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}.
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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
//
