※ dbPPT Protein Information
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UniProt Accession | |||||||||||||||||||||||||||||||
Theoretical PI | 5.52 | ||||||||||||||||||||||||||||||
Molecular Weight | 71334.04 | ||||||||||||||||||||||||||||||
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Protein Name | FACT complex subunit SSRP1-A; Early drought-induced protein R1G1A; Facilitates chromatin transcription complex subunit SSRP1-A; Recombination signal sequence recognition protein 1-A | ||||||||||||||||||||||||||||||
Gene Name | SSRP1-A; R1G1A; Os01g0184900; LOC_Os01g08970; P0510F03.10 | ||||||||||||||||||||||||||||||
Created Date | 2006-07-11 | ||||||||||||||||||||||||||||||
Organism | Oryza sativa subsp. japonica(Rice) | ||||||||||||||||||||||||||||||
NCBI Taxa ID | 39947 | ||||||||||||||||||||||||||||||
Phosphorylation Sites |
Functional Description Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. Binds specifically to double-stranded DNA (By similarity). Sequence Annotation chain 1 641 FACT complex subunit SSRP1-A DNA-binding region 556 624 HMG box compositionally biased region 458 507 Asp-rich (acidic) compositionally biased region 515 551 Lys-rich (basic) Keyword Chromosome,Complete proteome,DNA damage,DNA repair,DNA replication,DNA-binding,Nucleus,Reference proteome,Transcription,Transcription regulation Sequence Source UniProt Protein Sequence MTDGHLFNNI LLGGRAGSNP GQFKVYSGGL AWKRQGGGKT IEIEKSDLTS VTWMKVPRAY 60 QLGVRTKDGL FYKFIGFREQ DVSSLTNFMQ KNMGLSPDEK QLSVSGQNWG GIDINGNMLT 120 FMVGSKQAFE VSLADVSQTQ MQGKTDVLLE FHVDDTTGGN EKDSLMDLSF HVPTSNTQFL 180 GDENRTAAQV LWETIMGVAD VDSSEEAVVT FEGIAILTPR GRYSVELHLS FLRLQGQAND 240 FKIQYSSIVR LFLLPKSNNP HTFVVVTLDP PIRKGQTLYP HIVIQFETEA VVERNLALTK 300 EVLAEKYKDR LEESYKGLIH EVFTKVLRGL SGAKVTRPGS FRSCQDGYAV KSSLKAEDGL 360 LYPLEKGFFF LPKPPTLILH EEIEFVEFER HGAGGASISS HYFDLLVKLK NDQEHLFRNI 420 QRSEYHNLFN FINGKHLKIM NLGDGQGATG GVTAVLRDTD DDAVDPHLER IKNQAGDEES 480 DEEDEDFVAD KDDSGSPTDD SGGEDSDASE SGGEKEKLSK KEASSSKPPV KRKPKGRDEE 540 GSDKRKPKKK KDPNAPKRAM TPFMYFSMAE RGNMKNNNPD LPTTEIAKKL GEMWQKMTGE 600 EKQPYIQQSQ VDKKRYEKES AVYRGAAAMD VDSGSGGNES D 641 Gene Ontology GO:0035101; C: FACT complex; IEA: EnsemblPlants/Gramene GO:0005719; C: nuclear euchromatin; IEA: EnsemblPlants/Gramene GO:0003677; F: DNA binding; IEA: UniProtKB-KW GO:0006281; P: DNA repair; IEA: UniProtKB-KW GO:0006260; P: DNA replication; IEA: UniProtKB-KW GO:0006355; P: regulation of transcription, DNA-templated; IEA: UniProtKB-KW GO:0006351; P: transcription, DNA-templated; IEA: UniProtKB-KW GO:0010228; P: vegetative to reproductive phase transition of meristem; IEA: EnsemblPlants/Gramene Interpro Pfam SMART SMART; SM00398; HMG PROSITE PS50118; HMG_BOX_2 PRINTS PR00887; SSRCOGNITION |