ID G8NQK2_GRAMM Unreviewed; 364 AA.
AC G8NQK2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
GN OrderedLocusNames=AciX8_2925 {ECO:0000313|EMBL:AEU37228.1};
OS Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU37228.1, ECO:0000313|Proteomes:UP000007113};
RN [1] {ECO:0000313|EMBL:AEU37228.1, ECO:0000313|Proteomes:UP000007113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8
RC {ECO:0000313|Proteomes:UP000007113};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M.,
RA Haggblom M., Woyke T.;
RT "Complete sequence of Granulicella mallensis MP5ACTX8.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000213};
CC -!- SIMILARITY: Belongs to the type IB topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00006645}.
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DR EMBL; CP003130; AEU37228.1; -; Genomic_DNA.
DR AlphaFoldDB; G8NQK2; -.
DR STRING; 682795.AciX8_2925; -.
DR KEGG; gma:AciX8_2925; -.
DR eggNOG; COG3569; Bacteria.
DR HOGENOM; CLU_046978_1_1_0; -.
DR Proteomes; UP000007113; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:InterPro.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR Gene3D; 1.10.132.120; -; 1.
DR Gene3D; 3.30.66.10; DNA topoisomerase I domain; 1.
DR InterPro; IPR011010; DNA_brk_join_enz.
DR InterPro; IPR035447; DNA_topo_I_N_sf.
DR InterPro; IPR049331; Top1B_N_bact.
DR InterPro; IPR001631; TopoI.
DR InterPro; IPR014711; TopoI_cat_a-hlx-sub_euk.
DR InterPro; IPR013500; TopoI_cat_euk.
DR Pfam; PF21338; Top1B_N_bact; 1.
DR Pfam; PF01028; Topoisom_I; 1.
DR PRINTS; PR00416; EUTPISMRASEI.
DR SUPFAM; SSF56349; DNA breaking-rejoining enzymes; 1.
DR SUPFAM; SSF55869; DNA topoisomerase I domain; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AEU37228.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007113};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 44..92
FT /note="DNA topoisomerase IB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21338"
FT DOMAIN 105..318
FT /note="DNA topoisomerase I catalytic core eukaryotic-type"
FT /evidence="ECO:0000259|Pfam:PF01028"
SQ SEQUENCE 364 AA; 41326 MW; 28F2F487A75078FE CRC64;
MEPLPAKKQK PEVLADPVES ARAAGLRYVS DARPGLQRKQ WHHGFRYIDI NGSVIHDAET
LARIKSLVIP PAWSEVWICP HAKGHLQATG RDARGRKQSL YHPHWREVRD ETKYERMLLF
GATLPTIRKQ VEQDLALPGL PRRKVLATLV RLMETTLIRV GNSEYARQNK SYGLTTLREK
HVRVDGSTIT FNFQGKSGIH HTVDIHDRRL AKIVQRCQDI PGYELFQYFD HEGMHHTVDS
ADVNAYLQEI TDQPFTAKDF RTWAGTVLSC SLLCGCEVFE SETQAKRDVV QAIKAVAAQL
GNTPSICRKC YVHPAVLDCY MAGALMEATK RPMKKKLATQ YRGLKREEVA LVNLLQRQLP
RSTA
//
