Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for B8BDQ4

Entry ID Method Resolution Chain Position Source
AF-B8BDQ4-F1 Predicted AlphaFoldDB

No variants for B8BDQ4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B8BDQ4

No associated diseases with B8BDQ4

1 regional properties for B8BDQ4

Type Name Position InterPro Accession
domain DNA topoisomerase VI, subunit B, transducer 425 - 584 IPR015320

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

2 GO annotations of cellular component

Name Definition
DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex Complex that possesses DNA topoisomerase II (double strand cut, ATP-hydrolyzing) activity.
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.
protein homodimerization activity Binding to an identical protein to form a homodimer.

6 GO annotations of biological process

Name Definition
cell morphogenesis The developmental process in which the size or shape of a cell is generated and organized.
DNA endoreduplication Regulated re-replication of DNA within a single cell cycle, resulting in an increased cell ploidy. An example of this process occurs in the synthesis of Drosophila salivary gland cell polytene chromosomes.
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.
pattern specification process Any developmental process that results in the creation of defined areas or spaces within an organism to which cells respond and eventually are instructed to differentiate.
response to brassinosteroid Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a brassinosteroid stimulus.
trichome differentiation The process in which a relatively unspecialized epidermal cell acquires the specialized features of a trichome cell. An example of this process is found in Arabidopsis thaliana.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDDDAGDGAA SGGTKRKVTA ASSSAAAKGK AAGKGKAASK ASALATAKES SLLKQKSPAE
70 80 90 100 110 120
FFAENKNIAG FDNPGKSLYT TMRELVENAL DSAESISELP DIEIIIEEIT KSKFNTMIGL
130 140 150 160 170 180
VDRQRIDEEL YDDFESAKAR EKRLAKEARF QETQAKNAAL GKKVKEAPAA RGKGRGEAAF
190 200 210 220 230 240
FRVTCKDNGR GMPHDDIPNM LGRVLSGTKY GLRQTRGKFG LGAKMALIWS KMSTGLPIEI
250 260 270 280 290 300
KSSMKGQNFI SFCRLDIDIH KNVPHVHLHE KRENKDRWHG AELQVIIEGN WTTHRSKILH
310 320 330 340 350 360
YMRQMAVITP YAQFLFRFLS DSPDKNLTIQ FARRTDVMPP IPLQTKHHPS AVDLLLIKRL
370 380 390 400 410 420
ISETTKQNLL QFLQHEFVNI SKSHAERLIG EMGPDFSAKT TVKSLTSQQL VRIHQLFRQA
430 440 450 460 470 480
KFDDPSGNCL SPAGEYNLRL GIIKELHPDL VATHASSPQV FEGHPFIVEA GISIGGKDVK
490 500 510 520 530 540
HGLNIFRYAN RIPLLFEQGA DVITRTALKR INWSSYKINQ QQDKIGVFVS IVSTKIPFKG
550 560 570 580 590 600
TGKEYIGDDI TEIASAVQSA LKQCCLQLKS KIVKKLQARE RQDRKRNLNR YIPDVARAIM
610 620 630 640 650 660
ETLGEIADES PPKRPRYDKE DEELLEKVNS EEVTEMTFRD CLTQHVEQVD YEMALEYAMQ
670 680 690
SGVSEEPREA LYLNSLEGSY KFIDFQSPVF VFRFIP