ID A0A151R1S1_CAJCA Unreviewed; 418 AA.
AC A0A151R1S1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=DNA topoisomerase 6 subunit A {ECO:0000256|HAMAP-Rule:MF_03164};
DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_03164};
GN Name=TOP6A {ECO:0000256|HAMAP-Rule:MF_03164};
GN ORFNames=KK1_042415 {ECO:0000313|EMBL:KYP36459.1};
OS Cajanus cajan (Pigeon pea) (Cajanus indicus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Cajanus.
OX NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP36459.1, ECO:0000313|Proteomes:UP000075243};
RN [1] {ECO:0000313|EMBL:KYP36459.1, ECO:0000313|Proteomes:UP000075243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX PubMed=22057054; DOI=10.1038/nbt.2022;
RA Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., Schlueter J.A.,
RA Donoghue M.T., Azam S., Fan G., Whaley A.M., Farmer A.D., Sheridan J.,
RA Iwata A., Tuteja R., Penmetsa R.V., Wu W., Upadhyaya H.D., Yang S.P.,
RA Shah T., Saxena K.B., Michael T., McCombie W.R., Yang B., Zhang G.,
RA Yang H., Wang J., Spillane C., Cook D.R., May G.D., Xu X., Jackson S.A.;
RT "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop
RT of resource-poor farmers.";
RL Nat. Biotechnol. 30:83-89(2012).
CC -!- FUNCTION: Component of the DNA topoisomerase VI involved in chromatin
CC organization and progression of endoreduplication cycles. Relaxes both
CC positive and negative superturns and exhibits a strong decatenase
CC activity. {ECO:0000256|HAMAP-Rule:MF_03164}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03164};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_03164};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two TOP6A and two TOP6B subunits.
CC {ECO:0000256|HAMAP-Rule:MF_03164}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03164}.
CC -!- SIMILARITY: Belongs to the TOP6A family.
CC {ECO:0000256|ARBA:ARBA00006559, ECO:0000256|HAMAP-Rule:MF_03164}.
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DR EMBL; KQ484212; KYP36459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151R1S1; -.
DR STRING; 3821.A0A151R1S1; -.
DR Proteomes; UP000075243; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00132; Top6A; 1.
DR InterPro; IPR002815; Spo11/TopoVI_A.
DR InterPro; IPR013049; Spo11/TopoVI_A_N.
DR InterPro; IPR036078; Spo11/TopoVI_A_sf.
DR InterPro; IPR004085; TopoVI_A.
DR InterPro; IPR034136; TOPRIM_Topo6A/Spo11.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10848:SF4; DNA TOPOISOMERASE 6 SUBUNIT A; 1.
DR PANTHER; PTHR10848; MEIOTIC RECOMBINATION PROTEIN SPO11; 1.
DR Pfam; PF21180; TOP6A-Spo11_Toprim; 1.
DR Pfam; PF04406; TP6A_N; 1.
DR PRINTS; PR01550; TOP6AFAMILY.
DR PRINTS; PR01552; TPISMRASE6A.
DR SUPFAM; SSF56726; DNA topoisomerase IV, alpha subunit; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_03164};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_03164};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03164};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03164}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03164};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03164};
KW Reference proteome {ECO:0000313|Proteomes:UP000075243};
KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_03164}.
FT DOMAIN 132..193
FT /note="Spo11/DNA topoisomerase VI subunit A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04406"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03164"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03164"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03164"
SQ SEQUENCE 418 AA; 46788 MW; C68049FAC53A4E38 CRC64;
MADNKKRRRK EPTGDELPFK NSLKSDSDIL KTLKDFSTAS ASSSSAAQTL TLQDLPLPFR
CREVADLSLS SVQSNIESLI LRIAHSILSG HGFSFDVPSR SAANQLYVPE LDRIVLKDKS
SLRPFANIST VRKSAITSRI LQLIHQLCIK GIHVTKRDLF YTDVKLFQDQ IQSDAVLDDV
SCMLGCTRSS LNVVAAEKGV VVGRLIFSDN GDMIDCTKMG MGGKAIPPNI DRVGDMQSDA
LFILLVEKDA AYMRLAEDRF YNRFPCIIVT AKGQPDVSTR LFLRKMKTEL KLPVLALVDS
DPYGLKILSV YGCGSKNMSY DSANLTTPDI KWLGVRPSDL DKYKIPEQCR LPMTEQDIKT
GKDLLEEDFV KKNPGWVEEL SLMVKTKQKA EIQALSTFGF QYLSEVYLPL KLQQKDWL
//