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 28-FEB-2018, entry version 68.
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 then rotates around the
CC intact phosphodiester bond on the opposing strand, thus removing
CC DNA supercoils. Finally, in the religation step, the DNA 5'-OH
CC attacks the covalent intermediate to expel the active-site
CC tyrosine and restore the DNA phosphodiester backbone (By
CC 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}.
DR EMBL; EF421830; ABP57788.1; -; mRNA.
DR RefSeq; NP_001106268.1; NM_001112797.1.
DR UniGene; Ptr.6282; -.
DR ProteinModelPortal; 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 eggNOG; COG3569; LUCA.
DR HOGENOM; HOG000105469; -.
DR InParanoid; A9Q1D5; -.
DR KO; K03163; -.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003917; F:DNA topoisomerase type I 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; -; 2.
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 PANTHER; PTHR10290; PTHR10290; 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; 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
//
