P41001

PR
Gene name
TOP2
Protein name
DNA topoisomerase 2
Names
DNA topoisomerase II
Species
Plasmodium falciparum (isolate K1 / Thailand)
KEGG Pathway
EC number
5.6.2.2: Enzymes altering nucleic acid conformation
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

425-507 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P41001

Entry ID Method Resolution Chain Position Source
AF-P41001-F1 Predicted AlphaFoldDB

No variants for P41001

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P41001

No associated diseases with P41001

7 regional properties for P41001

Type Name Position InterPro Accession
domain DNA topoisomerase, type IIA, domain A 717 - 1194 IPR002205
domain Histidine kinase/HSP90-like ATPase 56 - 158 IPR003594
domain TOPRIM domain 493 - 608 IPR006171
domain DNA topoisomerase, type IIA, subunit B, domain 2 320 - 461 IPR013506
conserved_site DNA topoisomerase, type IIA, conserved site 497 - 505 IPR018522
domain C-terminal associated domain of TOPRIM 610 - 734 IPR031660
domain DNA topoisomerase 2, TOPRIM domain 493 - 612 IPR034157

Functions

Description
EC Number 5.6.2.2 Enzymes altering nucleic acid conformation
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity Catalysis of a DNA topological transformation by transiently cleaving a pair of complementary DNA strands to form a gate through which a second double-stranded DNA segment is passed, after which the severed strands in the first DNA segment are rejoined, driven by ATP hydrolysis. The enzyme changes the linking number in multiples of 2.
metal ion binding Binding to a metal ion.

1 GO annotations of biological process

Name Definition
DNA topological change The process in which a transformation is induced in the topological structure of a double-stranded DNA helix, resulting in a change in linking number.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAKNKTIEER YQKKSQIEHI LLRPDTYIGS VEMHTQLLWV WNKEKNRMVQ KNITYVPGLY
70 80 90 100 110 120
KIFDEIIVNA ADVKAREKEK SENPMTCIKI EINKENKRIS VYNDGEGIPV DIHKEMNIYV
130 140 150 160 170 180
PHMIFGELLT SDNYDDAEDR ITGGRNGFGA KLTNIFSKEF IVQCGDSSRK KEFKMTWSDN
190 200 210 220 230 240
MSKFSEPHIK NYNGKDYVKV TFKPDLNKFG MTEMDDDIES LLFKRVYDLA GTCSVRVYLN
250 260 270 280 290 300
GQRLAVKDFK SYVDLYLKDN SNDNKNNKGQ NDNNNNNNNN NDENANQNND NLDVSLSNEP
310 320 330 340 350 360
ADGTPTKNNN NNNNNNDEDE IVKIHEKQHR WEIVVSKSDG SQFQQVSFVN SICTTKGGSH
370 380 390 400 410 420
VNYIVEQLLS SLSKKANAKN KGGMEIKSGH IRNHLWVFVN CLIVNPTFDS QTKETLTTKP
430 440 450 460 470 480
VKFGSKCILS DKTINNVLKS PILSNILLWA QAKAQVELKK KMKAGSSKAR ERIIGIPKLE
490 500 510 520 530 540
DANDAGSKYS QECTLILTEG DSAKTSCLAG LSIVGRDKYG VFPLKGKLLN VRDASFKQLM
550 560 570 580 590 600
DNKEIQNIFR IMGLDITDKN KDDIKGLRYG SLMIMTDQDY DGSHIKGLLI NMIHKFWPSL
610 620 630 640 650 660
LKHKGFLSEF VTPIVKVQKG SQEYSFFTIA EYEQWKENTN LLGWKIKYYK GLGTSTDREF
670 680 690 700 710 720
KQYFSDIKNH KIMFLWTGDR DGDSIDMAFS KKRIEDRKLW LQNFILGSYV DHKEKDLSYY
730 740 750 760 770 780
DFVNKELIYY SRYDTERSIP NIMDGWKPGQ RKVLYGCFKR NLRNECKVAQ LVGYIAEHSA
790 800 810 820 830 840
YHHHGESSLQ QTIINMAQTF VGSNNINFLE PCGQFGSRKE GGKDASAARY IFTKLASSTR
850 860 870 880 890 900
SIFNEYDDPI LKYLNEEGQK IEPQYYIPVI PTILVNGCEG IGTGYSSFIP NYNYKDIIDN
910 920 930 940 950 960
IKRYINKEPL IPMVPWYKDF KGRIESNGKT GYETIGIINK IDNDTLEITE LPIKKWTQDY
970 980 990 1000 1010 1020
KEFLEELLTD EKHQLILDYI DNSSHEDICF TIKMDPAKLQ KAEEEGLEKV FKLKSTLTTT
1030 1040 1050 1060 1070 1080
NMTLFDPNLK LQRYSTELDI LKEFCYQRLK AYENRKSYLI SKLEKEKRII SNKTKFILAI
1090 1100 1110 1120 1130 1140
VNNELIVNKK KKKVLVEELY RKGYDPYKDI NKIKKEEIFE QELLDAADNP EDNEEIIAGI
1150 1160 1170 1180 1190 1200
TVKDYDYLLS MPIFSLTLEK VEDLLTQLKE KERELEILRN ITVETMWLKD IEKVEEAIEF
1210 1220 1230 1240 1250 1260
QRNVELSNRE ESNKFKVARK QGPSSMKKKK KKKKLSSDEE SEGGDTSDSS EFLVNTLNIK
1270 1280 1290 1300 1310 1320
KNTNKKTTTS SNNVNNSKKR LRKADDLNSN ELDNTLSVSK TFDDNNNLTD NTPLINRLND
1330 1340 1350 1360 1370 1380
ENNEFSSNNV DNKSTNKNSR KKKPKIADST NDNNSELNSS IQINDNVNDD INITISPNKT
1390
INVNEFSSIK NKLLELGI