ID A0A1I8CAW7_9BILA Unreviewed; 930 AA.
AC A0A1I8CAW7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE SubName: Full=Toprim domain-containing protein {ECO:0000313|WBParaSite:RSKR_0000258100.1};
OS Rhabditophanes sp. KR3021.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC Rhabditophanes.
OX NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000258100.1};
RN [1] {ECO:0000313|WBParaSite:RSKR_0000258100.1}
RP IDENTIFICATION.
RC STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000258100.1};
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00011080}.
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DR AlphaFoldDB; A0A1I8CAW7; -.
DR WBParaSite; RSKR_0000258100.1; RSKR_0000258100.1; RSKR_0000258100.
DR Proteomes; UP000095286; Unplaced.
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:InterPro.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
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; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
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; 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; 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; SSF56719; Type II DNA topoisomerase; 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}.
FT DOMAIN 1..110
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 738..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 679..733
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 773..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 930 AA; 106677 MW; C8FE73A4A8C2298F CRC64;
DSAKTLAVSG LGVVGRDKYG VFPLRGKFLN VRDASHKQIK ENAEIDALLK IIGLQYRLKY
DKEEDLKTLR YGKVMIMADQ DQDGSHIKGL LINFFHHNWP ALLKTTFLEE FITPIVKVTK
DGRSTSFFSL PEYMKWRVDH NNGKGFKIKY YKGLGTSTSK EAKEYFSDMA KHRIPFKYGD
EQCSVSIEMA FAKSKVEKRK EWLTSWMEER KRQRLTNEQE VYLYNENTKS ISYKQFIDQE
LILFSNMDNE RSIPNLMDGL KPGQRKVLFT CFKRADKKEV KVAQLAGAVG EMSAYHHGEV
SLMMTIVGLA QDFVGSNNIN LLLPIGQFGT RLQGGKDSAS PRYIFTQLSP LTKTIFKQED
EHVLKFLNEE NQRIEPEWYC PIIPMILING TEGIGTAWST KIPNYNPRDV VENIRRLINN
EETKVMAPWY RRFEGTMVKL GEGRYISNGR IAVINDTTVE ITELPIKTWT QKYKETVIDK
LNDNPDKNAA FNISDYKEYH TDSTVKFVVK MNEDKLAAAE REGMHKVFQL QSIINTTSMV
LFDSEGCLRR FDSPDEIMKD FFKCRRQKYI ERKIFLEGML QAQSDKLSAQ AKFIMAKIKG
EIKMENVKKA EIIKKLRDLG YLPDPLKKWN DDEKKRREKE DKMDVVEEIE EEDTVVKDSV
GDYDYLVGMA LIKLSEEEKD KLIRESKDKL TELEILKKKT WSDLWLADLD EFMAALKKHE
DKEEAEIEKA IRDATAKLKK EAGSAKSKRG GLAAAADFKP DPRGINVVPD IQSYKDKFEE
KPKKEKAPKK EKAPKKEKAV KKVENHGGDV SSFLVKKENG TGKKKASKKN ESDSDDTDEL
SEFDSDDEEE NSKPRSFSKK SNTSDEEKYS KPNPKKADQK TKPTPKEAGG KRKKTESDGE
ESKSSRNVPT RPAAKKAKLV ISSDEEDSFV
//