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Database: UniProt
Entry: A0A1V1V333_9CAUL
LinkDB: A0A1V1V333_9CAUL
Original site: A0A1V1V333_9CAUL 
ID   A0A1V1V333_9CAUL        Unreviewed;       339 AA.
AC   A0A1V1V333;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE            EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
GN   ORFNames=SH203_02915 {ECO:0000313|EMBL:GAW42498.1};
OS   Brevundimonas sp. SH203.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=345167 {ECO:0000313|EMBL:GAW42498.1, ECO:0000313|Proteomes:UP000195546};
RN   [1] {ECO:0000313|EMBL:GAW42498.1, ECO:0000313|Proteomes:UP000195546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH203 {ECO:0000313|EMBL:GAW42498.1,
RC   ECO:0000313|Proteomes:UP000195546};
RA   Suzuki T., Kikuchi M., Habu N., Konno N.;
RT   "Draft Genome Sequence of Brevundimonas sp. SH203, producing Cellouronate
RT   (beta-1,4-linked polyglucuronate) lyase.";
RL   Submitted (MAR-2017) 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:GAW42498.1}.
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DR   EMBL; BDMM01000008; GAW42498.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V1V333; -.
DR   OrthoDB; 9778962at2; -.
DR   Proteomes; UP000195546; 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:GAW42498.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195546};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          36..84
FT                   /note="DNA topoisomerase IB N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21338"
FT   DOMAIN          100..308
FT                   /note="DNA topoisomerase I catalytic core eukaryotic-type"
FT                   /evidence="ECO:0000259|Pfam:PF01028"
SQ   SEQUENCE   339 AA;  37420 MW;  07BCF65D6C872C90 CRC64;
     MADGSHAFDI AAEVPKGLSY CSDEFAGLTR RRSGKGWSYK DARGQTVTDA KTLARIRALA
     IPPAWTDVWI CPKANGHIQA TGRDVKGRKQ YRYHNDWSAA RSENKFDKLP AFSRALPRLR
     DKVEHDLALR GVCRDKVLAT AVRLLEITLI RVGNSIYAKQ NRSYGLTTLH KRHLDVDGAA
     LTFEFRGKSG KDHSVSVKDR RLARVVRELE GLPGQQLFKY RSADGTLCPV DSDDVNAYIR
     DAMGDQFSAK DFRTWAGTVS AARALRDMEA ATSPTDARRK ITVCVKAVAG LLGNTPTVCR
     ASYVHPKVFA LFESGEIAKT LPGSETKGFE KALIKHLSA
//
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