ID A0A090MXK7_STRRB Unreviewed; 1414 AA.
AC A0A090MXK7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=SRAE_2000028100 {ECO:0000313|EMBL:CEF65604.1,
GN ECO:0000313|WBParaSite:SRAE_2000028100.1,
GN ECO:0000313|WormBase:SRAE_2000028100};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF65604.1};
RN [1] {ECO:0000313|EMBL:CEF65604.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000028100.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF65604.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000028100.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
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; LN609529; CEF65604.1; -; Genomic_DNA.
DR STRING; 34506.A0A090MXK7; -.
DR EnsemblMetazoa; SRAE_2000028100.1; SRAE_2000028100.1; WBGene00260474.
DR WBParaSite; SRAE_2000028100.1; SRAE_2000028100.1; WBGene00260474.
DR WormBase; SRAE_2000028100; SRP08234; WBGene00260474; -.
DR eggNOG; KOG0355; Eukaryota.
DR OMA; NESMDYN; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000035682; Chromosome X.
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 CDD; cd16930; HATPase_TopII-like; 1.
DR CDD; cd00187; TOP4c; 1.
DR CDD; cd03481; TopoIIA_Trans_ScTopoIIA; 1.
DR CDD; cd03365; TOPRIM_TopoIIA; 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 Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
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; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
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 InterPro; IPR034157; TOPRIM_TopoII.
DR PANTHER; PTHR10169:SF62; DNA TOPOISOMERASE 2 TOP-2-RELATED; 1.
DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR Pfam; PF02518; HATPase_c; 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.
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:UP000035682};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 717..1204
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1145
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1414 AA; 161720 MW; F300BEDFCDADE437 CRC64;
MSDYDEMDLD DAVPSTSKLT LKERNGPSKD DLKVFTNIDE SRTNGKQTIE QMYQKKSQLE
HILLRPDTYI GSVEYTDKGV AWVYDMDEDK LVQREISYVP GLYKIFDEIL VNAADNKQRD
KKMNLIKVDI DKKNNTISVF NNGKGIPVAH HKVEKMYVPE LIFGTLLTSS NYNDDEKKTT
GGRNGYGAKL CNIFSTEFTL ETSSKEYKKK FKQTWINNMT KDKEAEISKA TEDDYTKVTF
KPDLKKFKMK ELDDDIVGLM ARRAYDIAGT TPGVRVYLNG KCIPIKSFKE YAEKYVESAI
GNEEEKPKII YEKINDRWEV ALTVSEKGFQ SVSFVNSIAT SKGGRHVDYI ADQITTNLVD
TVKKKAGGAK SGVNVKPFQI KNHMWIFVNC LIENPTFDSQ TKENMTLQAK SFGSKAEMTE
KFYKEVLKCG VVEAVLSWVR FKQQEQADKK CSTKKSTKVK GIPKLEDANE AGTKNSSKCT
LILTEGDSAK TLAVSGLGVV GRDFYGVFPL RGKMLNVRDC PMKQINDNQE IGHMIKILGL
QYRLKYETEE ERKTLRYGRV MIMADQDQDG SHIKGLLINW IHCNWPALMK NNFVEEFITP
IVKASKGSTS ISFFSLPEYM EWRNNTDNWK SYKIKYYKGL GTSTSKEAKE YFSDMDRHRI
PFTYSGPECE RAVEMAFSKK KIEARKTWLS NWMREKKDRR ENGGIEEYLY NKDTRSVSFV
EFINKELILF SNMDNERSIP CLVDGLKPGQ RKVLFTCFRR ADKKEVKVAQ LAGAVGEMSA
YHHGEQSLMM TIINLAQDYV GSNNINLLLP IGQFGTRLQG GKDSASPRYI FTQLSPVTKT
IFIPEDENVL RFLFEENQKI EPEWYCPIIP MVLVNGAEGI GTAWSTKIPN YNPRDVTENI
RRLIRGEQMK KMIPWYKHFE GTIMQVDEQK YISSGRVGTL DDETLEITEL PIKMWTQNYK
ESVLEDLSNS TDKSPALIQD YREYHTDQTV KFIVKMTEQN MKKCLSQGVH DILKLQTPIN
TSSMVLFDAE GCLRKFESPE QICQEFFEVR KKKYIERKEF LVGMLEAQSK RLSNQARFIV
CKIKGEIVME NRKKKNIVDQ LIKEKFDPDP VKAWKDYCKK RELEMCGEVE IEEEEANEED
SEEAGGTSTE AGLKKRLADY DYLVNMALIK LSEEEKDRLL EEAGNKLKEL ETLKKKSWAD
LWEHDLEIFE EALKKQEEKE LQDIEGSIKT AQSKLAKGGN SAKNKKNKVN VDAASFKPNP
NAEIVNVEFE ALKNKYEKKP KKVKSQPLPK VKGDEIANAL EDNDLKVPKV KKTKEPKVTK
KASENKNKKE SGGESDKLDD ENAMEVSPVA QKRTKRNVKK APIIIIDSES DIEFASPPPP
ESSQKGSKRK SATPQKAKKS KKAKVLDSSD ESDE
//
