ID A0A2K5YZ42_MANLE Unreviewed; 1616 AA.
AC A0A2K5YZ42;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN Name=TOP2B {ECO:0000313|Ensembl:ENSMLEP00000020815.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000020815.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000020815.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 STRING; 9568.ENSMLEP00000020815; -.
DR Ensembl; ENSMLET00000044314.1; ENSMLEP00000020815.1; ENSMLEG00000034275.1.
DR GeneTree; ENSGT00940000157921; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
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:0003682; F:chromatin binding; IEA:Ensembl.
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:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0045870; P:positive regulation of single stranded viral RNA replication via double stranded DNA intermediate; IEA:Ensembl.
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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 466..583
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1100..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1365..1381
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1616 AA; 182658 MW; 40BE23B9EDD50C90 CRC64;
KYFLCDGVGF GRVTLFDQNN AAKKEESETA NKNDSSKKLS VERVYQKKTQ LEHILLRPDT
YIGSVEPLTQ FMWVYDEDVG MNCREVTFVP GLYKIFDEIL VNAADNKQRD KNMTCIKVSI
DPESNIISIW NNGKGIPVVE HKVEKVYVPA LIFGQLLTSS NYDDDEKKVT GGRNGYGAKL
CNIFSTKFTV ETACKEYKHS FKQTWMNNMM KTSEAKIKHF DGEDYTCITF QPDLSKFKME
KLDKDIVALM TRRAYDLAGS CKGVKVMFNG KKLPVNGFRS YVDLYVKDKL DETGVALKVI
HELANERWDV CLTLSEKGFQ QISFVNSIAT TKGGRHVDYV VDQVVGKLIE VVKKKNKAGV
SVKPFQVKNH IWVFINCLIE NPTFDSQTKE NMTLQPKSFG SKCQLSEKFF KAASNCGIVE
SILNWVKFKA QTQLNKKCSS VKYSKIKGIP KLDDANDAGG KHSLECTLIL TEGDSAKSLA
VSGLGVIGRD RYGVFPLRGK ILNVREASHK QIMENAEINN IIKIVGLQYK KSYDDAESLK
TLRYGKIMIM TDQDQDGSHI KGLLINFIHH NWPSLLKHGF LEEFITPIVK ASKNKQELSF
YSIPEFDEWK KHIENQKAWK IKYYKGLGTS TAKEAKEYFA DMERHRILFR YAGPEDDAAI
TLAFSKKKID DRKEWLTNFM EDRRQRRLHG LPEQFLYGTA TKHLTYNDFI NKELILFSNS
DNERSIPSLV DGFKPGQRKV LFTCFKRNDK REVKVAQLAG SVAEMSAYHH GEQALMMTIV
NLAQNFVGSN NINLLQPIGQ FGTRLHGGKD AASPRYIFTM LSSLARLLFP AVDDNLLKFL
YDDNQRVEPE WYIPIIPMVL INGAEGIGTG WACKLPNYDA REIVNNVRRM LDGLDPHPML
PNYKNFKGTI QELGQNQYAV SGEIFVVDRN TVEITELPVR TWTQVYKEQV LEPMLNGTDK
TPALISDYKE YHTDTTVKFV VKMTEEKLAQ AEAAGLHKVF KLQTTLTCNS MVLFDHMGCL
KKYETVQDIL KEFFDLRLSY YGLRKEWLVG MLGAESTKLN NQARFILEKI QGKITIENRS
KKDLIQMLVQ RGYESDPVKA WKEAQEKAAE EDETQNQHDD SSSDSGTPSG PDFNYILNMS
LWSLTKEKVE ELIKQRDAKG REVNDLKRKS PSDLWKEDLA AFVEELDKVE AQEREDILAG
MSGKAIKGKV GKPKVKKLQL EETMPSPYGR RVIPEITAMK ADASKKLLKK KKGDLDTTAV
KVEFDEEFSG VPVEGAGEEA LIPSAPINKG PKPKREKKEP GTRVRKTPTS SGKPGAKKVK
KRNPWSDDES KSESDLEETE PVVIPRDSLL RRAAAERPKY TFDFSEEEDD DADDDDDDNN
DLEELKVKAS PITNDGEDEF VPSDGLDKDE YTFSPGKSKA TPEKSLHDKK SQDFGNLFSF
PSYSQKSEDD SAKFDSNEED SASVFSPSFG LKQIDKVPSK TVAAKKGKPS SDTAPKPKRA
PKQKKVVEAV NSDSDSEFGI PKKTTTPKGK GRGAKKRKAS GSENEGDYNP GRKTSKTASK
KPKKTSFDQD SDVDIFPSDF PSEPPSLPRT GRARKEVKYF AESDEEEEDV DFAMFN
//
