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fib

Gene
Fib
Protein
rRNA 2'-O-methyltransferase fibrillarin
Organism
Drosophila erecta
Length
345 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
34.709 kDa
Sequence
MGKPGFSPRGGGGGGGGGGGGFRGRGGGGGGGGGGGFGGGRGRGGGGDRGGRGGFGGGRGGGGRGGGGGGGRGGFGGRGGGGGRGGGGRGGGGRGGGGRGGGAGGFKGGKTVTIEPHRHEGVFIARGKEDALVTRNFVPGSEVYGEKRISVENNGEKIEYRVWNPFRSKLAAAVLGGVEQIHMPPGSKVLYLGAASGTTVSHVSDVVGPEGLVYAVEFSHRSGRDLINVAKKRTNIIPIIEDARHPHKYRMLVGMVDTIFADVAQPDQGRIVALNAQHFLKNGGHFVISIKASCIDSTAQPEAVFASEVKKMQADKLKPQEQLTLEPYERDHAVVVGVYRPPPKQ

Gene
Fib
Protein
rRNA 2'-O-methyltransferase fibrillarin
Organism
Drosophila melanogaster
Length
344 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
34.637 kDa
Sequence
MGKPGFSPRGGGGGGGGGGGGFRGRGGGGGGGGGGFGGGRGRGGGGDRGGRGGFGGGRGGGGRGGGGGGGRGAFGGRGGGGGRGGGGRGGGGRGGGGRGGGAGGFKGGKTVTIEPHRHEGVFIARGKEDALVTRNFVPGSEVYGEKRISVETNGEKIEYRVWNPFRSKLAAAVLGGVEQIHMPPGSKVLYLGAASGTTVSHVSDVVGPEGLVYAVEFSHRSGRDLINVAKKRTNIIPIIEDARHPHKYRMLVGMVDTIFADVAQPDQGRIVALNAQHFLKNGGHFVISIKASCIDSTAQPEAVFAAEVKKMQADKLKPQEQLTLEPYERDHAVVVGVYRPPPKQ

Gene
FIB
Protein
rRNA 2'-O-methyltransferase fibrillarin
Organism
Tetrahymena thermophila
Length
294 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
31.288 kDa
Sequence
MGKDFKSGGGNAGGKPFNKGPGGPGGRPFNKGPGGPGGPGGKFGGGRPGGPGGKFGAKGPRGPKTIIVKHRLEGVFICKGQQEALVTKNFFPGESVYNEKRMSVEENGEKIEYRVWNPYRSKIAAAVVGGISDIHIKPGSKVLYLGGASGTTVSHVADIVGPTGVVYAVEFSHRSGRDLVNMAKKRTNVVPIIGDARKPQEYRFLVGMVDVVFADVAQPDQARIMGMNCQYFLKNGGHFLISIKACCIDSTNEPAVVFAAEVQKLKEEGLKPEQQLTLEPYERDHAMVLGSYRA

Gene
fib
Protein
Fibrinogen-binding protein
Organism
Staphylococcus aureus (strain COL)
Length
165 amino acids
Function
Extracellular fibrinogen-binding protein that plays an important role in virulence. By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non-functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation. In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N-terminal.
Mass
18.765 kDa
Sequence
MKNKLIAKSLLTLAAIGITTTTIASTADASEGYGPREKKPVSINHNIVEYNDGTFKYQSRPKFNSTPKYIKFKHDYNILEFNDGTFEYGARPQFNKPAAKTDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLKQGLVK

Gene
fib
Protein
Fibrinogen-binding protein
Organism
Staphylococcus aureus (strain Newman)
Length
165 amino acids
Function
Extracellular fibrinogen-binding protein that plays an important role in virulence (PubMed:7934883, PubMed:8945578). By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non-functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation (PubMed:11418620). In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N-terminal (PubMed:24348255, PubMed:27112346).
Mass
18.765 kDa
Sequence
MKNKLIAKSLLTLAAIGITTTTIASTADASEGYGPREKKPVSINHNIVEYNDGTFKYQSRPKFNSTPKYIKFKHDYNILEFNDGTFEYGARPQFNKPAAKTDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLKQGLVK

