dual specificity phosphatase 11 (RNA/RNP complex 1-interacting), isoform CRA_b [Rattus norvegicus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| PTP_DSP_cys super family | cl28904 | cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ... |
1-29 | 4.85e-13 | ||
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases. The actual alignment was detected with superfamily member cd17665: Pssm-ID: 475123 Cd Length: 169 Bit Score: 63.06 E-value: 4.85e-13
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| Name | Accession | Description | Interval | E-value | ||
| DSP_DUSP11 | cd17665 | dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ... |
1-29 | 4.85e-13 | ||
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar proteins; dual specificity protein phosphatase 11 (DUSP11), also known as RNA/RNP complex-1-interacting phosphatase or phosphatase that interacts with RNA/RNP complex 1 (PIR1), has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity. It has activity for short RNAs but is less active toward mononucleotide triphosphates, suggesting that its primary function in vivo is to dephosphorylate RNA 5'-ends. It may play a role in nuclear mRNA metabolism. Also included in this subfamily is baculovirus RNA 5'-triphosphatase for Autographa californica nuclear polyhedrosis virus. Pssm-ID: 350503 Cd Length: 169 Bit Score: 63.06 E-value: 4.85e-13
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| Name | Accession | Description | Interval | E-value | ||
| DSP_DUSP11 | cd17665 | dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ... |
1-29 | 4.85e-13 | ||
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar proteins; dual specificity protein phosphatase 11 (DUSP11), also known as RNA/RNP complex-1-interacting phosphatase or phosphatase that interacts with RNA/RNP complex 1 (PIR1), has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity. It has activity for short RNAs but is less active toward mononucleotide triphosphates, suggesting that its primary function in vivo is to dephosphorylate RNA 5'-ends. It may play a role in nuclear mRNA metabolism. Also included in this subfamily is baculovirus RNA 5'-triphosphatase for Autographa californica nuclear polyhedrosis virus. Pssm-ID: 350503 Cd Length: 169 Bit Score: 63.06 E-value: 4.85e-13
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| RNA_5'-triphosphatase | cd14502 | RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ... |
1-29 | 1.06e-03 | ||
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes baculovirus RNA 5'-triphosphatase, dual specificity protein phosphatase 11 (DUSP11), and the RNA triphosphatase domains of metazoan and plant mRNA capping enzymes. RNA/polynucleotide 5'-triphosphatase (EC 3.1.3.33) catalyzes the removal of the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end. mRNA capping enzyme is a bifunctional enzyme that catalyzes the first two steps of cap formation. DUSP11 has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity. Pssm-ID: 350352 [Multi-domain] Cd Length: 167 Bit Score: 37.64 E-value: 1.06e-03
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