ID G3SGP2_GORGO Unreviewed; 1553 AA.
AC G3SGP2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 70.
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:ENSGGOP00000027278.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000027278.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000027278.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000027278.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000027278.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; CABD030020360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030020361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSGGOT00000031843.2; ENSGGOP00000027278.2; ENSGGOG00000028083.2.
DR GeneTree; ENSGT00940000157921; -.
DR HOGENOM; CLU_001935_1_0_1; -.
DR Proteomes; UP000001519; Chromosome 3.
DR Bgee; ENSGGOG00000028083; Expressed in cerebellum and 6 other cell types or tissues.
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 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:UP000001519};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 467..584
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1101..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1318
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1553 AA; 175629 MW; 3F089F8CB749AF5D CRC64;
HLKLGGGGCS EPRSHHCTLN NAAKKEESET ANKNDSSKKL SVERVYQKKT QLEHILLRPD
TYIGSVEPLM QFMWVYDEDV GMNCREVTFV PGLYKIFDEI LVNAADNKQR DKNMTCIKVS
IDPESNIISI WNNGKGIPVV EHKVEKVYVP ALIFGQLLTS SNYDDDEKKV TGGRNGYGAK
LCNIFSTKFT VETACKEYKH SFKQTWMNNM MKTSEAKIKH FDGEDYTCIT FQPDLSKFKM
EKLDKDIVAL MTRRAYDLAG SCRGVKVMFN GKKLPVNGFR SYVDLYVKDK LDETGVALKV
IHELANERWD VCLTLSEKGF QQISFVNSIA TTKGGRHVDY VVDQVVGKLI EVVKKKNKAG
VSVKPFQVKN HIWVFINCLI ENPTFDSQTK ENMTLQPKSF GSKCQLSEKF FKAASNCGIV
ESILNWVKFK AQTQLNKKCS SVKYSKIKGI PKLDDANDAG GKHSLECTLI LTEGDSAKSL
AVSGLGVIGR DRYGVFPLRG KILNVREASH KQIMENAEIN NIIKIVGLQY KKSYDDAESL
KTLRYGKIMI MTDQDQDGSH IKGLLINFIH HNWPSLLKHG FLEEFITPIV KASKNKQELS
FYSIPEFDEW KKHIENQKAW KIKYYKGLGT STAKEAKEYF ADMERHRILF RYAGPEDDAA
ITLAFSKKKI DDRKEWLTNF MEDRRQRRLH GLPEQFLYGT ATKHLTYNDF INKELILFSN
SDNERSIPSL VDGFKPGQRK VLFTCFKRND KREVKVAQLA GSVAEMSAYH HGEQALMMTI
VNLAQNFVGS NNINLLQPIG QFGTRLHGGK DAASPRYIFT MLSTLARLLF PAVDDNLLKF
LYDDNQRVEP EWYIPIIPMV LINGAEGIGT GWACKLPNYD AREIVNNVRR MLDGLDPHPM
LPNYKNFKGT IQELGQNQYA VSGEIFVVDR NTVEITELPV RTWTQVYKEQ VLEPMLNGTD
KTPALISDYK EYHTDTTVKF VVKMTEEKLA QAEAAGLHKV FKLQTTLTCN SMVLFDHMGC
LKKYETVQDI LKEFFDLRLS YYGLRKEWLV GMLGAESTKL NNQARFILEK IQGKITIENR
SKKDLIQMLV QRGYESDPVK AWKEAQEKAA EEDETQNQHD DSSSDSGTPS GPDFNYILNM
SLWSLTKEKV EELIKQRDAK GREVNDLKRK SPSDLWKEDL AAFVEELDGD LDTAAVKVEF
DEEFSGAPVE GAGEEALTPS VPINKGPKPK REKKEPGTRV RKTPTSSGKP SAKKVKKRNP
WSDDESKSES DLEETEPVVI PRDSLLRRAA AERPKYTFDF SEEEDDDADD DDDDDNNDLE
ELKVKASPIT NDGEDEFVPS DGLDKDEYTF SPGKSKATPE KSLHDKKSQD FGNLFSFPSY
SQKSEDDSAK FDSNEEDSAS VFSPSFGLKQ TDKVPSKTVA AKKGKPSSDT VPKPKRAPKQ
KKVVEAVNSD SDSEFGIPKK TTTPKGKGRG AKKRKASGSE NEGDYNPGRK TSKTTSKKPK
KTSFDQDSDV DIFPSDFPTE PPSLPRTGRA RKEVKYFAES DEEEEDVDFA MFN
//
