ID D2VU03_NAEGR Unreviewed; 374 AA.
AC D2VU03;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=NAEGRDRAFT_81222 {ECO:0000313|EMBL:EFC39811.1};
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:EFC39811.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC39811.1,
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 -!- 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 -!- 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; GG738897; EFC39811.1; -; Genomic_DNA.
DR RefSeq; XP_002672555.1; XM_002672509.1.
DR AlphaFoldDB; D2VU03; -.
DR STRING; 5762.D2VU03; -.
DR EnsemblProtists; EFC39811; EFC39811; NAEGRDRAFT_81222.
DR GeneID; 8860845; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_81222; -.
DR eggNOG; KOG2795; Eukaryota.
DR InParanoid; D2VU03; -.
DR OrthoDB; 169019at2759; -.
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 GO; GO:0022414; P:reproductive process; IEA:UniProt.
DR GO; GO:0019953; P:sexual reproduction; IEA:UniProt.
DR CDD; cd00223; TOPRIM_TopoIIB_SPO; 1.
DR Gene3D; 3.40.1360.10; -; 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; PTHR10848; MEIOTIC RECOMBINATION PROTEIN SPO11; 1.
DR PANTHER; PTHR10848:SF0; MEIOTIC RECOMBINATION PROTEIN SPO11; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 123..182
FT /note="Spo11/DNA topoisomerase VI subunit A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04406"
FT DOMAIN 230..351
FT /note="Topoisomerase 6 subunit A/Spo11 TOPRIM"
FT /evidence="ECO:0000259|Pfam:PF21180"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 43490 MW; 1EEAA46895C6CDE8 CRC64;
MNHENDAEDE EQGLSENATR LVLEENEDDM EDELNLFDIE KMCEIHYLLP NEEIISLIES
YVLEFLFKLI ENDEKNGQDL ILNYSFGTRD SNQSNGERLH QIIKSKSGTF EKKSLKNNHL
KKNHLVWLLM KDVHLLLNCR KKITQRELFY MNVTTFRDQI QCNRCLSTVG DVLKVDRSLL
NIICMSKGFI YSNDGRGNSL LSLNGNKQAS VESIPGDFPS IDYFGNVDTV LIIEKDAIFR
RLVEDKIFKL VRNCLLITGC GYPSIVTRYV VKHVSTRFPN ARLYALCDFN IFGYQIMSTY
KYGSVEMSRH KVQQESALKD RLQWLGMNYE DVKDIPHYYN QPISQREINL IDLKGLNFLS
TYLAKKISKF NIVK
//
