aliterella.
OX   NCBI_TaxID=1618023 {ECO:0000313|EMBL:KJH69361.1, ECO:0000313|Proteomes:UP000032452};
RN   [1] {ECO:0000313|EMBL:KJH69361.1, ECO:0000313|Proteomes:UP000032452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CENA595 {ECO:0000313|EMBL:KJH69361.1,
RC   ECO:0000313|Proteomes:UP000032452};
RA   Rigonato J., Alvarenga D.O., Branco L.H., Varani A.M., Brandini F.P.,
RA   Fiore M.F.;
RT   "Draft genome of a novel marine cyanobacterium (Chroococcales) isolated
RT   from South Atlantic Ocean.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC       {ECO:0000256|ARBA:ARBA00010708}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJH69361.1}.
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DR   EMBL; JYON01000050; KJH69361.1; -; Genomic_DNA.
DR   RefSeq; WP_045057305.1; NZ_JYON01000050.1.
DR   AlphaFoldDB; A0A0D8ZQ90; -.
DR   STRING; 1618023.UH38_24330; -.
DR   PATRIC; fig|1618023.3.peg.1971; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000032452; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
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 (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   CDD; cd16928; HATPase_GyrB-like; 1.
DR   CDD; cd00081; Hint; 2.
DR   CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 2.
DR   Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR002288; DNA_gyrase_B_C.
DR   InterPro; IPR011557; GyrB.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR003586; Hint_dom_C.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR030934; Intein_C.
DR   InterPro; IPR006141; Intein_N.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR001241; Topo_IIA.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR000565; Topo_IIA_B.
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   NCBIfam; TIGR01059; gyrB; 1.
DR   NCBIfam; TIGR01443; intein_Cterm; 1.
DR   NCBIfam; TIGR01445; intein_Nterm; 1.
DR   PANTHER; PTHR45866:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF00986; DNA_gyraseB_C; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF14890; Intein_splicing; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   PRINTS; PR01159; DNAGYRASEB.
DR   PRINTS; PR00418; TPI2FAMILY.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00306; HintN; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 2.
DR   PROSITE; PS50818; INTEIN_C_TER; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032452};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          851..874
FT                   /note="Intein C-terminal splicing"
FT                   /evidence="ECO:0000259|PROSITE:PS50818"
FT   DOMAIN          891..976
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   1081 AA;  123200 MW;  7FD1BF25F8F33AF5 CRC64;
     MTSSYSADQI QVLEGLEPVR KRPGMYIGTT GPRGLHHLVY EVVDNSIDEA LAGHCTHIEI
     DLNADGSVTV TDDGRGIPTD THPQTGKSAL ETVMTVLHAG GKFGGGGYKV SGGLHGVGIS
     VVNALSEFVE VTVWREKRVF LQRFERGIPV GELQSKPHKE PRTGTSVTFK PDAEIFTVGT
     EFDYITLAGR LRELAYLNAG VKITFTDNRL DVLKASEPKV ETYEYKGGIK EYVAYMNRDK
     QPLHEEIIFV QGERNDVQVE VALQWCTDAY TDNLLGFANN IRTVDGGTHL EGLKAVLTRT
     MNAIARKRNK IKENEPNLSG EHVREGLTAV ISVKVPDPEF EGQTKTKLGN TEVRGIVDSL
     VGEVLTEYLE FRPPVADQIL DKAIQAFKAA EAARHARELV RRKSVLESSP LPGKLADCSS
     RDPSESEIYI VEGDSAGGCW HGDTLVALAD GRNLSFKEIV AEQEMGKEHF CYTIRHDGNI
     GIERIIHPRI TKTDAEVIKV TLDNGETLIC TPDHPFMLRD GTYKAAASLT PDDSLMPLYR
     KISNKSEPKI TIDGYEMVWN PRSDSWLFTH LVADWYNRWQ GVYAKSAGEH CHHLDFNKLN
     NNPTNLRRIP ADEHLKIHQA HLEKTLHRPD VIDKCRKVHQ GETFRTKMSE RMRQPKTRQI
     LSSNAKAQWE NEAYKAYMAA KWNEFYSSND AYRAANHEQL NLAQQEYWSN EANCIAQAQR
     VRDYFENNPQ ARAAHSDLAK QQWQDEALIE WRRNKTQEQW TDEFRAKRQA ALNKIYYSKT
     IAALKQIEIE QGNLDLDAYR AYRLETKDKS LLRFETFCDR YFQGKQELAH EAVSNYNHRI
     VSIERLEERI DVYDIEVPHT HNFALASGIF VHNSAKQGRD RRFQAILPLR GKILNIEKTD
     DAKIYKNTEI QALITALGLG VKGEEFDASQ LRYHRIVIMT DADVDGAHIR TLLLTFFYRY
     QRSLIEQGYI YIACPPLYKI ERGRNHYYCY SDRELTNLVQ HEFPANANYT IQRFKGLGEM
     MPTQLWDTTM NPETRTLKQV EIEDAAEADR IFTVLMGDRV APRREFIETY GPRLNLAELD
     I
//
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