Gene
fib
Protein
Fibrinogen-binding protein
Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Length
165 amino acids
Function
Extracellular fibrinogen-binding protein that plays an important role in virulence. By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non-functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation. In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N-terminal.
Mass
18.793 kDa
Sequence
MKNKLIAKSLLTIAAIGITTTTIASTADASEGYGPREKKPVSINHNIVEYNDGTFKYQSRPKFNSTPKYIKFKHDYNILEFNDGTFEYGARPQFNKPAAKTDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLKQGLVR

Gene
fib
Protein
Fibrinogen-binding protein
Organism
Staphylococcus aureus (strain N315)
Length
165 amino acids
Function
Extracellular fibrinogen-binding protein that plays an important role in virulence. By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non-functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation. In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N-terminal.
Mass
18.793 kDa
Sequence
MKNKLIAKSLLTIAAIGITTTTIASTADASEGYGPREKKPVSINHNIVEYNDGTFKYQSRPKFNSTPKYIKFKHDYNILEFNDGTFEYGARPQFNKPAAKTDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLKQGLVR

Gene
fib
Protein
Fibrinogen-binding protein
Organism
Staphylococcus aureus (strain MRSA252)
Length
165 amino acids
Function
Extracellular fibrinogen-binding protein that plays an important role in virulence. By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non-functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation. In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N-terminal.
Mass
18.835 kDa
Sequence
MKNKLIAKSLLAIAAIGITTTTIASTADASEGYGPREKKPVSINHNIVEYNDGTFKYQSRPKFNTTPKYIKFRHDYNIVEYNDGTFEYGARPQFNKPAAKTEATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYNVKKMILQERIDQVLKQGLVR

Gene
fib
Protein
Fibrinogen-binding protein
Organism
Staphylococcus aureus (strain MSSA476)
Length
165 amino acids
Function
Extracellular fibrinogen-binding protein that plays an important role in virulence. By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non-functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation. In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N-terminal.
Mass
18.765 kDa
Sequence
MKNKLIAKSLLTIAAIGITTTTIASTADASEGYGPREKKPVSINHNIVEYNDGTFKYQSRPKFNSTPKYIKFKHDYNILEFNDGTFEYGARPQFNKPAAKTDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLKQGLVK

Gene
fib
Protein
Fibrinogen-binding protein
Organism
Staphylococcus aureus
Length
165 amino acids
Function
Extracellular fibrinogen-binding protein that plays an important role in virulence (PubMed:7934883). By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non-functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation. In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N-terminal (By similarity).
Mass
18.793 kDa
Sequence
MKNKLIAKSLLTIAAIGITTTTIASTADASEGYGPREKKPVSINHNIVEYNDGTFKYQSRPKFNSTPKYIKFKHDYNILEFNDGTFEYGARPQFNKPAAKTDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLKQGLVR

Gene
fib
Protein
Fibrinogen-binding protein
Organism
Staphylococcus aureus (strain MW2)
Length
165 amino acids
Function
Extracellular fibrinogen-binding protein that plays an important role in virulence. By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non-functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation. In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N-terminal.
Mass
18.765 kDa
Sequence
MKNKLIAKSLLTIAAIGITTTTIASTADASEGYGPREKKPVSINHNIVEYNDGTFKYQSRPKFNSTPKYIKFKHDYNILEFNDGTFEYGARPQFNKPAAKTDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLKQGLVK

Gene
fib
Protein
Fibrinogen-binding protein
Organism
Staphylococcus aureus (strain COL)
Length
165 amino acids
Function
Extracellular fibrinogen-binding protein that plays an important role in virulence. By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non-functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation. In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N-terminal.
Mass
18.765 kDa
Sequence
MKNKLIAKSLLTLAAIGITTTTIASTADASEGYGPREKKPVSINHNIVEYNDGTFKYQSRPKFNSTPKYIKFKHDYNILEFNDGTFEYGARPQFNKPAAKTDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLKQGLVK

