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Database: UniProt
Entry: TOP1M_PANTR
LinkDB: TOP1M_PANTR
Original site: 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   26-NOV-2014, entry version 48.
DE   RecName: Full=DNA topoisomerase I, mitochondrial;
DE            Short=TOP1mt;
DE            EC=5.99.1.2;
DE   Flags: Precursor;
GN   Name=TOP1MT;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
CC       duplex DNA. The scissile phosphodiester is attacked by the
CC       catalytic tyrosine of the enzyme, resulting in the formation of a
CC       DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a
CC       5'-OH DNA strand. The free DNA strand than undergoes passage
CC       around the unbroken strand thus removing DNA supercoils. Finally,
CC       in the religation step, the DNA 5'-OH attacks the covalent
CC       intermediate to expel the active-site tyrosine and restore the DNA
CC       phosphodiester backbone (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded
CC       DNA, followed by passage and rejoining. {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.
CC       {ECO:0000305}.
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DR   EMBL; EF421830; ABP57788.1; -; mRNA.
DR   RefSeq; NP_001106268.1; NM_001112797.1.
DR   UniGene; Ptr.6282; -.
DR   ProteinModelPortal; A9Q1D5; -.
DR   SMR; A9Q1D5; 42-601.
DR   STRING; 9598.ENSPTRP00000035312; -.
DR   GeneID; 472883; -.
DR   KEGG; ptr:472883; -.
DR   CTD; 116447; -.
DR   eggNOG; COG3569; -.
DR   HOGENOM; HOG000105469; -.
DR   InParanoid; A9Q1D5; -.
DR   KO; K03163; -.
DR   NextBio; 20849513; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IBA:RefGenome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003917; F:DNA topoisomerase type I activity; IBA:RefGenome.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IBA:RefGenome.
DR   GO; GO:0006265; P:DNA topological change; IBA:RefGenome.
DR   Gene3D; 1.10.10.41; -; 1.
DR   Gene3D; 1.10.132.10; -; 1.
DR   Gene3D; 2.170.11.10; -; 2.
DR   Gene3D; 3.90.15.10; -; 1.
DR   InterPro; IPR011010; DNA_brk_join_enz.
DR   InterPro; IPR013034; DNA_topo_domain1.
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; IPR013030; TopoI_DNA-bd_mixed-a/b_euk.
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; 2.
DR   SUPFAM; SSF56741; SSF56741; 1.
DR   PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; DNA-binding; Isomerase; Mitochondrion;
KW   Reference proteome; Topoisomerase; Transit peptide.
FT   TRANSIT       1     50       Mitochondrion. {ECO:0000250}.
FT   CHAIN        51    601       DNA topoisomerase I, mitochondrial.
FT                                /FTId=PRO_0000384394.
FT   REGION      261    262       Interaction with DNA. {ECO:0000250}.
FT   REGION      324    329       Interaction with DNA. {ECO:0000250}.
FT   REGION      421    423       Interaction with DNA. {ECO:0000250}.
FT   ACT_SITE    559    559       O-(3'-phospho-DNA)-tyrosine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10130}.
FT   SITE        152    152       Interaction with DNA. {ECO:0000250}.
FT   SITE        200    200       Interaction with DNA. {ECO:0000250}.
FT   SITE        248    248       Interaction with DNA. {ECO:0000250}.
FT   SITE        279    279       Interaction with DNA. {ECO:0000250}.
FT   SITE        337    337       Interaction with DNA. {ECO:0000250}.
FT   SITE        368    368       Interaction with DNA. {ECO:0000250}.
FT   SITE        410    410       Interaction with DNA. {ECO:0000250}.
FT   SITE        468    468       Interaction with DNA. {ECO:0000250}.
FT   SITE        486    486       Interaction with DNA. {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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