Rrp8

Ribosomal RNA-processing protein 8

457 amino acids

Essential component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. In the complex, RRP8 binds to H3K9me2 and probably acts as a methyltransferase. Its substrates are however unknown (By similarity).

Belongs to the methyltransferase superfamily. RRP8 family.

51.066 kDa

MFEEPEWVEAAPAIVGLGAATAQVRPATAPPVKGRKRRHLLATLRALEAASLSQQTPSLPGSDSEEEEEVGRKKRHLQRPSLASVSKEVGKKRKGKCQKQAPSISDSEGKEIRRKCHRQAPPLGGVSAGEEKGKRKCQEYSSLHLTQPLDSVDQTVHNSRTSTATIDPSKPSPESMSPNSSHTLSRKQWRNRQKNKRRHKNKFRPLQTPEQAPPKASIEETEVPPVPKSDSQESRAGALRARMTQRLDGARFRYLNEQLYSGPSSAARRLFQEDPEAFLLYHRGFQRQVKKWPLHPVDRIAKDLRQKPASLVVADFGCGDCRLASSVRNPVHCFDLASLDPRVTVCDMAQVPLEDESVDVAVFCLSLMGTNIRDFLEEANRVLKTGGLLKVAEVSSRFEDIRTFLGAVTKLGFKIIYKDLTNSHFFLFDFEKTGPPRVGPKAQLSGLKLQPCLYKRR

Rrp8

Ribosomal RNA-processing protein 8

457 amino acids

Essential component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. In the complex, RRP8 binds to H3K9me2 and probably acts as a methyltransferase. Its substrates are however unknown (By similarity).

Belongs to the methyltransferase superfamily. RRP8 family.

51.216 kDa

MFEEPEWVEAAPAIVGLRPVTTQVQAATAPPVKGRKRRHLLATLRALEAASLSQQCPSLPGSDSEEEEEVGRKKRHFQRSSLANVSKEVGKKRKGKCQKQAPFISDSEGKEVERTCHRQAPPLGGISAGEEKGKRKCQEYSYLHPTQSLNSVDQTVHNSRTSTATLDPPKSSRESASPNSSHTLSRKQWRNRQKNKRRHKNKFRPLETQDQVPLKASIEETEVPPAPKSDSQETRAGALRARMTQRLDGARFRYLNEQLYSGPSSAAQCLFQEDPEAFLLYHRGFQRQVKKWPLHPVDRIAKDLRQKPASLVVADFGCGDCRLASSVRNPVHCFDLAALDPRVTVCDMAQVPLEDESVDVAVFCLSLMGTNIRDFLEEANRVLKPGGLLKVAEVSSRFEDIRTFLGAVTKLGFKVIYKDLTNSHFFLFDFEKTGPPRVGPKAQLSGLKLQPCLYKHR

RRP8

Ribosomal RNA-processing protein 8

456 amino acids

Essential component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. In the complex, RRP8 binds to H3K9me2 and probably acts as a methyltransferase. Its substrates are however unknown.

Belongs to the methyltransferase superfamily. RRP8 family.

50.715 kDa

MFEEPEWAEAAPVAAGLGPVISRPPPAASSQNKGSKRRQLLATLRALEAASLSQHPPSLCISDSEEEEEERKKKCPKKASFASASAEVGKKGKKKCQKQGPPCSDSEEEVERKKKCHKQALVGSDSAEDEKRKRKCQKHAPINSAQHLDNVDQTGPKAWKGSTTNDPPKQSPGSTSPKPPHTLSRKQWRNRQKNKRRCKNKFQPPQVPDQAPAEAPTEKTEVSPVPRTDSHEARAGALRARMAQRLDGARFRYLNEQLYSGPSSAAQRLFQEDPEAFLLYHRGFQSQVKKWPLQPVDRIARDLRQRPASLVVADFGCGDCRLASSIRNPVHCFDLASLDPRVTVCDMAQVPLEDESVDVAVFCLSLMGTNIRDFLEEANRVLKPGGLLKVAEVSSRFEDVRTFLRAVTKLGFKIVSKDLTNSHFFLFDFQKTGPPLVGPKAQLSGLQLQPCLYKRR

