ID W2T8F4_NECAM Unreviewed; 1495 AA.
AC W2T8F4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-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=NECAME_10714 {ECO:0000313|EMBL:ETN77909.1};
OS Necator americanus (Human hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC Necator.
OX NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN77909.1, ECO:0000313|Proteomes:UP000053676};
RN [1] {ECO:0000313|Proteomes:UP000053676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441737; DOI=10.1038/ng.2875;
RA Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT "Genome of the human hookworm Necator americanus.";
RL Nat. Genet. 46:261-269(2014).
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 -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00011080}.
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DR EMBL; KI660143; ETN77909.1; -; Genomic_DNA.
DR RefSeq; XP_013300136.1; XM_013444682.1.
DR STRING; 51031.W2T8F4; -.
DR EnsemblMetazoa; NECAME_10714; NECAME_10714; NECAME_10714.
DR GeneID; 25350743; -.
DR KEGG; nai:NECAME_10714; -.
DR CTD; 25350743; -.
DR OMA; TWTQDFK; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000053676; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd16930; HATPase_TopII-like; 1.
DR CDD; cd00187; TOP4c; 1.
DR CDD; cd03365; TOPRIM_TopoIIA; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.1490.30; -; 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; 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; 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; 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; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ETN77909.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053676}.
FT DOMAIN 408..525
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1093..1120
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1278
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1495 AA; 169234 MW; 1AB1924EE69D5BAA CRC64;
MSESDDSDFF IDESPKKKAP AKKPAGEKKA PAKPKEQKEP KDKKEKIADI SMAMTEEDKN
VFTNIDQASK TGKKLAIEDI YQKKSQLEHI LLRPDTYIGS VEYTEKTPMW IYDMQTEKLV
MKDIQYVPGL YKIYDEILVN AADNKQRDPK MNCIKINIEK DKNQISIFNN GKGIPVVHHK
VENMYVPEMI FGTLLTSSNY DDSQRKVTGG RNGYGAKLCN IFSTEFTLET SSKEFGKAFK
QTWINNMTKD KDCQIAKAAG EDYTKVTFKP DLSKFRMKEL DDDIIGLMCR RAFDVAGSTK
GVKVLLNGKV LPVQGFKQYV EQYTKDLTGP TGEPAKVVYE SVSFMKQNEM MILQAINCGV
VDAVLAWVRF KQQEDMNKKC SGKKATKLKG IPKLEDANDA GTKNSQLCTL ILTEGDSAKT
LAVSGLGVVG RDRYGVFPLR GKLLNVREGN IKQVAENAEV NALIKILGLQ YKKKYETEED
FKSLRYGKVM VMADQDQDGS HIKGLVINFI HHNWPSLIQR NFVEEFITPI VKATKGKEEL
SFFSIPEYNE WRNNTDNWKT FKIKYYKGLG TSTSKEAKEY FSDMVRHRIR FKYGGTEDDN
AVDMAFSKKK IEERKDWLTK WMAEKKERRT RGLEEEYLYN KDTRAVTFSD FVNKELVLFS
NTDNERSIPS LVDGFKPGQR KVLFACFKRA DKREVKVAQL AGAVGELSAY HHGEASLMGT
IINLAQDFVG SNNVNLLLPI GQFGTRLQGG KDSASPRYIF TQLSPVARTI FPVPDDNVLR
FLFEENQRIE PEWYCPIIPM VLVNGASGIG TGWSTSIHNY NPREICENMR KLIRGEQPKP
IAPWFKNFRG TIEQLDPSRY VCSGEVAVLS DDTIEITELP VKTWTQTYKE TVLEPMLESS
EKKSPIISDF KEYHTDTTVR FVIKVASGKL RDLEAEGLHK VFKLQTVLNT TSMVLFDAAG
CLRKFNTPEE ICAEFFETRK QKYIERKAFM EGMLRAQSNR LTNQARFILA KIKGEILMEN
KKKAAIVEQL IKKGFDPDPV KKWKELQKKK ELELSGEYDV TEEEEQEEEE VVGDKEVEKK
LSDYDYLVGM ALIKLSEEEK NKLLKESDDK LRELRDLEAK SWSDLWNADL DTFLEALAKQ
EAKEKADQDV SIKNAMKKFT KEEKPKGKKA AAVTAEVFPS KDGIRIEPSI DKALKEKYDK
IKAAATREKK PKVPKEPKEP KIPKKEGGDI KKFLANEKKS PKKKKKDEWN SDASSSEFSD
NDDPEESAIF DDDDDDVEEV IPQKKNRGAR GVPKRESDVD SNMENGHAGA GDAGDVIMLD
DSSSSPVKTE PKKGAPKRKI VESDVSMDGS SPSQTTEKTE PKKSAPKRKK PLDDSIFEIP
DDDEDEGPPR KKAVAKRAET GGTNIPKKAT KGKTKAETNG SPKMTDFFGK KGKGKKKGGD
SDSEDDITIE DSEPMASRHT SRRQVAKPKY NYGDTDDDED EPKPKRKNVI DSDSD
//
