ID A0A0Q5YQK4_9BURK Unreviewed; 395 AA.
AC A0A0Q5YQK4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
GN ORFNames=ASG30_16750 {ECO:0000313|EMBL:KQT08076.1};
OS Ramlibacter sp. Leaf400.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT08076.1, ECO:0000313|Proteomes:UP000051173};
RN [1] {ECO:0000313|EMBL:KQT08076.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT08076.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT08076.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT08076.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KQT08076.1}.
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DR EMBL; LMQL01000014; KQT08076.1; -; Genomic_DNA.
DR RefSeq; WP_055901555.1; NZ_LMQL01000014.1.
DR AlphaFoldDB; A0A0Q5YQK4; -.
DR STRING; 1736365.ASG30_16750; -.
DR OrthoDB; 9778962at2; -.
DR Proteomes; UP000051173; Unassembled WGS sequence.
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: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:KQT08076.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051173};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 42..90
FT /note="DNA topoisomerase IB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21338"
FT DOMAIN 102..308
FT /note="DNA topoisomerase I catalytic core eukaryotic-type"
FT /evidence="ECO:0000259|Pfam:PF01028"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 44633 MW; 70F7FE576C89E68B CRC64;
MKEERTDEPA TADDPVEAAR SAGLKYVTDE DPGLRREPDG EGFRYLRTNG LPVRDDNEVQ
RIRKLAIPPA WTDVWICPSA DGHLQATGRD ARGRKQYRYH PRFREVREET KYGHMLEFAR
ALPGLRARVA EHMALRGLPR EKVLATVVHL LETTLIRVGN DDYARDNRSY GLTTLRNRHV
AIDGSQLRFE FKGKSGKTWR LQVQNRRVAR VVRACQELPG QRLFQYRDED GELREVTSSD
VNDYLREIGG RDITAKDFRT WAGTVMAALA LQEVERVDTQ AAMKKNVRAA VERVAARLGN
TPAICRKCYV HPEIFAAHAE GELLLEVGRE AERELRGPAA LNPEESAVLS LLQGRLERTL
EGQLGKSLVA LQERKKPARS AARRGRRKAT AESTG
//