ID A0A401SRI7_CHIPU Unreviewed; 1605 AA.
AC A0A401SRI7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=chiPu_0011474 {ECO:0000313|EMBL:GCC33008.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC33008.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC33008.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC33008.1}.
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DR EMBL; BEZZ01000478; GCC33008.1; -; Genomic_DNA.
DR STRING; 137246.A0A401SRI7; -.
DR OMA; QEMGYDS; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
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 GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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:SF61; DNA TOPOISOMERASE 2-ALPHA; 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; SM00387; HATPase_c; 1.
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 Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 456..573
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1088..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1114
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1370..1407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1551..1567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1605 AA; 181895 MW; B17D00CA7B3EB997 CRC64;
MASDLASSPL RPLFPNQISK LKKGDDRQLS VERIYQKKTQ LEHILLRPDS YIGSVEPVSQ
QMWVFDEEVG LNCREVTFVP GLYKIFDEIL VNAADNKQRD KNMSCIKINI DPENNSVTVW
NNGKGIPVVE HKIEKVFVPN LIFGQLLTSS NYDDDQKKVT GGRNGYGAKL CNIFSTKFTV
ETACREYKKS FKQTWTNNMG DAKEAKIKSF DGDDYTCITF QPDLPKFKMQ TLDKDIVAIM
SRRAYDIAGT CKGVKVFLNG KKLPVSGFRS YVDLYVKDKV DETGSPLKII HEVVNERWEV
CVTMSEKGFQ QISFANSIAT TKGGRHVDYV TDQLVNKLIE VVKKKNKGGV AVKPFQVKNH
LWVFVNSLIE NPTFDSQTKE NMTLQAKSFG SQCVLSEKFI KAAMNCGVVE SIMNWVKFKA
QNMLNKKCSG LKQTKIKGIP KLDDANDAGT KHSHGCTLIL TEGDSAKTLA VSGLGVVGRD
RYGVFPLRGK LLNVREASHK QIMENAEINN MIKIIGLQYK KNYDDQESLK TLRYGKLMIM
TDQDQDGSHI KGLVINFIHH NWPSLLRHNF IEEFITPIVK VSKNKQEIAF YSIPEFEEWR
SKTESNKTWK VKYYKGLGTS TAKEAKEYFA EMQRHRIPFK YNGPEDDSAI TLAFSRKKID
ERKEWLTNFM VDRRQRKLHG LPDQYLYGKE IKYLTFNDFI NKELVLFSNS DNERSIPSLV
DGLKPGQRKV LFTCFKRNDK REVKVAQLAG SVAEMSAYHH GEASLMMTIV GLAQDFVGSN
NINLLKPIGQ FGTRLNGGKD AASPRYIFTM LSALTRLLFP ATDDNLLKYL DDDNQRVEPE
WYMPIVPMVL VNGAEGIGTG WACKIPNYDI REIVDNIRRM LDGDEPLPML PNYKNFKGTI
FELGANQYMV IGEISVLDTT TIEISELPIK TWTQTYKEQV LEPMLNGTEK TPSLITGYKE
YHTDTSVRFI VTMTEQKLAE AEAAGLHKVF KLNVPLTCNS MVLFDHVGCL KKYENVQDIL
KEFFDLRLKY YRLRKDWLEG FLGAEYGKLS NQARFILEKI EGTLVIENKP KRELIQLLLD
RGYDSDPVKR WKESQDKEQE SELENTEEEE EITTSSGADF NYLLNMPLWY LTKEKKDELL
KQRDVKETEL KCLKRKSPSD LWKEDLAAFI EELERVEMQE KEDELAHVGK AVKGKGGKGK
MRKLQLEETM PSPHGRRVVP RVTSAMKTEA TRKNIKKKGK GETDSLAVKM EFGDKEGSSP
EYANLAERIS KKVKTKAETK TKPTAQKQTK LQFKPLAKKK NPWSDSDSMS ESDDDVEVID
LPPRQKQQRA AASKAKYVLE SSDEDDDNGD KMMSEVESDD ECHISDSGTE FSKPKANCTL
KKVQSKPSVK SVPQENEIFQ SSQESSKTFG EDMEKHIPQI VDEVLSSSDS VNEPEVSPIH
CNTYKPKGKK AAAKPAGEKA APKKRALGKK PTTVSKKDEN QPSIFDVLTK QKAAPKFSKT
ALKAKNKTSS DDDNVTKKVA PAKGKKTKRK KDSDSDSEFD FGLKPAKSAA NKKSKMKEDD
SYHIDIDEDS NSNISLGGAP PRVTSRAKKP VQYLEDSDDD DDDLF
//
