ID TOP1M_PANTR Reviewed; 601 AA. AC A9Q1D5; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 24-JAN-2024, entry version 87. DE RecName: Full=DNA topoisomerase I, mitochondrial; DE Short=TOP1mt; DE EC=5.6.2.1 {ECO:0000255|PROSITE-ProRule:PRU10130}; DE Flags: Precursor; GN Name=TOP1MT; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Zhang H., Pommier Y.; RT "Chimpanzee mitochondrial topoisomerase I."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. 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; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10130}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EF421830; ABP57788.1; -; mRNA. DR RefSeq; NP_001106268.1; NM_001112797.1. DR AlphaFoldDB; A9Q1D5; -. DR SMR; A9Q1D5; -. DR STRING; 9598.ENSPTRP00000058183; -. DR PaxDb; 9598-ENSPTRP00000058183; -. DR GeneID; 472883; -. DR KEGG; ptr:472883; -. DR CTD; 116447; -. DR eggNOG; KOG0981; Eukaryota. DR InParanoid; A9Q1D5; -. DR OrthoDB; 10940at2759; -. DR Proteomes; UP000002277; Unplaced. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0042645; C:mitochondrial nucleoid; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IEA:UniProt. 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 CDD; cd03488; Topoisomer_IB_N_htopoI_like; 1. DR Gene3D; 1.10.132.10; -; 1. DR Gene3D; 2.170.11.10; DNA Topoisomerase I, domain 2; 1. DR Gene3D; 1.10.10.41; Yeast DNA topoisomerase - domain 1; 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; IPR018521; TopoI_AS. 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 InterPro; IPR048045; Topoisomer_I_DNA-bd. DR PANTHER; PTHR10290; DNA TOPOISOMERASE I; 1. DR PANTHER; PTHR10290:SF1; DNA TOPOISOMERASE I, MITOCHONDRIAL; 1. 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; DNA breaking-rejoining enzymes; 1. DR SUPFAM; SSF46596; Eukaryotic DNA topoisomerase I, dispensable insert domain; 1. DR SUPFAM; SSF56741; Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment; 1. DR PROSITE; PS00176; TOPO_IB_1; 1. DR PROSITE; PS52038; TOPO_IB_2; 1. PE 2: Evidence at transcript level; KW DNA-binding; Isomerase; Mitochondrion; Reference proteome; Topoisomerase; KW Transit peptide. FT TRANSIT 1..50 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 51..601 FT /note="DNA topoisomerase I, mitochondrial" FT /id="PRO_0000384394" FT DOMAIN 268..601 FT /note="Topo IB-type catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01382" FT REGION 22..48 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 261..262 FT /note="Interaction with DNA" FT /evidence="ECO:0000250" FT REGION 324..329 FT /note="Interaction with DNA" FT /evidence="ECO:0000250" FT REGION 421..423 FT /note="Interaction with DNA" FT /evidence="ECO:0000250" FT ACT_SITE 559 FT /note="O-(3'-phospho-DNA)-tyrosine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01382, FT ECO:0000255|PROSITE-ProRule:PRU10130" FT SITE 152 FT /note="Interaction with DNA" FT /evidence="ECO:0000250" FT SITE 200 FT /note="Interaction with DNA" FT /evidence="ECO:0000250" FT SITE 248 FT /note="Interaction with DNA" FT /evidence="ECO:0000250" FT SITE 279 FT /note="Interaction with DNA" FT /evidence="ECO:0000250" FT SITE 337 FT /note="Interaction with DNA" FT /evidence="ECO:0000250" FT SITE 368 FT /note="Interaction with DNA" FT /evidence="ECO:0000250" FT SITE 410 FT /note="Interaction with DNA" FT /evidence="ECO:0000250" FT SITE 468 FT /note="Interaction with DNA" FT /evidence="ECO:0000250" FT SITE 486 FT /note="Interaction with DNA" FT /evidence="ECO:0000250" SQ SEQUENCE 601 AA; 69758 MW; F8064FE822DB84F3 CRC64; MRVVRLLRLR AALTLLGEVP RRPASRGVPG SRRTQKGSGA RWEKEKHEDG VKWRQLEHKG PYFAPPYEPL PDGVRFFYEG KPVRLSVAAE EVATFYGRML GHEYTTKEVF RKNFFNDWRK EMAVEEREVI KSLDKCDFTE IHRYFVDKAA ARKVLSREEK QKLKEEAEKL QREFGYCILD GHQEKIGNFK IEPPGLFRGR GDHPKMGMLK RRIMPEDVVI NCSRDSKIPE PPAGHQWKEV RSDNTVTWLA AWTESVQNSI KYIMLNPCSK LKGETAWQKF ETARRLRGFV DEIRSQYRAD WKSREMKTRQ RAVALYFIDK LALRAGNEKE DGEAADTVGC CSLRVEHVQL HPEADGCQHV VEFDFLGKDC IRYYNRVPVE KPVYKNLQLF MESKGPRDNL FDRLTTTSLN KHLQELMDGL TAKVFRTYNA SITLQEQLRA LTRAEDSIAA KILSYNRANR VVAILCNHQR ATPSTFEKSM QNLQTKIQAK KEQVAEARAE LRRARAEHKA QGDGKSRSVL EKKRRLLEKL QEQLAQLSVQ ATDKEENKQV ALGTSKLNYL DPRISIAWCK RFRVPVEKIY SKTQRERFAW ALAMAGEDFE F //