PAPS

Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase

338 amino acids

Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase VP55 that creates mRNA's poly(A) tail. In the presence of VP39, VP55 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Poxvirus/kinetoplastid 2'-O-MTase family.

39.722 kDa

MEPVSMDKPFMYFDEIDDELEYEPESVNETPKKLPHQGQLKLLLGELFFLSKLQRHGILDGSTIVYIGSAPGTHIKYLRDHFMSMGLVIKWMLIDGRTHDPILEGLRDVILITKFVDEAYIRQLKKQLYPSRVILISDVRSKRGQKEPTTQDLLSNYSLQNIMVSVLKPAASSLKWRCPFPDQWIKDFYVPHGNEMLQPFAPSYSAEMRLLSIYSGTPIRLKCITQQDSSKYEKKMYYLNKIIRNRIIINFDYSNQEYDFFHMYHMLKTVYSNKSFTSNKSKVLHFHQSIFRFLKIPITNTEKIHHEPTQRKVPSKNTMLKSRNTKKSVRGNKQGRRT

PAPS

Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase

338 amino acids

Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase VP55 that creates mRNA's poly(A) tail. In the presence of VP39, VP55 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Poxvirus/kinetoplastid 2'-O-MTase family.

39.722 kDa

MEPVSMDKPFMYFDEIDDELEYEPESVNETPKKLPHQGQLKLLLGELFFLSKLQRHGILDGSTIVYIGSAPGTHIKYLRDHFMSMGLVIKWMLIDGRTHDPILEGLRDVILITKFVDEAYIRQLKKQLYPSRVILISDVRSKRGQKEPTTQDLLSNYSLQNIMVSVLKPAASSLKWRCPFPDQWIKDFYVPHGNEMLQPFAPSYSAEMRLLSIYSGTPIRLKCITQQDSSKYEKKMYYLNKIIRNRIIINFDYSNQEYDFFHMYHMLKTVYSNKSFTSNKSKVLHFHQSIFRFLKIPITNTEKIHHEPTQRKVPSKNTMLKSRNTKKSVRGNKQGRRT

PAPS

Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase

333 amino acids

Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase VP55 that creates mRNA's poly(A) tail. In the presence of VP39, VP55 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Poxvirus/kinetoplastid 2'-O-MTase family.

38.888 kDa

MDVVSLDKPFMYFEEIDNELDYEPESANEVAKKLPYQGQLKLLLGELFFLSKLQRHGILDGATVVYIGSAPGTHIRYLRDHFYNLGVIIKWMLIDGRHHDPILNGLRDVTLVTRFVDEEYLRSIKKQLHPSKIILISDVRSKRGGNEPSTADLLSNYALQNVMISILNPVASSLKWRCPFPDQWIKDFYIPHGNKMLQPFAPSYSAEMRLLSIYTGENMRLTRVTKSDAVNYEKKMYYLNKIVRNKVVVNFDYPNQEYDYFHMYFMLRTVYCNKTFPTTKAKVLFLQQSIFRFLNIPTTSTEKVSHEPIQRKISSKNSMSKNRNSKRSVRSNK

PAPS

Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase

333 amino acids

Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase VP55 that creates mRNA's poly(A) tail. In the presence of VP39, VP55 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Poxvirus/kinetoplastid 2'-O-MTase family.

38.918 kDa

MDVVSLDKPFMYFEEIDNELDYEPESANEVAKKLPYQGQLKLLLGELFFLSKLQRHGILDGATVVYIGSAPGTHIRYLRDHFYNLGMIIKWMLIDGRHHDPILNGLRDVTLVTRFVDEEYLRSIKKQLHPSKIILISDVRSKRGGNEPSTADLLSNYALQNVMISILNPVASSLKWRCPFPDQWIKDFYIPHGNKMLQPFAPSYSAEMRLLSIYTGENMRLTRVTKSDVVNYEKKMYYLNKIVRNKVVVNFDYPNQEYDYFHMYFMLRTVYCNKTFPTTKAKVLFLQQSIFRFLNIPTTSTEKVSHEPIQRKISSKNSMSKNRNSKRSVRGNK

PAPS

Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase

333 amino acids

Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase VP55 that creates mRNA's poly(A) tail. In the presence of VP39, VP55 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Poxvirus/kinetoplastid 2'-O-MTase family.

