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RT106_ASPTN
ID   RT106_ASPTN             Reviewed;         468 AA.
AC   Q0CTS1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Histone chaperone rtt106;
GN   Name=rtt106; ORFNames=ATEG_02913;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histones H3 and H4 chaperone involved in the nucleosome
CC       formation and heterochromatin silencing. Required for the deposition of
CC       H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role
CC       in the transcriptional regulation of the cell-cycle dependent histone
CC       genes by creating a repressive structure at the core histone gene
CC       promoter (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with histones H3 and H4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RTT106 family. {ECO:0000305}.
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DR   EMBL; CH476597; EAU36187.1; -; Genomic_DNA.
DR   RefSeq; XP_001212091.1; XM_001212091.1.
DR   AlphaFoldDB; Q0CTS1; -.
DR   SMR; Q0CTS1; -.
DR   STRING; 341663.Q0CTS1; -.
DR   EnsemblFungi; EAU36187; EAU36187; ATEG_02913.
DR   GeneID; 4317477; -.
DR   VEuPathDB; FungiDB:ATEG_02913; -.
DR   eggNOG; ENOG502R9PE; Eukaryota.
DR   HOGENOM; CLU_033828_0_0_1; -.
DR   OMA; AMPEAHR; -.
DR   OrthoDB; 1283058at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR013719; DUF1747.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   Pfam; PF08512; Rtt106; 1.
DR   SMART; SM01287; Rtt106; 1.
PE   3: Inferred from homology;
KW   Chaperone; Chromosome; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..468
FT                   /note="Histone chaperone rtt106"
FT                   /id="PRO_0000320486"
FT   REGION          67..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..451
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   468 AA;  50696 MW;  47C2A4192EABD774 CRC64;
     MAFATINSSA IPPATPSSIP TIEHAFASEP SLRKRVYDAI GATPQYIPLF EDIARYTSSL
     LARNATSTAP PAEASADGPA AKKRKIQNGD VSGTPQSLGD LKADAELQFH MRDVSFAMPQ
     RKKLTLEVTA GGGFLRARNQ TSKEVEFGVP VEKIQHVLCL PVPEKNQRQF NFCVIPQNGD
     GINTPAGGEA APESIVWTVA DGPPKSEFSI NGQAVAGGAG GESAEKVVLR VLNDALTQTK
     VIRPDDREFV SAMPEAHRKG EKAYHVKAFR GSKEGYLFFL STGILFGFKK PLIFFAFENI
     DSVSYTSVLQ RTFNLNIMAR ATAGGEPQEF ELSMIDQADF SGIDAYIKTH GLQDASLAEE
     RRAKRYNING KTEEAAAAAN GDETAEEESE LQKAQRELED QEDEEEEDYD PGSDGDSDGS
     GSSSDDDDDD DDEHQDDEDD MDEDEDGEQD LVAAELGSQA ADIPEDQV
 
 
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