TOP1M_RAT
ID TOP1M_RAT Reviewed; 593 AA.
AC Q6IM78;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=DNA topoisomerase I, mitochondrial;
DE Short=TOP1mt;
DE EC=5.6.2.1;
DE Flags: Precursor;
GN Name=Top1mt;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15096574; DOI=10.1093/nar/gkh525;
RA Zhang H., Meng L.-H., Zimonjic D.B., Popescu N.C., Pommier Y.;
RT "Thirteen-exon-motif signature for vertebrate nuclear and mitochondrial
RT type IB topoisomerases.";
RL Nucleic Acids Res. 32:2087-2092(2004).
CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA
CC introduced during duplication of mitochondrial DNA by transiently
CC cleaving and rejoining one strand of the DNA duplex. Introduces a
CC single-strand break via transesterification at a target site in duplex
CC DNA. The scissile phosphodiester is attacked by the catalytic tyrosine
CC of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-
CC enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free
CC DNA strand then rotates around the intact phosphodiester bond on the
CC opposing strand, thus removing DNA supercoils. Finally, in the
CC religation step, the DNA 5'-OH attacks the covalent intermediate to
CC expel the active-site tyrosine and restore the DNA phosphodiester
CC backbone (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Divalent metal ions (calcium or magnesium). {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type IB topoisomerase family. {ECO:0000305}.
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DR EMBL; BK001786; DAA02296.1; -; mRNA.
DR RefSeq; NP_001002798.1; NM_001002798.1.
DR AlphaFoldDB; Q6IM78; -.
DR SMR; Q6IM78; -.
DR STRING; 10116.ENSRNOP00000009965; -.
DR PaxDb; Q6IM78; -.
DR Ensembl; ENSRNOT00000009965; ENSRNOP00000009965; ENSRNOG00000007500.
DR GeneID; 300029; -.
DR KEGG; rno:300029; -.
DR UCSC; RGD:1303177; rat.
DR CTD; 116447; -.
DR RGD; 1303177; Top1mt.
DR eggNOG; KOG0981; Eukaryota.
DR GeneTree; ENSGT00940000162943; -.
DR InParanoid; Q6IM78; -.
DR OMA; RNYIDPR; -.
DR OrthoDB; 303947at2759; -.
DR PhylomeDB; Q6IM78; -.
DR TreeFam; TF105281; -.
DR PRO; PR:Q6IM78; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000007500; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q6IM78; baseline and differential.
DR Genevisible; Q6IM78; RN.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
DR CDD; cd00659; Topo_IB_C; 1.
DR Gene3D; 1.10.10.41; -; 1.
DR Gene3D; 1.10.132.10; -; 1.
DR Gene3D; 2.170.11.10; -; 1.
DR Gene3D; 3.90.15.10; -; 1.
DR InterPro; IPR011010; DNA_brk_join_enz.
DR InterPro; IPR013034; DNA_topo_DNA_db_N_dom1.
DR InterPro; IPR013030; DNA_topo_DNA_db_N_dom2.
DR InterPro; IPR001631; TopoI.
DR InterPro; IPR025834; TopoI_C_dom.
DR InterPro; IPR014711; TopoI_cat_a-hlx-sub_euk.
DR InterPro; IPR014727; TopoI_cat_a/b-sub_euk.
DR InterPro; IPR013500; TopoI_cat_euk.
DR InterPro; IPR008336; TopoI_DNA-bd_euk.
DR InterPro; IPR036202; TopoI_DNA-bd_euk_N_sf.
DR InterPro; IPR013499; TopoI_euk.
DR Pfam; PF14370; Topo_C_assoc; 1.
DR Pfam; PF01028; Topoisom_I; 1.
DR Pfam; PF02919; Topoisom_I_N; 1.
DR PRINTS; PR00416; EUTPISMRASEI.
DR SMART; SM00435; TOPEUc; 1.
DR SUPFAM; SSF56349; SSF56349; 1.
DR SUPFAM; SSF56741; SSF56741; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Isomerase; Mitochondrion; Reference proteome; Topoisomerase;
KW Transit peptide.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 44..593
FT /note="DNA topoisomerase I, mitochondrial"
FT /id="PRO_0000384395"
FT REGION 254..255
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 317..322
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 414..416
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT ACT_SITE 551
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
FT SITE 145
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 193
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 241
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 272
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 330
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 361
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 403
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 461
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 479
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 593 AA; 69011 MW; 6B691D668970BD9E CRC64;
MLLLWLRALC RRFQHVPRRV PSRQVSRGSK ASRAGWGETS KSSVKWKQLE HKGPCFAPAY
EPLPDGVRFF YDGKPVRLSL AAEEVATFYG KMLHLECTTK EVFRRNFFSD WQKEMTAEER
KLITHLDKCD FSEIHRHFME RAEARRTLPR EQKQKLKEEA EKLQQEFGYC ILDGHREKIG
NFKTEPPGLF RGRGDHPKMG MLKRRVMPED VVINCSRDSK IPEPPAGHQW KEVRSDNTVM
WLAAWVENIQ NSFKYIILNP SSKPKGEMDW QKYEVARRLK GVVDKIRAQY QADWKSPEMK
KRQLAVALYF IDKLALRTGN EKEEGETADT VGCCSLRVEH VRLHTPADGQ EHVVELDFLG
KDSIRYKNHV TVEKLVFQNL QHFMEDKDPR DDLFDALTTS SLNKHLQDLM EGLTAKVFRT
YNASITLQEQ LRVLTRAEDS LTCKVLAYNR ANRAVAVLCN HQRAIPKTFE ESMQTLQKKI
ETKKAQVAEA QVELQKAETD LRMRGDSKSK SFLQKQQRLL KLEEQLARLC TKATDKEENK
QVALGTAKLN YLDPRISIAW CKRFGVPVEK IYNKTQRERF AWAFNQAGED FEF
