ID Q5REX2_PONAB Unreviewed; 1620 AA.
AC Q5REX2;
DT 21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN Name=DKFZp469C0215 {ECO:0000313|EMBL:CAH89685.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|EMBL:CAH89685.1};
RN [1] {ECO:0000313|EMBL:CAH89685.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Kidney {ECO:0000313|EMBL:CAH89685.1};
RG The German cDNA Consortium;
RA Koehrer K., Beyer A., Mewes H.W., Weil B., Amid C., Osanger A., Fobo G.,
RA Han M., Wiemann S.;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Key decatenating enzyme that alters DNA topology by binding
CC to two double-stranded DNA molecules, generating a double-stranded
CC break in one of the strands, passing the intact strand through the
CC broken strand, and religating the broken strand.
CC {ECO:0000256|RuleBase:RU362094}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185,
CC ECO:0000256|RuleBase:RU362094};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|RuleBase:RU362094};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU362094};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU362094};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362094}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}. Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00011080, ECO:0000256|RuleBase:RU362094}.
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DR EMBL; CR857392; CAH89685.1; -; mRNA.
DR RefSeq; NP_001127186.1; NM_001133714.1.
DR GeneID; 100439073; -.
DR KEGG; pon:100439073; -.
DR CTD; 7155; -.
DR OrthoDB; 1944951at2759; -.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd16930; HATPase_TopII-like; 1.
DR CDD; cd00187; TOP4c; 1.
DR CDD; cd03481; TopoIIA_Trans_ScTopoIIA; 1.
DR CDD; cd03365; TOPRIM_TopoIIA; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.1490.30; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR InterPro; IPR012542; DTHCT.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_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; IPR001154; TopoII_euk.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR031660; TOPRIM_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034157; TOPRIM_TopoII.
DR PANTHER; PTHR10169:SF36; DNA TOPOISOMERASE 2-BETA; 1.
DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR Pfam; PF08070; DTHCT; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF16898; TOPRIM_C; 1.
DR PRINTS; PR01158; TOPISMRASEII.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362094};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362094};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362094};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362094}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 471..588
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1104..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1369..1385
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1620 AA; 182540 MW; 83ACBCE8DCC5DA6C CRC64;
MAKSGGCGAG AGVGGGNGAL TWVNNAAKKE ESETANKNDS SKKLSVERVY QKKTQLEHIL
LRPDTYIGSV EPLTQFMWVY DEDVGMNCRE VTFVPGLYKI FDEILVNAAD NKQRDKNMTC
IKVSIDPESN IISIWNNGKG IPVVEHKVEK VYVPALIFGQ LLTSSNYDDD EKKVTGGRNG
YGAKLCNIFS TKFTVETACK EYKHSFKQTW MNNMMKTSEA KIKHFDGEDY TCITFQPDLS
KFKMEKLDKD IVALMTRRAY DLAGSCRGVK VMFNGKKLPV NGFRSYVDLY VKDKLDETGV
ALKVIHELAN ERWDVCLTLS EKGFQQISFV NSIATTKGGR HVDYVVDQVV GKLIEVVKKK
NKAGVSVKPF QVKNHIWVFI NCLIENPTFD SQTKENMTLQ PKSFGSKCQL SEKFFKAASN
CGIVESILNW VKFKAQTQLN KKCSSVKYSK IKGIPKLDDA NDAGGKHSLE CTLILTEGDS
AKSLAVSGLG VIGRDRYGVF PLRGKILNVR EASHKQIMEN AEINNIIKIV GQQYKKSYDD
AESLKTLRYG KIMIMTDQDQ DGSHIKGLLI NFIHHNWPSL LKHGFLEEFI TPIVKASKNK
QELSFYSIPE FDEWKKHIEN QKAWKIKYYK GLGTSTAKEA KEYFADMERH RILFRYAGPE
DDAAITLAFS KKKIDDRKEW LTNFMEDRRQ RRLHGLPEQF LYGTATKHLT YNDFINKELI
LFSNSDNERS IPSLVDGFKP GQRKVLFTCF KRNDKREVKV AQLAGSVAEM SAYHHGEQAL
MMTIVNLAQN FVGSNNINLL QPIGQFGTRL HGGKDAASPR YIFTMLSSLA RLFPAVDDNL
LKFLYDDNQR VEPEWYIPII PMVLINGAEG IGTGWACKLP NYDAREIVNN VRRMLDGLDP
HPMLPNYKNF KGTIQELGQN QYAVSGEIFV VDRNTVEITE LPVRTWTQVY KEQVLEPMLN
GTDKTPALIS DYKEYHTDTT VKFVVKMTEE KLAQAEAAGL HKVFKLQTTL TCNSMVLFDH
MGCLKKYETV QDILKEFFDL RLSYYGLRKE WLVGMLGAES TKLNNQARFI LEKIQGKITI
ENRSKKDLIQ MLVQRGYESD PVKAWKEAQE KAAEEDETQN QHDDSSSDSG TPSGPDFNYI
LNMSLWSLTK EKVEELIKQR DAKGRDVNDL KRKSPSDLWK EDLAAFVEEL DKVESQERED
ILAGMSGKAI KGKVGKPKVK KLQLEETMPS PYGRRIIPEI TAMKADASKK LLKKKKGDLD
TAAVKVEFDE EFSGAPVEGA GEEALTPSAP MNKGPKPKRE KKEPGTRVRK TPTSSGKPSA
KKVKKRNPWS DDESKSESDL EETEPVVIPR DSLLRRAAAE RPKYTFDFSE EEDDDADDDD
DDNNDLEELK VKASPITNDG EDEFVPSDGL DKDEYTFSPG KSKATPEKSL HDKKSQDFGN
LFSFPSYSQK SEDDSAKFDS NEEDSASVFS PSFGLKQTDK VPSKTVAAKK GKPSSDTAPK
PKRAPKQKKV VEAVNSDSDS EFGIPKKTTT PKGKGRGAKK RKASGSENEG DYNPGRKTSK
TTSKKPKKTS FDQDSDVDIF PSEFPTEPPS LPRTGRARKE VKYFAESDEE EEDVDFAMFN
//
