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Database: UniProt
Entry: A1UCF0_MYCSK
LinkDB: A1UCF0_MYCSK
Original site: A1UCF0_MYCSK 
ID   A1UCF0_MYCSK            Unreviewed;       339 AA.
AC   A1UCF0;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE            EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
GN   OrderedLocusNames=Mkms_1296 {ECO:0000313|EMBL:ABL90508.1};
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL90508.1};
RN   [1] {ECO:0000313|EMBL:ABL90508.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:ABL90508.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) 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; CP000518; ABL90508.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1UCF0; -.
DR   STRING; 189918.Mkms_1296; -.
DR   KEGG; mkm:Mkms_1296; -.
DR   HOGENOM; CLU_046978_1_1_11; -.
DR   OrthoDB; 9778962at2; -.
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};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          21..69
FT                   /note="DNA topoisomerase IB N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21338"
FT   DOMAIN          80..298
FT                   /note="DNA topoisomerase I catalytic core eukaryotic-type"
FT                   /evidence="ECO:0000259|Pfam:PF01028"
SQ   SEQUENCE   339 AA;  38152 MW;  0642790EA4350797 CRC64;
     MRLRRSVVSG PGLTRVRRGK GFSYRDANGD AVTDKKTIDR INSLVIPPAW KKVWICPYPN
     GHIQAVGTDA AGRRQYLYHQ KWQEERNEEK FDRVLQMSSA LPEMRRQIAA DLGGRGWQRN
     RVLALALHLL DLGYFRAGGD QYAEENNSFG IATLLCEHVK LQRQAVEFDY PAKSGVQRSL
     VIDDPEVVKS VRALLRHPDR PDRLLACRNG DGWAEIRSDD LNTRFKELVG EDYSVKDLRT
     WHGTVLAAVA FVDADPPVNK TVIKRVESAV MKEVSGSLGN TPAVARTSYV DPRVVSAYES
     GATIAAAERR ALRAKRPDER QLIRERATAK LIRRAAKSR
//
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