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TOP1M_PANTR
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   03-AUG-2022, entry version 82.
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; A9Q1D5; -.
DR   PRIDE; A9Q1D5; -.
DR   GeneID; 472883; -.
DR   KEGG; ptr:472883; -.
DR   CTD; 116447; -.
DR   eggNOG; KOG0981; Eukaryota.
DR   InParanoid; A9Q1D5; -.
DR   OrthoDB; 303947at2759; -.
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   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; 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   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.
DR   PROSITE; PS00176; TOPOISOMERASE_I_EUK; 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   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: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
 
 
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