TOP6A_PYRFU
ID TOP6A_PYRFU Reviewed; 382 AA.
AC Q8U0K9;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Type 2 DNA topoisomerase 6 subunit A {ECO:0000255|HAMAP-Rule:MF_00132};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00132};
DE AltName: Full=Type II DNA topoisomerase VI subunit A {ECO:0000255|HAMAP-Rule:MF_00132};
GN Name=top6A {ECO:0000255|HAMAP-Rule:MF_00132}; OrderedLocusNames=PF1578;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
CC -!- FUNCTION: Relaxes both positive and negative superturns and exhibits a
CC strong decatenase activity. {ECO:0000255|HAMAP-Rule:MF_00132}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00132};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00132};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two Top6A and two Top6B chains.
CC {ECO:0000255|HAMAP-Rule:MF_00132}.
CC -!- SIMILARITY: Belongs to the TOP6A family. {ECO:0000255|HAMAP-
CC Rule:MF_00132}.
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DR EMBL; AE009950; AAL81702.1; -; Genomic_DNA.
DR RefSeq; WP_011012724.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U0K9; -.
DR SMR; Q8U0K9; -.
DR IntAct; Q8U0K9; 1.
DR STRING; 186497.PF1578; -.
DR EnsemblBacteria; AAL81702; AAL81702; PF1578.
DR GeneID; 41713402; -.
DR KEGG; pfu:PF1578; -.
DR PATRIC; fig|186497.12.peg.1644; -.
DR eggNOG; arCOG04143; Archaea.
DR HOGENOM; CLU_037229_1_0_2; -.
DR OMA; NWGEARF; -.
DR OrthoDB; 22842at2157; -.
DR PhylomeDB; Q8U0K9; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd00223; TOPRIM_TopoIIB_SPO; 1.
DR Gene3D; 1.10.10.10; -; 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; PTHR10848; 1.
DR Pfam; PF04406; TP6A_N; 1.
DR PRINTS; PR01550; TOP6AFAMILY.
DR PRINTS; PR01552; TPISMRASE6A.
DR SUPFAM; SSF56726; SSF56726; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Topoisomerase.
FT CHAIN 1..382
FT /note="Type 2 DNA topoisomerase 6 subunit A"
FT /id="PRO_0000145453"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
SQ SEQUENCE 382 AA; 44073 MW; 4994F23656AC5F26 CRC64;
MKLKRGKPKE KFSYDPQKVL KKLEDLAYKI LEEVKAGKNP YFDVPTRGLS NVYFDEEARL
IKLGDKLSRR YFLNVAHARK FMQTLILMAY VKRLVSEGKH ASLREAYYAN KHTIPGTHEN
TFEDQSESDP IIEDLERMLG VLREEMHITA DRRGYVYGDI VIKDGEDEFN ASKLGMGGWA
VPGTVEHIQF PEINVDYVLV VETAAMADRL IEEKYPKRER ALIIATQGQA SRGVRRLIHR
LHYEEGLPII VFTDGDPYGW YIYSTIKQGS INLAYLSEKL ATPDAKFVGM TMDDIKEYGL
EHVTEKLKGI PPDKKGGPTG DYKRLIEELN YPWFQNKEWQ RQLKLALKWG VRIEQQALAN
KSLEFVAKEY LPEKIREGKL LP