cytosolic purine 5'-nucleotidase isoform 5 [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| 5_nucleotid super family | cl17687 | 5' nucleotidase family; This family of eukaryotic proteins includes 5' nucleotidase enzymes, ... |
1-298 | 8.32e-159 | |||||
5' nucleotidase family; This family of eukaryotic proteins includes 5' nucleotidase enzymes, such as purine 5'-nucleotidase EC:3.1.3.5. The actual alignment was detected with superfamily member pfam05761: Pssm-ID: 473086 Cd Length: 445 Bit Score: 453.13 E-value: 8.32e-159
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| Name | Accession | Description | Interval | E-value | |||||
| 5_nucleotid | pfam05761 | 5' nucleotidase family; This family of eukaryotic proteins includes 5' nucleotidase enzymes, ... |
1-298 | 8.32e-159 | |||||
5' nucleotidase family; This family of eukaryotic proteins includes 5' nucleotidase enzymes, such as purine 5'-nucleotidase EC:3.1.3.5. Pssm-ID: 461733 Cd Length: 445 Bit Score: 453.13 E-value: 8.32e-159
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| HAD_cN-II | cd07522 | cytosolic 5'-nucleotidase II (cN-II) similar to human NT5DC1 (5'-nucleotidase ... |
1-272 | 2.92e-96 | |||||
cytosolic 5'-nucleotidase II (cN-II) similar to human NT5DC1 (5'-nucleotidase domain-containing protein 1) and NT5DC2; Cytosolic 5'-nucleotidase II (cN-II), also known as purine 5'-nucleotidase, IMP-GMP specific nucleotidase, or high Km 5prime-nucleotidase, catalyzes the dephosphorylation of 6-hydroxypurine nucleoside monophosphates. It is ubiquitously expressed and likely to play an important role in the regulation of purine nucleotide interconversions and in the regulation of IMP and GMP pools within the cell. It is also acts as a phosphotransferase, catalyzing the reverse reaction, the transfer of a phosphate from a monophosphate substrate to a nucleoside acceptor, to form a nucleoside monophosphate. The nucleoside acceptor is preferentially inosine and deoxyinosine, phosphate donors include any 6-hydroxypurine monophosphate substrate of the nucleotidase reaction. Both the dephosphorylation and phosphotransferase reactions are allosterically activated by adenine-based nucleotides and 2,3-bisphosphoglycerate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319824 Cd Length: 352 Bit Score: 290.33 E-value: 2.92e-96
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| HAD-IG-Ncltidse | TIGR02244 | HAD superfamily (subfamily IG) hydrolase, 5'-nucleotidase; This model includes a 5 ... |
1-201 | 2.73e-93 | |||||
HAD superfamily (subfamily IG) hydrolase, 5'-nucleotidase; This model includes a 5'-nucleotidase specific for purines (IMP and GMP). These enzymes are members of the Haloacid Dehalogenase (HAD) superfamily. HAD members are recognized by three short motifs {hhhhDxDx(T/V)}, {hhhh(T/S)}, and either {hhhh(D/E)(D/E)x(3-4)(G/N)} or {hhhh(G/N)(D/E)x(3-4)(D/E)} (where "h" stands for a hydrophobic residue). Crystal structures of many HAD enzymes has verified PSI-PRED predictions of secondary structural elements which show each of the "hhhh" sequences of the motifs as part of beta sheets. This subfamily of enzymes is part of "Subfamily I" of the HAD superfamily by virtue of a "cap" domain in between motifs 1 and 2. This subfamily's cap domain has a different predicted secondary structure than all other known HAD enzymes and thus has been designated "subfamily IG". This domain appears to consist of a mixed alpha/beta fold. A Pfam model (pfam05761) detects an identical range of sequences above the trusted cutoff, but does not model the N-terminal motif 1 region. A TIGRFAMs model (TIGR01993) represents a (putative) family of _pyrimidine_ 5'-nucleotidases which are also subfamily I HAD's, which should not be confused with the current model. Pssm-ID: 274052 Cd Length: 343 Bit Score: 282.67 E-value: 2.73e-93
