A0A2R6QMF5 · A0A2R6QMF5_ACTCC
- ProteinProtein CHROMATIN REMODELING like
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids2125 (go to sequence)
- Protein existencePredicted
- Annotation score2/5
Function
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent chromatin remodeler activity | |
Molecular Function | chromatin binding | |
Molecular Function | DNA binding | |
Molecular Function | helicase activity | |
Molecular Function | histone binding | |
Molecular Function | metal ion binding |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > Ericales > Actinidiaceae > Actinidia
Accessions
- Primary accessionA0A2R6QMF5
Proteomes
Genome annotation databases
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-90 | Disordered | ||||
Sequence: MKESSSTTSKMSNWNKASKRKRSKVPCGEDIFNGKEGSSTPLEPPTSSSSKRRLKNETSKEGSSTPLEPPTSPSSKRRLKNETSSDPSAI | ||||||
Compositional bias | 60-78 | Polar residues | ||||
Sequence: KEGSSTPLEPPTSPSSKRR | ||||||
Domain | 99-146 | PHD-type | ||||
Sequence: YYECVICDLGGNLLCCDSCPRTYHLQCLDPPLKRIPSGKWQCPKCCQK | ||||||
Region | 236-392 | Disordered | ||||
Sequence: SSVNIDNEKKPELSPIDQPGEKKSISPEMEVSSVSTTMDLKSNNEAVEMTPDLLGDNGSPGKKVVSDSGAAKKDKKRKRKTHISESQKKTRTDGGKLTMDSSRKRGSEVNSSRPRTSKSHRKRNEASASGSKEDIRTLSANIHPKDEHVSEETGNLS | ||||||
Compositional bias | 263-279 | Polar residues | ||||
Sequence: EMEVSSVSTTMDLKSNN | ||||||
Compositional bias | 321-365 | Basic and acidic residues | ||||
Sequence: SQKKTRTDGGKLTMDSSRKRGSEVNSSRPRTSKSHRKRNEASASG | ||||||
Compositional bias | 373-388 | Basic and acidic residues | ||||
Sequence: LSANIHPKDEHVSEET | ||||||
Region | 459-486 | Disordered | ||||
Sequence: LATENPDGDKTLDGGAAENSTEGCQNIM | ||||||
Region | 508-555 | Disordered | ||||
Sequence: REGKGLGSARRDTNGSSSTAPCGKNQDDPAGNTGDLETTTEKISGGEK | ||||||
Compositional bias | 517-553 | Polar residues | ||||
Sequence: RRDTNGSSSTAPCGKNQDDPAGNTGDLETTTEKISGG | ||||||
Domain | 598-653 | Chromo | ||||
Sequence: IETQSSVPAKVTSDGASVLYEFLVKWVGKSHIHNTWVSESQLKALAKRKLDNYRAK | ||||||
Domain | 667-719 | Chromo | ||||
Sequence: KQPQRVIALRTSKDGSTEAFIKWTGLPYDECSWERIDEPVVANMSHLIDLFKQ | ||||||
Domain | 773-950 | Helicase ATP-binding | ||||
Sequence: RKCWHKSKNVILADEMGLGKTVSACAFMSSLYFEFKVKLPCLVLVPLSTMPNWMAEFASWAPHLNVVEYHGCAKARAIVRQHEWHANDPSGLNKKTTSYKFNVLLTTYEMVLADSSHLRAVPWEVLVVDEGHRLKNSSSKLFSLLNTISFQHRVLLTGTPLQNNIGEMYNLLNFLQPA | ||||||
Domain | 1080-1232 | Helicase C-terminal | ||||
Sequence: LLHSMLKLLRKDGHRVLIFSQMTKLLDILEDYLTIEFGPKTFERVDGSVSVADRQTAIARFNQDSSKFVFLLSTRSCGLGINLATADTVIIYDSDFNPHADIQAMNRAHRIGQSKRLLVYRLVVRASVEERILQLAKKKLMLDQLFVNKSGWE | ||||||
Region | 1259-1341 | Disordered | ||||
Sequence: TLQPGETLSEGGHDEEPVPVPEPEREYTEAGRFHKEKYAKRRARQKERLAQRNVEETSAPIDGVTRPESLHEVPVANSKDREQ | ||||||
Compositional bias | 1267-1294 | Basic and acidic residues | ||||
Sequence: SEGGHDEEPVPVPEPEREYTEAGRFHKE | ||||||
Region | 1968-2013 | Disordered | ||||
Sequence: TPTIPPFLVPGPPPSQPTDPRKSLKKKNRRANTPGQFPPVPQSAVG | ||||||
Compositional bias | 1972-1986 | Pro residues | ||||
Sequence: PPFLVPGPPPSQPTD | ||||||
Compositional bias | 2035-2066 | Polar residues | ||||
Sequence: NPSSSSVLPNPQKKSSTGLSPSPETGPLAAVT | ||||||
Region | 2035-2125 | Disordered | ||||
Sequence: NPSSSSVLPNPQKKSSTGLSPSPETGPLAAVTSSSLLGARGPHADNKIVQTQSEDSSKTHSDPILPEQRPDVEEISSEGTVSDHPVSDGEP | ||||||
Compositional bias | 2094-2112 | Basic and acidic residues | ||||
Sequence: HSDPILPEQRPDVEEISSE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,125
- Mass (Da)235,284
- Last updated2018-06-20 v1
- ChecksumA74B0C4554988722
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 60-78 | Polar residues | ||||
Sequence: KEGSSTPLEPPTSPSSKRR | ||||||
Compositional bias | 263-279 | Polar residues | ||||
Sequence: EMEVSSVSTTMDLKSNN | ||||||
Compositional bias | 321-365 | Basic and acidic residues | ||||
Sequence: SQKKTRTDGGKLTMDSSRKRGSEVNSSRPRTSKSHRKRNEASASG | ||||||
Compositional bias | 373-388 | Basic and acidic residues | ||||
Sequence: LSANIHPKDEHVSEET | ||||||
Compositional bias | 517-553 | Polar residues | ||||
Sequence: RRDTNGSSSTAPCGKNQDDPAGNTGDLETTTEKISGG | ||||||
Compositional bias | 1267-1294 | Basic and acidic residues | ||||
Sequence: SEGGHDEEPVPVPEPEREYTEAGRFHKE | ||||||
Compositional bias | 1972-1986 | Pro residues | ||||
Sequence: PPFLVPGPPPSQPTD | ||||||
Compositional bias | 2035-2066 | Polar residues | ||||
Sequence: NPSSSSVLPNPQKKSSTGLSPSPETGPLAAVT | ||||||
Compositional bias | 2094-2112 | Basic and acidic residues | ||||
Sequence: HSDPILPEQRPDVEEISSE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
NKQK01000014 EMBL· GenBank· DDBJ | PSS11095.1 EMBL· GenBank· DDBJ | Genomic DNA |