DNA topoisomerase 2 - Pisum sativum (Garden pea)

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O24308 (TOP2_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
DNA topoisomerase 2
EC=5.99.1.3

Alternative name(s):
DNA topoisomerase II
PsTopII

Gene names

Name:	TOP2
Synonyms:	TOPII

Organism

Pisum sativum (Garden pea)

Taxonomic identifier

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

Protein attributes

Sequence length	1462 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.
Tissue specificity	Abundant in proliferative tissues.
Induction	By light and growth factors.
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
Ligand	ATP-binding DNA-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Isomerase Topoisomerase
Gene Ontology (GO)
Biological_process	DNA topological change Inferred from electronic annotation. Source: InterPro
Cellular_component	chromosome Inferred from electronic annotation. Source: InterPro
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

1462

DNA topoisomerase 2

PRO_0000145381

Regions

Domain

115

Toprim

Nucleotide binding

3

ATP By similarity

Nucleotide binding

8

ATP By similarity

Nucleotide binding

3

ATP By similarity

Sites

Active site

1

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

Metal binding

1

Magnesium 1; catalytic By similarity

Metal binding

1

Magnesium 1; catalytic By similarity

Metal binding

1

Magnesium 2 By similarity

Metal binding

1

Magnesium 2 By similarity

Binding site

1

ATP By similarity

Binding site

1

ATP By similarity

Site

1

Interaction with DNA By similarity

Site

1

Interaction with DNA By similarity

Site

1

Interaction with DNA By similarity

Site

1

Interaction with DNA By similarity

Site

1

Interaction with DNA By similarity

Site

1

Interaction with DNA By similarity

Site

1

Transition state stabilizer By similarity

Site

1

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

Sequences

Sequence

Length

Mass (Da)

Tools

O24308 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: D9212C54AE0F8B2E
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1,462

164,206

        10         20         30         40         50         60 
MEKRPLQTSN AANIPSKTIE EMYQKKTQLE HILLRPDTYV GSIEKHTQNL WVYENDEMVH 

        70         80         90        100        110        120 
RAVSYVPGLY KIFDEILVNA ADNKQRDPSM DSLKVTIDPE ANTVSVYNNG DGVPVEIHQE 

       130        140        150        160        170        180 
EKVYVPELIF GHLLTSSNYD DNVKKTTGGR NGYGAKLTNI FSTEFIIETA DGRRLKKYKQ 

       190        200        210        220        230        240 
VFSNNMGTKC EPVITKCKAS ENWTKVTFKP DLEKFKMAYL EEDVVALMKK RVLDMAGCFG 

       250        260        270        280        290        300 
KTVKVELNGT LIRFKSFRDY ADLFLKCAEK SKPMPLPRIH AKVGDRWEIC ISLSDGQFQQ 

       310        320        330        340        350        360 
VSFVNSIATI KGGTHVDYIT NQITTYIMNK VNKKKKDANV KAHTVKNHLW VFVNSLIDNP 

       370        380        390        400        410        420 
AFDSQTKETL TTRQASFGSK CDVPESMLKD VEKSGIVDTL LSWADFKQSK DLKKTDGTKT 

       430        440        450        460        470        480 
QRLRGCKAED ANEAGGRNSE KCTLILTEGD SAKALAMAGL SVVGRDHYGV FPLRGKLLNV 

       490        500        510        520        530        540 
REASSKQIMD NEEIQNIKKI LGLQQNKEYT NVKSLRYGHL MIMADQDHDG SHIKGLLINF 

       550        560        570        580        590        600 
IHSFWPSLLK VPSFLVEFTT PVIRASHPNK TITSFYSMPE YEAWKERLGN SATSWKIKYY 

       610        620        630        640        650        660 
KGLGTSTPQE GREYFSDLGR HRKDFIWDDE LDGNAIELAF SKKKAEGRKI WMRNFEPGTC 

       670        680        690        700        710        720 
RDHEAKLINY KDFVNKELIL FSRADLFGSF KKKLYKEIKV AQFIGYVSEH SAYHHGEQSL 

       730        740        750        760        770        780 
ASTIIGMAQD FVGSNNINLL KPNGQFGTCN LGGKDHASAR YIYTELSPVT RCLFHEHDDK 

       790        800        810        820        830        840 
LLEYLNEDGK SIEPNWYMPI IPLVLVNGSE GIGTGWSSYI PNYNPREIIA NVRRLLNGEE 

       850        860        870        880        890        900 
LVPMDPWYKG FRGTIEKSAK EGGYIVNGTV TEIDEQTFRI TELPIRKWTQ DYKQFLESIT 

       910        920        930        940        950        960 
DGAPNVKDPL IEDFRQNGDD AIVDIEIKMK PEKIATILQE GLFKKFKLTS TISTSNMHLF 

       970        980        990       1000       1010       1020 
DAEGNKKFDT PEQILEEFFP LRLDYYEKSK EYILGNLNRL LLILDNKVRF ILGVVNGEII 

      1030       1040       1050       1060       1070       1080 
VSNRKKAELL IELKEKGFTP MPRKGKSTKP QVAGANDDDS EEQEDAEPET ASQSVSVEGA 

      1090       1100       1110       1120       1130       1140 
TWGDYDDLLS LPIGTLTLES VQKLLDEKTE KEKEYEILSG TPTTSLWLKD LDEFEKKLDE 

      1150       1160       1170       1180       1190       1200 
LDLKYAEDDR KRASQGSKKA NGFASKPAKK PPQPRKNTKK AKSVEPENDN SSMEIENAVE 

      1210       1220       1230       1240       1250       1260 
AAKPAEVAKP KGRAAPKKNI QKEPEDDIQS LQERLAAYNI ESSGEKSQAM ESEEVQQKAA 

      1270       1280       1290       1300       1310       1320 
GKKQNNKRGG AKKKSSTIVL ESDSDNEVND VDDDDDDFEE VQQKAAPVKK GGRKPAAQNA 

      1330       1340       1350       1360       1370       1380 
KKAPAKAPAK APAAPKKRSV GTKQSAGQKL LTDMLQPAEG TGTSPEKKVR KMRESPFNKK 

      1390       1400       1410       1420       1430       1440 
SGSILGRAAA AKDISPIADC SAGSASNTPL SEDEVVEIAP QPARARPQRA NRTQMKYALS 

      1450       1460 
ESESEEDSDE DAELSDFEED DD

References

[1]

"Cloning and characterization of a cDNA encoding topoisomerase II in pea and analysis of its expression in relation to cell proliferation."
Reddy M.K., Nair S., Tewari K.K., Mudgil Y., Yadav B.S., Sopory S.K.
Plant Mol. Biol. 41:125-137(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leaf.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y14559 mRNA. Translation: CAA74891.1.
PIR	T06819.
3D structure databases
ProteinModelPortal	O24308.
SMR	O24308. Positions 18-392.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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. 2 hits.
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_PEA

Accession

Primary (citable) accession number: O24308

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents