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

5 structures for O42861

Entry ID Method Resolution Chain Position Source
7XWY X-ray 225 A A 232-620 PDB
7XXE X-ray 420 A A/B 626-903 PDB
7XYF EM 430 A K 232-903 PDB
7XYG EM 540 A K 1-922 PDB
AF-O42861-F1 Predicted AlphaFoldDB

2 variants for O42861

Variant ID(s) Position Change Description Diseaes Association Provenance
I_2100671_C_T 127 A>T No Jeffares_SNPs
I_2099756_T_G 432 K>Q No Jeffares_SNPs

No associated diseases with O42861

3 regional properties for O42861

Type Name Position InterPro Accession
domain SNF2, N-terminal 406 - 665 IPR000330
domain Helicase, C-terminal 762 - 922 IPR001650
domain Helicase superfamily 1/2, ATP-binding domain 383 - 579 IPR014001

Functions

Description
EC Number 3.6.4.12 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
  • Nucleus
  • Chromosome
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
chromatin The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome.
heterochromatin A compact and highly condensed form of chromatin that is refractory to transcription.
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.

8 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
ATP-dependent activity, acting on DNA Catalytic activity that acts to modify DNA, driven by ATP hydrolysis.
ATP-dependent chromatin remodeler activity An activity, driven by ATP hydrolysis, that modulates the contacts between histones and DNA, resulting in a change in chromosome architecture within the nucleosomal array, leading to chromatin remodeling.
chromatin binding Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
damaged DNA binding Binding to damaged DNA.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA helicase activity Unwinding of a DNA helix, driven by ATP hydrolysis.

4 GO annotations of biological process

Name Definition
attachment of telomeric heterochromatin to nuclear envelope The process in which physical connections are formed between sub-telomeric heterochromatin and the nuclear envelope facilitating bouquet formation.
chromatin remodeling A dynamic process of chromatin reorganization resulting in changes to chromatin structure. These changes allow DNA metabolic processes such as transcriptional regulation, DNA recombination, DNA repair, and DNA replication.
positive regulation of DNA strand resection involved in replication fork processing Any process that activates or increases the frequency, rate or extent of DNA strand resection involved in replication fork processing.
replication fork processing The process in which a DNA replication fork that has stalled is restored to a functional state and replication is restarted. The stalling may be due to DNA damage, DNA secondary structure, bound proteins, dNTP shortage, or other causes.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDGKRKIEHT ADGTHYDATS NVKRKPIFPP FIADSLSEAT EKANVMGGGM NSRLQILSEM
70 80 90 100 110 120
SKRVQATAPI SSLEHFKQLS DISPSFTSSA NSINQPYNYS GSLENLVPTP SAGTPSQFMD
130 140 150 160 170 180
AQNPYGAVYN ALSQFSETEP KMPSYMDDEE ASDSLPLSLS SQSLSSQVTN QKPAPHRLTM
190 200 210 220 230 240
RERYAANNLT NGLQFTLPLS SRKTYEPEAD DDSNDDMYSD DDSNADRWAS RIDTAALKEE
250 260 270 280 290 300
VLKYMNRCST QDLADMTGCT LAEAEFMVAK RPFPDLESAL VVKQPRPVIP KGRRGRREKT
310 320 330 340 350 360
PLGPRLVGIC MEIMRGYFVV DALIRQCEQL GGKIQRGIEA WGLSNTATSD EGETSLVNFD
370 380 390 400 410 420
QMKSFGTPAN SSFITTPPAS FSPDIKLQDY QIIGINWLYL LYELKLAGIL ADEMGLGKTC
430 440 450 460 470 480
QTIAFFSLLM DKNINGPHLV IAPASTMENW LREFAKFCPK LKIELYYGSQ VEREEIRERI
490 500 510 520 530 540
NSNKDSYNVM LTTYRLAATS KADRLFLRNQ KFNVCVYDEG HYLKNRASER YRHLMSIPAD
550 560 570 580 590 600
FRVLLTGTPL QNNLKELISL LAFILPHVFD YGLKSLDVIF TMKKSPESDF ERALLSEQRV
610 620 630 640 650 660
SRAKMMMAPF VLRRKKSQVL DALPKKTRII EFCEFSEEER RRYDDFASKQ SVNSLLDENV
670 680 690 700 710 720
MKTNLDTNAN LAKKKSTAGF VLVQLRKLAD HPMLFRIHYK DDILRQMAKA IMNEPQYKKA
730 740 750 760 770 780
NELYIFEDMQ YMSDIELHNL CCKFPSINSF QLKDEPWMDA TKVRKLKKLL TNAVENGDRV
790 800 810 820 830 840
VLFSQFTQVL DILQLVMKSL NLKFLRFDGS TQVDFRQDLI DQFYADESIN VFLLSTKAGG
850 860 870 880 890 900
FGINLACANM VILYDVSFNP FDDLQAEDRA HRVGQKKEVT VYKFVVKDTI EEHIQRLANA
910 920
KIALDATLSG NAETVEAEDD DD