38.888 kDa

MDVVSLDKPFMYFEEIDNELDYEPESANEVAKKLPYQGQLKLLLGELFFLSKLQRHGILDGATVVYIGSAPGTHIRYLRDHFYNLGVIIKWMLIDGRHHDPILNGLRDVTLVTRFVDEEYLRSIKKQLHPSKIILISDVRSKRGGNEPSTADLLSNYALQNVMISILNPVASSLKWRCPFPDQWIKDFYIPHGNKMLQPFAPSYSAEMRLLSIYTGENMRLTRVTKSDAVNYEKKMYYLNKIVRNKVVVNFDYPNQEYDYFHMYFMLRTVYCNKTFPTTKAKVLFLQQSIFRFLNIPTTSTEKVSHEPIQRKISSKNSMSKNRNSKRSVRSNK

PAPS

Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase

333 amino acids

Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase VP55 that creates mRNA's poly(A) tail. In the presence of VP39, VP55 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Poxvirus/kinetoplastid 2'-O-MTase family.

38.868 kDa

MDVVSLDKPFMYFEEIDNELDYEPESANEVAKKLPYQGQLKLLLGELFFLSKLQRHGILDGATVVYIGSAPGTHIRYLRDHFYNLGVIIKWMLIDGRHHDPILNGLRDVTLVTRFVDEEYLRSIKKQLHPSKIILISDVRSKRGGNEPSTEDLLSNYALQNVMISILNPVASSLKWRCPFPDQWIKDFYIPHGNKMSQPFAPSYSAEMRLLSIYTGENMRLTRVTKSDAVNYEKKMYYLNKIVRNKVVVNFDYPNQEYDYFHMYFMLRTVYCNKTFPTTKAKVLFLQQSIFRFLNIPTTSTEKVSHEPIQCKVSSKDSVYKNRNSKRSVRGNK

PAPS

Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase

308 amino acids

Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase VP55 that creates mRNA's poly(A) tail. In the presence of VP39, VP55 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Poxvirus/kinetoplastid 2'-O-MTase family.

36.655 kDa

MHEGHQESFKELEMTKPYMFFNELVGEEDYNKELENSNTKFQGQGQLKLLLGELYFLNTLIKNKTLCSDTVIVYIGSAPGSHINFLYHYMDDLKIDLKWILIDGRDHDRSLESLKNVSIIHRFVDEQYLFKLRNMIRKNHKIVLISDIRSLRGKEPTSEDLLHDYALQNQMVSILKPIASSLKWRCPFPDQWIRDFYIPCGDEFLQPFAPPFSAEMRLLSCYSRAPIRLIRIDKNAAIEYEKKMFYLNTKIRPKIVLDFDYPNQKYDYFYMFYILKDIVLPTYKEFSTYKQKVIFLQEAIFNALNIKP

PAPS

Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase

220 amino acids

Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase VP55 that creates mRNA's poly(A) tail. In the presence of VP39, VP55 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Poxvirus/kinetoplastid 2'-O-MTase family.

25.378 kDa

single

MEAVSMDKPFMYFDEIDNELEYDPKTSEEKPKKLPYQGQLKLLLCELFFLSKLQRHGILDGCTIVYVGSAPGTHIKYLRDHFLSMGLVIRWILIDGRQHDTILNGLRDVTLITKFVDESYIRVLKKQLYQSKIVLISDVRSKRGGNEPSTFDLLSNYALQNIMVSILKPAASSLKWRCPFPDQWVKDFYIPHGNEMLQPFAPKYSAEIVNNIYSGNPIKL

PAPS

Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase

69 amino acids

Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase VP55 that creates mRNA's poly(A) tail. In the presence of VP39, VP55 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Poxvirus/kinetoplastid 2'-O-MTase family.

8.069 kDa

single

MEPLSIDKPFMYFDEINNELEYDPDSANEKHKKFPYQGQLKLLLCELFFLSKLQRHGILDGSTIVYIGS