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| Name | Accession | Description | Interval | E-value | |||||
| 5_nucleotid | pfam05761 | 5' nucleotidase family; This family of eukaryotic proteins includes 5' nucleotidase enzymes, ... |
1-298 | 8.32e-159 | |||||
5' nucleotidase family; This family of eukaryotic proteins includes 5' nucleotidase enzymes, such as purine 5'-nucleotidase EC:3.1.3.5. Pssm-ID: 461733 Cd Length: 445 Bit Score: 453.13 E-value: 8.32e-159
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| HAD_cN-II | cd07522 | cytosolic 5'-nucleotidase II (cN-II) similar to human NT5DC1 (5'-nucleotidase ... |
1-272 | 2.92e-96 | |||||
cytosolic 5'-nucleotidase II (cN-II) similar to human NT5DC1 (5'-nucleotidase domain-containing protein 1) and NT5DC2; Cytosolic 5'-nucleotidase II (cN-II), also known as purine 5'-nucleotidase, IMP-GMP specific nucleotidase, or high Km 5prime-nucleotidase, catalyzes the dephosphorylation of 6-hydroxypurine nucleoside monophosphates. It is ubiquitously expressed and likely to play an important role in the regulation of purine nucleotide interconversions and in the regulation of IMP and GMP pools within the cell. It is also acts as a phosphotransferase, catalyzing the reverse reaction, the transfer of a phosphate from a monophosphate substrate to a nucleoside acceptor, to form a nucleoside monophosphate. The nucleoside acceptor is preferentially inosine and deoxyinosine, phosphate donors include any 6-hydroxypurine monophosphate substrate of the nucleotidase reaction. Both the dephosphorylation and phosphotransferase reactions are allosterically activated by adenine-based nucleotides and 2,3-bisphosphoglycerate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319824 Cd Length: 352 Bit Score: 290.33 E-value: 2.92e-96
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| HAD-IG-Ncltidse | TIGR02244 | HAD superfamily (subfamily IG) hydrolase, 5'-nucleotidase; This model includes a 5 ... |
1-201 | 2.73e-93 | |||||
HAD superfamily (subfamily IG) hydrolase, 5'-nucleotidase; This model includes a 5'-nucleotidase specific for purines (IMP and GMP). These enzymes are members of the Haloacid Dehalogenase (HAD) superfamily. HAD members are recognized by three short motifs {hhhhDxDx(T/V)}, {hhhh(T/S)}, and either {hhhh(D/E)(D/E)x(3-4)(G/N)} or {hhhh(G/N)(D/E)x(3-4)(D/E)} (where "h" stands for a hydrophobic residue). Crystal structures of many HAD enzymes has verified PSI-PRED predictions of secondary structural elements which show each of the "hhhh" sequences of the motifs as part of beta sheets. This subfamily of enzymes is part of "Subfamily I" of the HAD superfamily by virtue of a "cap" domain in between motifs 1 and 2. This subfamily's cap domain has a different predicted secondary structure than all other known HAD enzymes and thus has been designated "subfamily IG". This domain appears to consist of a mixed alpha/beta fold. A Pfam model (pfam05761) detects an identical range of sequences above the trusted cutoff, but does not model the N-terminal motif 1 region. A TIGRFAMs model (TIGR01993) represents a (putative) family of _pyrimidine_ 5'-nucleotidases which are also subfamily I HAD's, which should not be confused with the current model. Pssm-ID: 274052 Cd Length: 343 Bit Score: 282.67 E-value: 2.73e-93
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| HAD_like | cd01427 | Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ... |
44-180 | 9.15e-03 | |||||
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319763 [Multi-domain] Cd Length: 106 Bit Score: 35.45 E-value: 9.15e-03
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