DNA topoisomerase 2 - Bombyx mori (Silk moth)

Preferred order of sections

Names and origin

Protein names

Recommended name:
DNA topoisomerase 2
EC=5.99.1.3

Alternative name(s):
DNA topoisomerase II
Short name=TOPOII

Gene names

Name:

TOP2

Organism

Bombyx mori (Silk moth) [Reference proteome]

Taxonomic identifier

7091 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Bombycoidea › Bombycidae › Bombycinae › Bombyx

Protein attributes

Sequence length	1547 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.
Catalytic activity	ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Cofactor	Magnesium. Binds two Mg²⁺ per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn²⁺ and Ca²⁺ By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Nucleus By similarity.
Miscellaneous	Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils.
Sequence similarities	Belongs to the type II topoisomerase family. Contains 1 Toprim domain.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	ATP-binding DNA-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Isomerase Topoisomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA topological change Inferred from electronic annotation. Source: InterPro
Cellular_component	chromosome Inferred from electronic annotation. Source: InterPro nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA topoisomerase type II (ATP-hydrolyzing) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1547

1547

DNA topoisomerase 2

PRO_0000145373

Regions

Domain

463 – 580

118

Toprim

Nucleotide binding

156 – 158

3

ATP By similarity

Nucleotide binding

169 – 176

8

ATP By similarity

Nucleotide binding

385 – 387

3

ATP By similarity

Region

351 – 353

3

Interaction with DNA By similarity

Sites

Active site

813

1

O-(5'-phospho-DNA)-tyrosine intermediate By similarity

Metal binding

469

1

Magnesium 1; catalytic By similarity

Metal binding

549

1

Magnesium 1; catalytic By similarity

Metal binding

549

1

Magnesium 2 By similarity

Metal binding

551

1

Magnesium 2 By similarity

Binding site

99

1

ATP By similarity

Binding site

128

1

ATP By similarity

Site

497

1

Interaction with DNA By similarity

Site

500

1

Interaction with DNA By similarity

Site

669

1

Interaction with DNA By similarity

Site

670

1

Interaction with DNA By similarity

Site

731

1

Interaction with DNA By similarity

Site

765

1

Interaction with DNA By similarity

Site

771

1

Interaction with DNA By similarity

Site

812

1

Transition state stabilizer By similarity

Site

864

1

Important for DNA bending; intercalates between base pairs of target DNA By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O16140 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: EDFE086253F22CEE
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FASTA

1,547

176,184

        10         20         30         40         50         60 
MADIKSMFNK MSSPKQNGTG EPAPAKGQKG AIEKIYQKKS QLEHILLRPD TYIGSVERAT 

        70         80         90        100        110        120 
ETMWVYDKVK ECMMQKELTS VPDCSFPGLY KIYDEILVNA ADNKQRDPKM DVIKIDINQE 

       130        140        150        160        170        180 
TNTISVYNNG SGIPVVMHKD EKMYVPTMIF GHLLTSSNYN DEEEKVTGGR NGYGAKLCNI 

       190        200        210        220        230        240 
FSTKFTVETA SKQYKKHFKQ TWGSNMTKAS EPKIKDSGKD DDFTKIVFSP DLAKFKMEKL 

       250        260        270        280        290        300 
EDDIVLLMSR RAYDVAASSQ GVKVYLNGER LKINKFKDYV DLYIKGKDDE NGQPLKVVYE 

       310        320        330        340        350        360 
KVSDRWEVAL TISDMGFQQV SFVNSIATTK GGKHVDTVAD SVVKNVLEVL KKKNKGGVNI 

       370        380        390        400        410        420 
KPYQVKTHMW LFVNCLIVNP TFDSQTKENM TLQAKSFGSK CNLSEKFITA VTKCGLVESV 

       430        440        450        460        470        480 
LTWAKFKAQD QLVKASGKKQ SKLKGIPKLE DANDAGTKNA HLCTLILTEG DSAKTLAVSG 

       490        500        510        520        530        540 
LSVVGRDHYG VFPLEGKPLN VRDASHKQVL ENVEINNLIK ILGLQYKKKY NSVDDLKTLR 

       550        560        570        580        590        600 
YGKVMIMADQ DQDGSHIKGL IINFIHHNWP ELLKLPFLEE FITPIVKATK KDKEISFYSL 

       610        620        630        640        650        660 
PEFEEWKKET ENHHTYNIKY YKGLGTSTSK EAKEYFQNMD RHRIRFKYSG PTDDHHIELA 

       670        680        690        700        710        720 
FSKKGADQRK EWLTNHMDEV KRRKEIGLSE RYLYTKETKT VTYSDFVNLE LVLFSNGDNV 

       730        740        750        760        770        780 
RSIPSMIDGL KPGQRKVIFT CIKRNDKREV KVAQLAGSVA EHSAYHHGEQ SLAMTIVNLA 

