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Database: UniProt
Entry: D2VKE9_NAEGR
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Original site: D2VKE9_NAEGR 
ID   D2VKE9_NAEGR            Unreviewed;      1251 AA.
AC   D2VKE9;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=Type IIB DNA topoisomerase {ECO:0000313|EMBL:EFC42675.1};
GN   ORFNames=NAEGRDRAFT_50278 {ECO:0000313|EMBL:EFC42675.1};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN   [1] {ECO:0000313|EMBL:EFC42675.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC42675.1,
RC   ECO:0000313|Proteomes:UP000006671};
RX   PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA   Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA   Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA   Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA   Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT   "The genome of Naegleria gruberi illuminates early eukaryotic
RT   versatility.";
RL   Cell 140:631-642(2010).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the TOP6A family.
CC       {ECO:0000256|ARBA:ARBA00006559}.
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DR   EMBL; GG738878; EFC42675.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2VKE9; -.
DR   STRING; 5762.D2VKE9; -.
DR   EnsemblProtists; EFC42675; EFC42675; NAEGRDRAFT_50278.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_50278; -.
DR   eggNOG; KOG2795; Eukaryota.
DR   InParanoid; D2VKE9; -.
DR   OrthoDB; 3015043at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006259; P:DNA metabolic process; IEA:InterPro.
DR   CDD; cd00223; TOPRIM_TopoIIB_SPO; 1.
DR   Gene3D; 3.40.1360.10; -; 1.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR002815; Spo11/TopoVI_A.
DR   InterPro; IPR013049; Spo11/TopoVI_A_N.
DR   InterPro; IPR036078; Spo11/TopoVI_A_sf.
DR   InterPro; IPR034136; TOPRIM_Topo6A/Spo11.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR33099; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR33099:SF13; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF21180; TOP6A-Spo11_Toprim; 1.
DR   Pfam; PF04406; TP6A_N; 1.
DR   PRINTS; PR01550; TOP6AFAMILY.
DR   SUPFAM; SSF56726; DNA topoisomerase IV, alpha subunit; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:EFC42675.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT   DOMAIN          51..106
FT                   /note="Spo11/DNA topoisomerase VI subunit A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04406"
FT   REGION          1203..1251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1215..1237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1251 AA;  143573 MW;  6808D79BFEEF2EEC CRC64;
     METIQVRERI EEKVLAFVRE LVSSPSSDIP NEKGFLLKDL TKYPSTFISK FQVMNLVYQL
     CTLNKFSTKR DLYYCNKPIL KDQTQLDSIL KDLSSSWRVN RHDLHIVPQS KGEVCGPIAW
     KEISLIDIEN RGQQPTTTIV SASKGCNLPS IPHLQIVEFS IPVEVDKVII VEKESVFQVL
     KSQASSLKDT SLIITSKGYP DVPTRDFIVT LTKQVAKYQR RSLNIFTLTD GDPYGAEIAN
     VYMNGSLSFE NEKENLTIHS CVDSTEDWHY WVLQTCSRMS WIGVHLNDFD NAPQLISKWK
     DCWMPLEELD LKKINSLNNT QLELDDTVKT QINLQKDLNY KVEIEESSET DSDYCEAYGS
     DFYDDCVQLH ADTIKTSDNL QEFILDAQNK GGSKFTQCGA LDSDFGLPGL QLKLDNEQFK
     TIGFPLSNGS ASELIQFCSK APYGRGEDTI YDENVRKTWQ LDPSRFEITN PTWDDLIDGL
     VDNEIRDGLG ISKHLRLSAN LYKLLVYEEG GHFQFHKDSE KEERMFGTLV VQLPSEYSGG
     EIIVRHGEEE EEYDFASVSR YTPHFISFYA DCEHMIKNVN SGYRVCLIYN LCFSGNKESK
     PTLKGYEELA KRLQQIVSEW NADAKDVDTL YRMYVFQHQY SQKSLDPENL KGSDYNIYDI
     LERYAEEYQD LVLDLGIMER KVEGFDDPEV SLEYIFGSQQ RKIDVPFRSV VCKSALSSMK
     LFHKSINENT GNEGSTKEKQ YRNACLMIYP KKCQQRICLK FGFSFCSKIL PSFIESNSRE
     NSIAFVKQML AKKNIYLWGD EEKVVIQSII QLNDVELAKL VIGIDQKSLS SLISHFTIEP
     FRETISENLC KKRYMKEFIG SLIEINDVPL IQMTMPKYSV NKYDHLYDSS CFEKLIILAQ
     KCTYSMHSTV VENIVEDYYK YASYKESITK LIDLLKDTSI YEKLIVKELA KNSIPNQRGR
     GSYENKELDL PLIIKIANQI GVEKLKNLRF SFSKWLTSEN CLNMVLSTMS CKPLSELLIE
     WMLYDHRDCF LDLKFATSFI RMLHNHSWND FITRACRVVL SVASEENYST LVAPLIEVVS
     NIMPKSDQLD ILLNWSIDLI DDGIRTKKFI IPLPNFSVKS SISCICSDCK ILKQFLWSET
     ERTCSITGLV KELSHIESMV APIREIQKQR VQKSIILTKL VISERLVKQA TELNNAAKTK
     LESLLKKRRT PPEESTDNNS TLQLEVAPSS SIEPPNKKSK TDAPEIICID D
//
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