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 O60126

Entry ID Method Resolution Chain Position Source
AF-O60126-F1 Predicted AlphaFoldDB

No variants for O60126

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O60126

No associated diseases with O60126

10 regional properties for O60126

Type Name Position InterPro Accession
domain DNA topoisomerase, type IA, domain 2 107 - 195 IPR003601
domain DNA topoisomerase, type IA, DNA-binding domain 249 - 519 IPR003602
domain TOPRIM domain 1 - 116 IPR006171
domain DNA topoisomerase, type IA, central 75 - 88 IPR013497-1
domain DNA topoisomerase, type IA, central 131 - 567 IPR013497-2
domain DNA topoisomerase, type IA, zn finger 599 - 633 IPR013498
active_site DNA topoisomerase, type IA, active site 286 - 308 IPR023406
repeat Topoisomerase C-terminal repeat 661 - 718 IPR025589-1
repeat Topoisomerase C-terminal repeat 720 - 769 IPR025589-2
domain DNA topoisomerase 1, TOPRIM domain 1 - 128 IPR034149

Functions

Description
EC Number 5.6.2.1 Enzymes altering nucleic acid conformation
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 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.
RecQ family helicase-topoisomerase III complex A complex containing a RecQ family helicase and a topoisomerase III homologue (a member of the topoisomerase type IA subfamily); may also include one or more additional proteins; conserved from E. coli to human.
site of double-strand break A region of a chromosome at which a DNA double-strand break has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix.

3 GO annotations of molecular function

Name Definition
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA topoisomerase activity Catalysis of the transient cleavage and passage of individual DNA strands or double helices through one another, resulting a topological transformation in double-stranded DNA.
DNA topoisomerase type I (single strand cut, ATP-independent) activity Catalysis of a DNA topological transformation by transiently cleaving one DNA strand at a time to allow passage of another strand; changes the linking number by +1 per catalytic cycle.

5 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.
maintenance of rDNA Any process involved in sustaining the fidelity and copy number of rDNA repeats.
mitotic DNA replication Any nuclear DNA replication that is involved in a mitotic cell cycle.
postreplication repair The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication. Includes pathways that remove replication-blocking lesions in conjunction with DNA replication.
resolution of meiotic recombination intermediates The cleavage and rejoining of intermediates, such as Holliday junctions, formed during meiotic recombination to produce two intact molecules in which genetic material has been exchanged.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MRVLCVAEKN SIAKSVASIL GGGHVRRRDT RSKYVKNYDF SFNFGGNVGS SDVTMTSVSG
70 80 90 100 110 120
HLTEASFPSE YSSWSSVPQD VLFDAQIITS VSKNAEVLAD NIKKEARNAQ YLYIWTDCDR
130 140 150 160 170 180
EGEHIGVEIS NVARASNPSI QVIRADFNNL ERSHIISAAK RPRDVSKNAA DAVDARIELD
190 200 210 220 230 240
FRLGAIFTRL QTIQLQKSFD ILQNKIISYG PCQFPTLGFV VDRWQRVEDF VPETYWHLRF
250 260 270 280 290 300
VDKRQGKTIQ FNWERAKVFD RLTTMIILEN CLECKTAKVV NITQKPKTKY KPLPLSTVEL
310 320 330 340 350 360
TKLGPKHLRI SAKKTLELAE NLYTNGFVSY PRTETDQFDS SMNLHAIIQK LTGAQEWDSY
370 380 390 400 410 420
AEGLLAGDYR PPRKGKHNDR AHPPIHPVQM VHRSALPSQD HWKVYELITR RFLACCSDNA
430 440 450 460 470 480
KGAETLVQVK MEEELFSKKG LLVTEKNYLE VYPYEKWESS DQLPEYRLHE EFQPHILDMM
490 500 510 520 530 540
DSSTSSPSYI TEPELIALMD ANGIGTDATM AEHIEKVQER EYVIKRKKRG QGVTEFVPSS
550 560 570 580 590 600
LGVALAKGYD EIGLEWSLTK PFLRKEMEVQ LKNIENGQLN RNVLVHMILT QFRDVFHLTK
610 620
QRFDCLKNSC RVYLMSHNEP QT