ID A0A061D1P7_BABBI Unreviewed; 994 AA.
AC A0A061D1P7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=BBBOND_0110140 {ECO:0000313|EMBL:CDR94716.1};
OS Babesia bigemina.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5866 {ECO:0000313|EMBL:CDR94716.1, ECO:0000313|Proteomes:UP000033188};
RN [1] {ECO:0000313|Proteomes:UP000033188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bond {ECO:0000313|Proteomes:UP000033188};
RX PubMed=24799432; DOI=10.1093/nar/gku322;
RA Jackson A.P., Otto T.D., Darby A., Ramaprasad A., Xia D., Echaide I.E.,
RA Farber M., Gahlot S., Gamble J., Gupta D., Gupta Y., Jackson L.,
RA Malandrin L., Malas T.B., Moussa E., Nair M., Reid AJ., Sanders M.,
RA Sharma J., Tracey A., Quail M.A., Weir W., Wastling J.M., Hall N.,
RA Willadsen P., Lingelbach K., Shiels B., Tait A., Berriman M., Allred D.R.,
RA Pain A.;
RT "The evolutionary dynamics of variant antigen genes in Babesia reveal a
RT history of genomic innovation underlying host-parasite interaction.";
RL Nucleic Acids Res. 42:7113-7131(2014).
CC -!- FUNCTION: Control of topological states of DNA by transient breakage
CC and subsequent rejoining of DNA strands. Topoisomerase II makes double-
CC strand breaks. {ECO:0000256|RuleBase:RU362094}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185,
CC ECO:0000256|RuleBase:RU362094};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362094}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {ECO:0000256|RuleBase:RU362094}.
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DR EMBL; LK391707; CDR94716.1; -; Genomic_DNA.
DR RefSeq; XP_012766902.1; XM_012911448.1.
DR AlphaFoldDB; A0A061D1P7; -.
DR STRING; 5866.A0A061D1P7; -.
DR EnsemblProtists; CDR94716; CDR94716; BBBOND_0110140.
DR GeneID; 24563257; -.
DR KEGG; bbig:BBBOND_0110140; -.
DR VEuPathDB; PiroplasmaDB:BBBOND_0110140; -.
DR OMA; QLWSTTM; -.
DR OrthoDB; 231762at2759; -.
DR Proteomes; UP000033188; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
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; IPR006171; TOPRIM_domain.
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; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00433; TOP2c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362094};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362094};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362094};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362094};
KW Reference proteome {ECO:0000313|Proteomes:UP000033188};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 687..837
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 899..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 994 AA; 110032 MW; 34E3E1D003D76D1C CRC64;
MRFRVWNHAN CCAWWSAACA IWACAILLAA APALAIAERF AGCSSWRSKA RHGALEPFVA
TYTFRFHSEA GGSILNAEKQ SSHMQSRKPF VGQRTTPSSA AAFIWAVSND LPTVASAKPI
SKVSNRITRN DGKQGIYRKV ELCAEKDDIL DEDEDENIDI TLDNDCDAVA DDVNVNLCAD
GEINESVATV AEGDSVDDQN ANSPDVPAPR EVQYSTSDIV VLQGLDAVRK RPGMYIGNTG
ESGVHQLLFE ILDNSVDEYL AGACNRITVT LRADGSAEVM DNGRGIPCEI SESTGRSGLE
TVLTVLHSGG KFNDAATQTQ DHEDEFYDTS VSRKFRSQHV RGLRKKLKDA SNAPYEYSSG
LHGVGLSVVN ALSKWLHAEV YKGTRVYTME LSKGQVMSPL SMSRGQKRTG TKISFLPDYE
DVFRIHHEHI SDGECKGCVE AFHFDTVRTR VEELSYVNPM LTLRLVDERK VNEDGTFWEE
TFMHKGGTRE FLQDIIKDRT PLYKAANIIN IRGKSNGVEV ETSLSWSAEP SAAQLRGFAN
NVSTVAGTHI DGFKAAITKA VNHCCRRSGY FKAKAPPLSG EFIREGMTAI VSVKLMGAEF
DGQTKSKLGN QVARTAVERI VSYQMIEILE KHPQLLLAIY NKSLASKKAF EAAKHAKELA
QQKNANFLTT GLPTKLSDCT SNDMDATEIF IVEGESAAGN AKQARNRRFQ AVLPLKGKIL
NIEKINSDLK VMENEEIKLL ISSLGIAVNP RTWRQDTLTH VETMVPTGTQ EIVLGETEDG
GKILSPLPPL PLRYGKIILL TDADVDGAHL RILLLGLLFR ICPQLYEHGR VYVACPPLYR
ITNMRRSSSS KGDGQSRSAY TYAWSEDELP EALQREMSSR QAGRVGDQSG KMLDIFSEKS
EESTDDRAGD RPTHKLSDSR GLSVQRFKGL GEMMAQQLWD TTMDPEKRVL RRISVQDGLR
ASQMLELLMG SDVQQRKEFI FANSDTFQLQ DLDR
//