RRP8

25S rRNA (adenine(645)-N(1))-methyltransferase

392 amino acids

S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of adenine 645 in 25S rRNA. Required both for ribosomal 40S and 60S subunits biogenesis. Required for efficient pre-rRNA cleavage at site A2. Also involved in telomere length regulation and maintenance.

Belongs to the methyltransferase superfamily. RRP8 family.

45.985 kDa

MALFNVEGWSIKTKTVAFDNKTNKSSKDKKKNNRKNGKLTREQKLKEETEAELKEQVEDIPSEGSVAKDIPKKNQEKSDQNETSKKRKHDEEAPLMQVKENIEKPTKKQLTPLQQKMMAKLTGSRFRWINEQLYTISSDEALKLIKEQPQLFDEYHDGFRSQVQAWPENPVDVFVDQIRYRCMKPVNAPGGLPGLKDSKEIVIADMGCGEAQLALEINNFFKNYNKKAKKYLKRRHKVHSFDLKKANERITVADIRNVPLPDESCTIVVFCLALMGTNFLDFIKEAYRILAPRGELWIAEIKSRFSDGKGNEFVDALKLMGFFHKKTFDENKMFTRFEFFKPPAEIIEERRQKLERRQKFIEVETEKEELEKKRRKIAEGKWLLKPCIYKRR

rrp8

Ribosomal RNA-processing protein 8

390 amino acids

Probable methyltransferase required to silence rDNA.

Belongs to the methyltransferase superfamily. RRP8 family.

45.193 kDa

MTNTKKSKQKNTVGNKVKKTNTNKNNNNNNNNNNKNKQNKINNKNNKNNKNNDSNNKNNNTNNKNNINIKNKNLKKVENNKSLKVISSNKNKNILNNLKKEEKVNSNDILIQQQQNREKEDITNEDDDEKYNLWNPKPTSSVSVSSSKSSKSLKTTDLQNEMSEKLKGSRFRWLNETLYTTHSKEAFKEFSEDRSLFDQYHSGFKSQVESWPINPLDLIIDDLSSIKQRKRIADLGCGEAKLAERLQHKHTIQSFDLVAVNERVTACDISNLPLKNESIDIAVFCLSLMGTNFIDFIIEAERVLVKGGLLKIAEIESRITDINAFTNEIQQHGFNLIKKNEQNQYFTLFEFSKLQKKDQQFMRSLKQYQKLKKQQATNEPVLKPCLYKKR

rrp8

25S rRNA (adenine(645)-N(1))-methyltransferase

318 amino acids

S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of adenine in helix 25.1 in 25S rRNA. Required both for ribosomal 40S and 60S subunits biogenesis. Required for efficient pre-rRNA cleavage at site A2 (By similarity).

Belongs to the methyltransferase superfamily. RRP8 family.

36.329 kDa

MFKVDWDLGPVSKSASDQTKESRKEKKRKKGERKNVGDKGEKLNEKVLKKAKSVTTNNSLKSEIKKEKSVPSIKEKNKGDAKHTKLTSLQQKMKDKLDGANFRWINEQLYTTESDKAVQMFKENPDLFDIYHAGFRYQVEGWPENPVDIFIQHLKIRFEHSNAKKKNNIVIADLGCGEAKIASTFRKSRSLQVHSFDLVAPNEHVVACDIANVPMADETVDIAVFCLSLMGTNWQSFLKEAYRILKVGGLLWVAEIKSRFSDKSGEVFAKELPKLGFETKSIQLQNKMFTLFEFKKVPVHGKCEELPPILSACIYKRR