ID T1C5S1_9ZZZZ Unreviewed; 366 AA.
AC T1C5S1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=B2A_03593 {ECO:0000313|EMBL:EQD60609.1};
OS mine drainage metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=410659 {ECO:0000313|EMBL:EQD60609.1};
RN [1] {ECO:0000313|EMBL:EQD60609.1}
RP NUCLEOTIDE SEQUENCE.
RA Mendez C., Richter M., Ferrer M., Sanchez J.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EQD60609.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24430486; DOI=10.1038/ismej.2013.242;
RA Mendez-Garcia C., Mesa V., Sprenger R.R., Richter M., Diez M.S., Solano J.,
RA Bargiela R., Golyshina O.V., Manteca A., Ramos J.L., Gallego J.R.,
RA Llorente I., Martins Dos Santos V.A., Jensen O.N., Pelaez A.I., Sanchez J.,
RA Ferrer M.;
RT "Microbial stratification in low pH oxic and suboxic macroscopic growths
RT along an acid mine drainage.";
RL ISME J. 8:1259-1274(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQD60609.1}.
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DR EMBL; AUZZ01002405; EQD60609.1; -; Genomic_DNA.
DR AlphaFoldDB; T1C5S1; -.
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-KW.
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:0006265; P:DNA topological change; IEA:InterPro.
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; IPR049333; Topo_VI_alpha.
DR InterPro; IPR004085; TopoVI_A.
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; PF20768; Topo_VI_alpha; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:EQD60609.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 67..137
FT /note="Spo11/DNA topoisomerase VI subunit A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04406"
FT DOMAIN 145..186
FT /note="Type II DNA topoisomerase VI subunit A all-beta"
FT /evidence="ECO:0000259|Pfam:PF20768"
FT DOMAIN 191..359
FT /note="Topoisomerase 6 subunit A/Spo11 TOPRIM"
FT /evidence="ECO:0000259|Pfam:PF21180"
SQ SEQUENCE 366 AA; 41982 MW; 822A4C4986160182 CRC64;
MRRGTIVEEK LRDFGKSIVN EIYRGENPKF VTSVRSRSNV IYDDKGGYLH LGPSQEERNF
INISQSRKFM QTVAIASKCN SFVKENLHTS IRGLFYQLKY SLGEDVDENI FSEQSESNPL
IEDLESSLGV RREDLNLSAD RKGFLAGNMR IIDKFGGDRL EIDASKQGRS GFPIPSDVDN
GIELVDVKAK YVLVVEKDAV WQRLNEDGFW KKEDAILITP KGQASRGTRR MIKKLSELGL
PVYVFNDCDA WGWYIYWTIK TGSMNLAYLG KDMATPNARF LGVTMSDIEH YDFLGKLTMK
ASEVDLKRAQ EMLSYPWINK HKEWVDELKK VLKTKTKLEQ DTLQGPKLTF LGEYVREKIK
GKEFLP
//