       790        800        810        820        830        840 
QNYVGSNNIN LLEPRGQFGT RLSGGKDSAS PRYIFTLMSP LTRLIFHPHD DPLLVHEFED 

       850        860        870        880        890        900 
NQKIEPVYYL PIIPMVLVNG VEGIGTGWST KIPNYNPRDI AENLRRLLDG EKPKVMHPWY 

       910        920        930        940        950        960 
KNFKGNVEGF GDKYVISGEA AILPGDKIEI TELPVGTWTH NYKENVLEPM LGTDKVKPLI 

       970        980        990       1000       1010       1020 
SEYREYNTDT TVRFVVSLLP GKLSEIEAEG IHKVFKLQTT ISMTCMNAFD YNCCLEKYDK 

      1030       1040       1050       1060       1070       1080 
VEEILREFYD LRVKYYVRRK DYLEGQLQAE ADKLSNQARF ILKKCDKGLV IENKKRKAMV 

      1090       1100       1110       1120       1130       1140 
EELIKRGYAP DPIADWKKRA SKIQGLTALE DDDAQESEEE EPEPDPKGKP VDPDKAFQQL 

      1150       1160       1170       1180       1190       1200 
KEVKKFNYLL GMSMWMLTKE KKDELLKQRD QKLTELTTLK NKTAPMLWRE DLDAFLIKLD 

      1210       1220       1230       1240       1250       1260 
EVEDKERREE LNVNKKTSKA MAGKKNRKSM FDIIPSENGR RVEPKISDDL IKRIQAAEKA 

      1270       1280       1290       1300       1310       1320 
KTRKEIKKEY DPDDPTGISP SSGEKKPKAR VKKEKPEKAE KPDKVDKAEK TDGLKQTKLT 

      1330       1340       1350       1360       1370       1380 
FKKEPKKKKM TFSGSSSGEM SASDAEVEVL VPRERTNARR AATRVQKYKD GSDDSGSDSE 

      1390       1400       1410       1420       1430       1440 
PELLDNKIDS DHEAPQTLSI SDEDDDFNIK KNPAKKPAEM DSDCLFDSLI EDAKKDEPQK 

      1450       1460       1470       1480       1490       1500 
TLTKSKSESI LIRRLNIERQ RRCDTSVPPK EKAAPKRKLM NVDKDEKKTK KRPARVMLDQ 

      1510       1520       1530       1540 
DSDDEDSIFD SKKGKKKTAA NPKKKAKKKV ESDSESDFNI SDSSLSD

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References

[1]	"Cloning of topoisomerase II from the silkworm Bombyx mori." Larsen J.J. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF013277 mRNA. Translation: AAB67168.1.
RefSeq	NP_001037009.1. NM_001043544.1.
UniGene	Bmo.164.
3D structure databases
ProteinModelPortal	O16140.
SMR	O16140. Positions 31-434.
ModBase	Search...
Proteomic databases
PRIDE	O16140.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	692558.
Organism-specific databases
CTD	35225.
Family and domain databases
Gene3D	1.10.268.10. 1 hit. 3.30.1360.40. 1 hit. 3.30.230.10. 1 hit. 3.30.565.10. 1 hit. 3.40.50.670. 1 hit. 3.90.199.10. 1 hit.
InterPro	IPR024946. Arg_repress_C-like. IPR003594. HATPase_ATP-bd. IPR020568. Ribosomal_S5_D2-typ_fold. IPR014721. Ribosomal_S5_D2-typ_fold_subgr. IPR001241. Topo_IIA. IPR002205. Topo_IIA_A/C. IPR013758. Topo_IIA_A/C_ab. IPR013757. Topo_IIA_A_a. IPR013506. Topo_IIA_bsu_dom2. IPR013759. Topo_IIA_cen_dom. IPR013760. Topo_IIA_like_dom. IPR018522. TopoIIA_CS. IPR006171. Toprim_domain. [Graphical view]
Pfam	PF00204. DNA_gyraseB. 1 hit. PF00521. DNA_topoisoIV. 1 hit. PF02518. HATPase_c. 1 hit. PF01751. Toprim. 1 hit. [Graphical view]
PRINTS	PR00418. TPI2FAMILY.
SMART	SM00387. HATPase_c. 1 hit. SM00433. TOP2c. 1 hit. SM00434. TOP4c. 1 hit. [Graphical view]
SUPFAM	SSF55874. ATP_bd_ATPase. 1 hit. SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit. SSF56719. Topo_IIA_cen. 1 hit.
PROSITE	PS00177. TOPOISOMERASE_II. 1 hit. PS50880. TOPRIM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TOP2_BOMMO

Accession

Primary (citable) accession number: O16140

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Family and domain databases

Entry information

Relevant documents