TOP2M_CAEEL
ID TOP2M_CAEEL Reviewed; 1170 AA.
AC P34534; Q8MQ00;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 5.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Putative DNA topoisomerase 2, mitochondrial;
DE Short=DNA topoisomerase II;
DE EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995};
DE Flags: Precursor;
GN ORFNames=R05D3.12;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Control of topological states of DNA by transient breakage
CC and subsequent rejoining of DNA strands. Topoisomerase II makes double-
CC strand breaks (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00995};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges
CC with both the protein and the DNA. Can also accept other divalent metal
CC cations, such as Mn(2+) or Ca(2+). {ECO:0000255|PROSITE-
CC ProRule:PRU00995};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a;
CC IsoId=P34534-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P34534-2; Sequence=VSP_042233;
CC Name=c;
CC IsoId=P34534-3; Sequence=VSP_042232;
CC -!- SIMILARITY: Belongs to the type II topoisomerase family. {ECO:0000305}.
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DR EMBL; FO081667; CCD73199.1; -; Genomic_DNA.
DR EMBL; FO081667; CCD73187.1; -; Genomic_DNA.
DR EMBL; FO081667; CCD73195.1; -; Genomic_DNA.
DR RefSeq; NP_001129839.2; NM_001136367.2.
DR RefSeq; NP_001254958.1; NM_001268029.1. [P34534-3]
DR RefSeq; NP_741252.2; NM_171214.4. [P34534-1]
DR AlphaFoldDB; P34534; -.
DR SMR; P34534; -.
DR STRING; 6239.R05D3.12a; -.
DR EPD; P34534; -.
DR PaxDb; P34534; -.
DR PeptideAtlas; P34534; -.
DR EnsemblMetazoa; R05D3.12a.1; R05D3.12a.1; WBGene00019884. [P34534-1]
DR EnsemblMetazoa; R05D3.12b.1; R05D3.12b.1; WBGene00019884.
DR EnsemblMetazoa; R05D3.12c.1; R05D3.12c.1; WBGene00019884. [P34534-3]
DR GeneID; 259522; -.
DR KEGG; cel:CELE_R05D3.12; -.
DR UCSC; R05D3.1; c. elegans. [P34534-1]
DR UCSC; R05D3.12; c. elegans.
DR CTD; 259522; -.
DR WormBase; R05D3.12a; CE45903; WBGene00019884; -. [P34534-1]
DR WormBase; R05D3.12b; CE31048; WBGene00019884; -.
DR WormBase; R05D3.12c; CE42620; WBGene00019884; -. [P34534-3]
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_1_0_1; -.
DR InParanoid; P34534; -.
DR OMA; AFESLWP; -.
DR OrthoDB; 117851at2759; -.
DR PhylomeDB; P34534; -.
DR Reactome; R-CEL-4615885; SUMOylation of DNA replication proteins.
DR PRO; PR:P34534; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00019884; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; P34534; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0000819; P:sister chromatid segregation; IBA:GO_Central.
DR CDD; cd00187; TOP4c; 1.
DR CDD; cd03365; TOPRIM_TopoIIA; 1.
DR Gene3D; 1.10.268.10; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.90.199.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR031660; TOPRIM_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034157; TOPRIM_TopoII.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF16898; TOPRIM_C; 1.
DR SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW Alternative splicing; ATP-binding; DNA-binding; Isomerase; Magnesium;
KW Metal-binding; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Topoisomerase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..1170
FT /note="Putative DNA topoisomerase 2, mitochondrial"
FT /id="PRO_0000034819"
FT DOMAIN 475..590
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT ACT_SITE 813
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 163..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 176..183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 396..398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 559
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 559
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 561
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 509
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 512
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 679
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 680
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 730
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 765
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 771
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 812
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 864
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250"
FT VAR_SEQ 127..1170
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_042232"
FT VAR_SEQ 145..1170
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_042233"
SQ SEQUENCE 1170 AA; 133720 MW; E4A72D635186E61E CRC64;
MHRLRVLRHL KFCISTSHRT TVVLKNTRSF CNNIPSTSFA SEAAAKYEKK SPTEHVLLRP
DTYIGGVAMR EDQIIWLRDS ENRKMIAKEV TYPPGLLKIF DEILVNAADN KARDSSMNRL
EVWLDRETAR ISVWNNGSGL PVEIHPTEGI YVPTLVFGNL FTSSNYDDSE IKTVGGRNGY
GAKLCNIFSK EFIVETVDTR IKRRFRQKWY DNMKKCNEAE VVEILDETVK DYTKVEFVPD
LERFQIDKLS DDVIDLIGRR VFEVAATLPR DVDVYLNGQK CDVDGFEDYV KMFNDSSSLL
FLHPTPRWHV GVAKRNNFFG ESHVVLPKIV SFVNNINTEK GGSHVDYVMD KIVNIIKPIV
DSKLGDPTKS VKPAVIKNNL SIFINCLIEN PSFESQTKET LTTKAKNFGS IFECDAKKTA
EWAEQSGLIE DIVEEVLNMK KKKLPGKRVS VSSVRDIVKL EDAEWAGITG TAEKCTLILT
EGDSAKALAL AGLEVLGRET YGVFPLKGKL LNVSNLDDAR ASKNEEISNL LRILGLKFED
SNSITRESLR YGRLLILADQ DEDGSHIKGL IVNFIHKFWP SLVHTDGFIQ SFRTPLLKAK
KGDKVRSFFS MNEYRKWADV EEGGKWKIKY YKGLGTSTSN EAREYFSDLD HHTVNFKYTG
TTDDDAIRMA FDRDKSDERK EWIRRSENEI TNEDDGKTEI SYQEFVDGQL MQFGMVDLKR
SIPSLIDGLK PSQRKILWTL LNNMDESTEI KVSQLAGAVA HRQSYHHGEE SLVRTIIRMG
QTFCGSSNLP LLQPIGQFGT RHEGGNDAAS ARYIFTALAP TTRLLFPQAD DDLLQKNVEE
GMVVEPTWLC PIVPLILING TEGIGTGWST KIANRNPIDI IDMIRRKIDS ISTEYEIPPF
YEEFRGKLEV VTPTKFISSG KIQLIRPERK NASTFSIEIV ELPIGIWTSK YKEKLSKIVE
TLPVLEFSER HTEKRVHFRI TLDRKKSSRF LQKSNSDLLN YFKLRTSLTE NRVLFDRNGE
LKEFGNISEI AAEFFEVRRD LYEKRLKIQK EECEAKLIYV ENQLNFIEMV TNGTIEIRSM
GRNQLEEKLQ EMGFRVDPMA TIAKNSKKAN YGYLLEMPVS RLTSDEMKRL EERKSRRRTE
LEAAESADWK SVWRSELDKL AEAVGNNRKS
