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Protein

Histone chaperone rtt106

Gene

rtt106

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Histones H3 and H4 chaperone involved in the nucleosome formation and heterochromatin silencing. Required for the deposition of H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role in the transcriptional regulation of the cell-cycle dependent histone genes by creating a repressive structure at the core histone gene promoter (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone chaperone rtt106
Gene namesi
Name:rtt106
ORF Names:An18g06020
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706 Componenti: Chromosome 8L

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Histone chaperone rtt106PRO_0000320484Add
BLAST

Interactioni

Subunit structurei

Interacts with histones H3 and H4.By similarity

Protein-protein interaction databases

STRINGi5061.CADANGAP00013971.

Structurei

3D structure databases

ProteinModelPortaliA2RBA1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RTT106 family.Curated

Phylogenomic databases

eggNOGiNOG78439.
HOGENOMiHOG000048523.
OrthoDBiEOG7TBCC0.

Family and domain databases

InterProiIPR013719. DUF1747.
[Graphical view]
PfamiPF08512. Rtt106. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2RBA1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFATINSSV PSSIPAIEDA FAAEPALKKR VYDAIAHTPQ HGLLFEDIAK
60 70 80 90 100
YTSSLLARTA TAPVRPVEVV SDGPAMKKRK LQNGNATSAQ SSGDLKSDTS
110 120 130 140 150
LQFYMQDVSF AVPQRKKLTL EVTAGFLRAR NQTSKEVEFG VPLDNIQHVL
160 170 180 190 200
CLPVPEKNQR QFNFCIIPQY ADGVNSPPEG VAAPDAIVWT VNDGPPKAAF
210 220 230 240 250
SGNGQQLGTD NEETADKLVQ RILNDSLPRT KVVRPDEREF VSAMPEAHRK
260 270 280 290 300
GEKAFHVKAF RGSKEGYLFL LSTGILFGFK KPLVFFAFEN VDSISYTSVL
310 320 330 340 350
QRTFNLNVVA RPTSSEETQE FEFSMIDQAD FSGIDGYIKK HGLQDASLAE
360 370 380 390 400
ARRAKRYNVN GAKGEDEAAA NEEGAVEEES ELQKAQRELE DQEDEDEEDY
410 420 430 440 450
DPGSDSDSDG SGSSSEEDDD DDEEDDEGDM EEDDEEGDRN LVAEELGSEA

EDVPAEEL
Length:458
Mass (Da):50,310
Last modified:March 6, 2007 - v1
Checksum:i053AEFE3FBD85B59
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270411 Genomic DNA. Translation: CAK43325.1.
RefSeqiXP_001399053.1. XM_001399016.1.

Genome annotation databases

EnsemblFungiiCADANGAT00014240; CADANGAP00013971; CADANGAG00014240.
GeneIDi4990168.
KEGGiang:ANI_1_806164.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270411 Genomic DNA. Translation: CAK43325.1.
RefSeqiXP_001399053.1. XM_001399016.1.

3D structure databases

ProteinModelPortaliA2RBA1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00013971.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANGAT00014240; CADANGAP00013971; CADANGAG00014240.
GeneIDi4990168.
KEGGiang:ANI_1_806164.

Phylogenomic databases

eggNOGiNOG78439.
HOGENOMiHOG000048523.
OrthoDBiEOG7TBCC0.

Family and domain databases

InterProiIPR013719. DUF1747.
[Graphical view]
PfamiPF08512. Rtt106. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiRT106_ASPNC
AccessioniPrimary (citable) accession number: A2RBA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 6, 2007
Last modified: May 27, 2015
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.