Gene
fib
Protein
Fibrinogen-binding protein
Organism
Staphylococcus aureus (strain Newman)
Length
165 amino acids
Function
Extracellular fibrinogen-binding protein that plays an important role in virulence (PubMed:7934883, PubMed:8945578). By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non-functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation (PubMed:11418620). In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N-terminal (PubMed:24348255, PubMed:27112346).
Mass
18.765 kDa
Sequence
MKNKLIAKSLLTLAAIGITTTTIASTADASEGYGPREKKPVSINHNIVEYNDGTFKYQSRPKFNSTPKYIKFKHDYNILEFNDGTFEYGARPQFNKPAAKTDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLKQGLVK

Gene
fib
Protein
Fibrinogen-binding protein
Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Length
165 amino acids
Function
Extracellular fibrinogen-binding protein that plays an important role in virulence. By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non-functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation. In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N-terminal.
Mass
18.793 kDa
Sequence
MKNKLIAKSLLTIAAIGITTTTIASTADASEGYGPREKKPVSINHNIVEYNDGTFKYQSRPKFNSTPKYIKFKHDYNILEFNDGTFEYGARPQFNKPAAKTDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLKQGLVR

Gene
fib
Protein
Fibrinogen-binding protein
Organism
Staphylococcus aureus (strain N315)
Length
165 amino acids
Function
Extracellular fibrinogen-binding protein that plays an important role in virulence. By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non-functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation. In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N-terminal.
Mass
18.793 kDa
Sequence
MKNKLIAKSLLTIAAIGITTTTIASTADASEGYGPREKKPVSINHNIVEYNDGTFKYQSRPKFNSTPKYIKFKHDYNILEFNDGTFEYGARPQFNKPAAKTDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLKQGLVR

Gene
fib
Protein
Fibrinogen-binding protein
Organism
Staphylococcus aureus (strain MRSA252)
Length
165 amino acids
Function
Extracellular fibrinogen-binding protein that plays an important role in virulence. By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non-functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation. In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N-terminal.
Mass
18.835 kDa
Sequence
MKNKLIAKSLLAIAAIGITTTTIASTADASEGYGPREKKPVSINHNIVEYNDGTFKYQSRPKFNTTPKYIKFRHDYNIVEYNDGTFEYGARPQFNKPAAKTEATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYNVKKMILQERIDQVLKQGLVR

Gene
fib
Protein
Fibrinogen-binding protein
Organism
Staphylococcus aureus (strain MSSA476)
Length
165 amino acids
Function
Extracellular fibrinogen-binding protein that plays an important role in virulence. By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non-functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation. In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N-terminal.
Mass
18.765 kDa
Sequence
MKNKLIAKSLLTIAAIGITTTTIASTADASEGYGPREKKPVSINHNIVEYNDGTFKYQSRPKFNSTPKYIKFKHDYNILEFNDGTFEYGARPQFNKPAAKTDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLKQGLVK

Gene
fib
Protein
Fibrinogen-binding protein
Organism
Staphylococcus aureus
Length
165 amino acids
Function
Extracellular fibrinogen-binding protein that plays an important role in virulence (PubMed:7934883). By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non-functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation. In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N-terminal (By similarity).
Mass
18.793 kDa
Sequence
MKNKLIAKSLLTIAAIGITTTTIASTADASEGYGPREKKPVSINHNIVEYNDGTFKYQSRPKFNSTPKYIKFKHDYNILEFNDGTFEYGARPQFNKPAAKTDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLKQGLVR

Gene
fib
Protein
Fibrinogen-binding protein
Organism
Staphylococcus aureus (strain MW2)
Length
165 amino acids
Function
Extracellular fibrinogen-binding protein that plays an important role in virulence. By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non-functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation. In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N-terminal.
Mass
18.765 kDa
Sequence
MKNKLIAKSLLTIAAIGITTTTIASTADASEGYGPREKKPVSINHNIVEYNDGTFKYQSRPKFNSTPKYIKFKHDYNILEFNDGTFEYGARPQFNKPAAKTDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLKQGLVK