UniProt: A0A0N4YME6

Database: UniProt
Entry: A0A0N4YME6_NIPBR

LinkDB:  A0A0N4YME6_NIPBR 
Original site:  A0A0N4YME6_NIPBR

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (25)   
   InterPro (16)   
   Pfam (5)   
   PROSITE (2)   
   SMART (2)   
All databases (32)   

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ID   A0A0N4YME6_NIPBR        Unreviewed;      1610 AA.
AC   A0A0N4YME6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE            EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN   ORFNames=NBR_LOCUS18341 {ECO:0000313|EMBL:VDL82066.1};
OS   Nippostrongylus brasiliensis (Rat hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Heligmosomidae; Nippostrongylus.
OX   NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0001834001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:NBR_0001834001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL82066.1, ECO:0000313|Proteomes:UP000271162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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; UYSL01023341; VDL82066.1; -; Genomic_DNA.
DR   STRING; 27835.A0A0N4YME6; -.
DR   WBParaSite; NBR_0001834001-mRNA-1; NBR_0001834001-mRNA-1; NBR_0001834001.
DR   OMA; TWTQDFK; -.
DR   Proteomes; UP000038043; Unplaced.
DR   Proteomes; UP000271162; 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: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.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362094};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000271162};
KW   Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT   DOMAIN          504..621
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1172..1194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1274..1610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1209..1274
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        18..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1175..1189
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1301..1371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1372..1392
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1393..1440
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1451..1465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1539..1557
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1584..1610
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1610 AA;  182674 MW;  C784784FAA803B04 CRC64;
     MSDSDDSDFF VDSQSSPKKK APAKKPPGEK KAPAKPKEPK EKKEKIADIS MSMTEEDRNV
     FVNIDKVSKT GKKLAIEEMY QKKTQLEHIL LRPDTYIGSV EYTEKTPMWI YDSEKEKLVL
     KDIQYVPGLY KIFDEILVNA ADNKQRDPKM NCIKINIDKE NNKVSIFNNG KGIPVVHHKV
     EQMYVPEMIF GTLLTSSNYD DSERKVTGGR NGYGAKLCNI FSTEFTLETS SKEFGKAFKQ
     TWINNMTKDK EPQIVKATSD DYTKVTFKPD LSKFKMQQLD DDIIGLMSRR AYDIAGSTKG
     VKVFLNGRAL PVQGFKDYVD QYTKDLTGPT GEPAKVVYEN VNDRWEVALT VSEKGFQQVS
     FVNSIATTKG GRHVDYVADQ MVAKLIDVIK KKVGKSTVNV KPFQVKNHMW VFVNCLIENP
     TFDSQTKETM TLQAKSFGSK CELSEKFTKS AISCGVVDSV LAWVRFKQQE DMNKKCSGKK
     ATKLKGIPKL EDANDAGTKN SQLCTLILTE GDSAKTLAVS GLGVVGRDRY GVFPLRGKLL
     NVREGNIKQV AENVEINALL KILGLQYKKK YETEEDFKSL RYGKVMVMAD QDQDGSHIKG
     LVINFIHHNW PSLIQRNFVE EFITPIVKGI IPILFPHILQ RFSNLPARQA TKGKEELSFF
     SIPEYNEWRN NTENWKTYKI KYYKGLGTST SKEAKEYFSD MVRHRIRFKY GGVEDDNAVD
     MAFSKKKIEE RKDWLTKWMA EKKERRTRGL EEDYLYNKDT RAVTFSDFIN KELVLFSNTD
     NERSIPCLVD GFKPGQRKVL FACFKRADKR EVKVAQLAGA VAELSAYHHG EQSLMGTIVN
     LAQDFVGSNN INVLLPIGQF GTRLQGGKDS ASARYIFTQL NPVTRTIFPA VDEHVLRFLF
     EENQRIEPEW YCPIIPMVLV NGASGIGTGW STNIHNYNPR EICENMRLLI RGKEPKALTP
     WFKNFRGTIE KMDASRYVCS GEVAVLGDDT IEITELPIKM WTQTYKESVI EPLLESSDKK
     PALISDFKEY HTDTTVRFVI KVQQGKLREL EAEGLHKVFK LQTVLNTTSM VLFDAAGCLR
     RFNTVEEICA EFFESRKQKY IERKAFMEGM LKAQSDRLSN QARFIVAKIK GEIVMENKKK
     AYIVQQLVQR GFDPDPVKKW KELQRKKELE QTGEFDAAEV EENEEEGEGD KDLDGKLSDY
     DYLVGMALIR LSEEEKNKLL KESDDKMKEL QDLQKKSWQD LWSADLDTFI EALDKQEAKE
     KADLESNIKN AAKKYMKEEK PKGKKAPAFA TEVFPSRDGI RVEPSIDKAL KEKYDKMSKP
     KVPREPKPPK EKKEPKEKKP KKEGDDIKKF MSAEKKSPKK RKAKEWDSDE SSIEFSDTED
     PEENTLFDNS DDDVEEIIPK KDRSRGATKR RLDGDDMENG FGGDDVVHLD DEDSPSAKSA
     PAKKEVKTGS QGDIVDSTPS KKSKTTSKKA PPKAKAGEGS GASKKKEELD DVYEIPDDDD
     DDEKTTSKKA PAKKAPAKKA PAKSKKENGA GSPKMTDFFG AKEKAKGRKR GGASDSDSDD
     EVVLEDDSPV VPRQQSRRPR AVTTYDLGES DDEIEVMPKK KRRLVESDSD
//

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