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fbl

Gene
fbl
Protein
rRNA 2'-O-methyltransferase fibrillarin
Organism
Dictyostelium discoideum
Length
334 amino acids
Function
S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ105me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (By similarity).
Similarity
Belongs to the methyltransferase superfamily. Fibrillarin family.
Mass
34.853 kDa
Sequence
MEGRGGSRGGAMARGGGRGGFGGGRGGFGGGDRGGRGGGRGGFGGGDRGGRGGFGGGRGGRGGFGGGDRGGRGGARGGRGGARGGKPAAGGKPGAKVIVEKHPRHEGVFIVRGKEESLATLNSVPGESVYGEKRVSVGEGEDKKEYRIWNPFRSKIAAGLHRGVDEIHIKPGSKVLYIGAASGTTISHVSDIVGPTGVVYGIELSHRPGRDLIGMAKKRTNVIPIIEDARHPQKYRMLIGMVDVVFADVAQPNQAQIVAQNSAYFLKNEGHFIISIKASCIDSTAPTEVVVQNEITKLKKEKLRPQHLLKTLDPYERNHSLVIGVYRKFGSSEK

Gene
Fbl
Protein
rRNA 2'-O-methyltransferase fibrillarin
Organism
Mus musculus
Length
327 amino acids
Function
S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ104me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (By similarity).
Similarity
Belongs to the methyltransferase superfamily. Fibrillarin family.
Mass
34.307 kDa
Sequence
MKPGFSPRGGGFGGRGGFGDRGGRGGGRGGRGGFGGGRGGFGGGGRGRGGGGGGFRGRGGGGGRGGGFQSGGNRGRGGGRGGKRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGEKRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDIVGPDGLVYAVEFSHRSGRDLINLAKKRTNIIPVIEDARHPHKYRMLIAMVDVIFADVAQPDQTRIVALNAHTFLRNGGHFVISIKANCIDSTASAEAVFASEVKKMQQENMKPQEQLTLEPYERDHAVVVGVYRPPPKVKN

Gene
Fbl
Protein
rRNA 2'-O-methyltransferase fibrillarin
Organism
Rattus norvegicus
Length
327 amino acids
Function
S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ104me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (By similarity).
Similarity
Belongs to the methyltransferase superfamily. Fibrillarin family.
Mass
34.222 kDa
Sequence
MKPGFSPRGGGFGGRGGFGDRGGRGGGRGGRGGFGGGRGGFGGGGRGRGGGGGGFRGRGGGGGRGGGFQSGGGRGRGGGRGGKRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGEKRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDIVGPDGLVYAVEFSHRSGRDLINLAKKRTNIIPVIEDARHPHKYRMLIAMVDVIFADVAQPDQTRIVALNAHTFLRNGGHFVISIKANCIDSTASAEAVFASEVKKMQQENMKPQEQLTLEPYERDHAVVVGVYRPPPKAKN

Gene
fbl
Protein
rRNA 2'-O-methyltransferase fibrillarin
Organism
Xenopus laevis
Length
323 amino acids
Function
S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ104me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (By similarity).
Similarity
Belongs to the methyltransferase superfamily. Fibrillarin family.
Mass
34.332 kDa
Sequence
MRPGFSPRGGRGGFGDRGGFGGRGGFGDRGGFRGGSRGGFGGRGRGGDRGGRGGFRGGFSSPGRGGPRGGGRGGFGGGRGGFGAGRKVIVEPHRHEGIFICRGKEDALVTKNLVPGESVYGEKRISVEDGEVKTEYRAWNPFRSKIAAAILGGVDQIHIKPGVKVLYLGAASGTTVSHVSDVVGPEGLVYAVEFSHRSGRDLINVAKKRTNIIPVIEDARHPHKYRILVGMVDVVFADVAQPDQTRIVALNAHNFLKNGGHFVISIKANCIDSTAAPEAVFAAEVKKMQQENMKPQEQLTLEPYERDHAVVVGIYRPPPKQKK

Gene
FBL
Protein
rRNA 2'-O-methyltransferase fibrillarin
Organism
Homo sapiens
Length
321 amino acids
Function
S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ104me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (PubMed:24352239).
Similarity
Belongs to the methyltransferase superfamily. Fibrillarin family.
Mass
33.784 kDa
Sequence
MKPGFSPRGGGFGGRGGFGDRGGRGGRGGFGGGRGRGGGFRGRGRGGGGGGGGGGGGGRGGGGFHSGGNRGRGRGGKRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGEKRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDIVGPDGLVYAVEFSHRSGRDLINLAKKRTNIIPVIEDARHPHKYRMLIAMVDVIFADVAQPDQTRIVALNAHTFLRNGGHFVISIKANCIDSTASAEAVFASEVKKMQQENMKPQEQLTLEPYERDHAVVVGVYRPPPKVKN