ID A0A0B1SZC7_OESDE Unreviewed; 872 AA.
AC A0A0B1SZC7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=OESDEN_10923 {ECO:0000313|EMBL:KHJ89256.1};
OS Oesophagostomum dentatum (Nodular worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Strongylidae; Oesophagostomum.
OX NCBI_TaxID=61180 {ECO:0000313|EMBL:KHJ89256.1, ECO:0000313|Proteomes:UP000053660};
RN [1] {ECO:0000313|EMBL:KHJ89256.1, ECO:0000313|Proteomes:UP000053660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OD-Hann {ECO:0000313|EMBL:KHJ89256.1,
RC ECO:0000313|Proteomes:UP000053660};
RA Mitreva M.;
RT "Draft genome of the hookworm Oesophagostomum dentatum.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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 family.
CC {ECO:0000256|ARBA:ARBA00011080, ECO:0000256|RuleBase:RU362094}.
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DR EMBL; KN554486; KHJ89256.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B1SZC7; -.
DR Proteomes; UP000053660; Unassembled WGS sequence.
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:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd03481; TopoIIA_Trans_ScTopoIIA; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.1490.30; -; 1.
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 Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
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; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR InterPro; IPR001154; TopoII_euk.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR031660; TOPRIM_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR10169:SF38; DNA TOPOISOMERASE 2; 1.
DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF16898; TOPRIM_C; 1.
DR PRINTS; PR01158; TOPISMRASEII.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 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; PS00177; TOPOISOMERASE_II; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362094};
KW Reference proteome {ECO:0000313|Proteomes:UP000053660};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 352..469
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 872 AA; 98783 MW; 0FC38DFC4B75BD65 CRC64;
MSSFVLNFSE QGKISVFNNG RGLPIEIHPK EGIYVPTLIF GNLFTSSNYD DAEIKVVGGR
NGYGAKLCNI FSKEFIVETS SHESGRSFKQ VWTNNMRDCE EPIIVESQNA IDGTKITFTP
DVAKFGLSSL DDAICEMFKK RTFDVAGTLR GVKVYYNGNL IQGYALQVPS FEEYVRLYSS
DSSADDLLFV NAGERWQWAV KRSASGFQQI SFVNNIATIK GGKHVDYIAD QLINTIKPLV
DSQLKTGIKK VVIKNHLCVF VNALIENPSF TSQTKEVLTT PAAEFGSKCE CNIAKVQSWA
LSSGLVDELV REAQAKENRP PKKVKSKAED LSDIVKLEDA NWAGDHGHSQ DCRLLITEGD
SAKALAVAGL EVVGRDRYGV YPIQGKLTNV SGLSEEKAIA SKEVNHLMRI LGLKYGQDYS
ILENRRKLRY GGVIILTDQD EDGSHIKGLI INFLHTFWPE LLHGDFIESF VTPLLKARYK
GECLSFYSMD EYKKWKERTE NAEKYTVKYY KGLGTSTSKE AREYFSNIEK YLVRFRYEDE
SDKERIDMVF DRGRADDRKV WINKMLQKES LDNQFRNETS YKDFIDNEFF RYSLLDLKRS
IPSVVDGLKP SQRKVLHTLL RRSSNKEIKV NQLAAAVALN EAYHHGEGTL VTTIVRLAQD
FLGANNVCLL EPLGQFGTRH EGGDDAASAR YIYTKLSPVT RQIFPAADDD LLNYLQEENQ
LIEPEWYCPI IPMVLVNGAE GIATGWSTLV LGHNIREVID NVRRLIDGDD IKKMTPSFSD
FSGKIEELDT NRYAISGSYK IVPSQRKNTP NLRIEITELP VGEWTNRYKQ NTLHTLQKKG
LISGFKEYHT ERNVRFVVEL SKEFTLKLRK DA
//
