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Conserved domains on  [gi|568965461|ref|XP_006512827|]
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5'-nucleotidase domain-containing protein 1 isoform X1 [Mus musculus]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 7-187 4.05e-50

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member cd07522:

Pssm-ID: 473868  Cd Length: 352  Bit Score: 165.52  E-value: 4.05e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965461   7 LGACDVVGFDLDHTLCRYNLPESARLIYNSFAQFLVKEKGYDEGLLTLTPeDWDFCCKGLALDLEDGTFIKLAADGTVLR 86
Cdd:cd07522    8 LEKIKVFGFDMDYTLARYNSPELESLIYDLAKERLVEEKGYPEELLKFDY-DPNFPVRGLVFDKEKGNLLKLDAYGQILR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965461  87 ASHGTKMMTPEALTEAFGKKewrhcvsdkrctsdkpgVSDIPCCSGKCYFYDNYFDLPGALLCARVVDSLTKQNRG--QK 164
Cdd:cd07522   87 AYHGTRPLSDEEVREIYGSN-----------------NTGVRDDESRYYFLNTLFSLPEACLLAQLVDYFDNNPLEsdMS 149

                        170       180
                 ....*....|....*....|...
gi 568965461 165 TFDFWKDVVAGIQHNFKMSAFKE 187
Cdd:cd07522  150 YRSIYQDVRAAVDWVHSKGLLKK 172
 
Name Accession Description Interval E-value
HAD_cN-II cd07522
cytosolic 5'-nucleotidase II (cN-II) similar to human NT5DC1 (5'-nucleotidase ...
 7-187 4.05e-50

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: 165.52  E-value: 4.05e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965461   7 LGACDVVGFDLDHTLCRYNLPESARLIYNSFAQFLVKEKGYDEGLLTLTPeDWDFCCKGLALDLEDGTFIKLAADGTVLR 86
Cdd:cd07522    8 LEKIKVFGFDMDYTLARYNSPELESLIYDLAKERLVEEKGYPEELLKFDY-DPNFPVRGLVFDKEKGNLLKLDAYGQILR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965461  87 ASHGTKMMTPEALTEAFGKKewrhcvsdkrctsdkpgVSDIPCCSGKCYFYDNYFDLPGALLCARVVDSLTKQNRG--QK 164
Cdd:cd07522   87 AYHGTRPLSDEEVREIYGSN-----------------NTGVRDDESRYYFLNTLFSLPEACLLAQLVDYFDNNPLEsdMS 149

                        170       180
                 ....*....|....*....|...
gi 568965461 165 TFDFWKDVVAGIQHNFKMSAFKE 187
Cdd:cd07522  150 YRSIYQDVRAAVDWVHSKGLLKK 172
5_nucleotid pfam05761
5' nucleotidase family; This family of eukaryotic proteins includes 5' nucleotidase enzymes, ...
 11-178 1.88e-21

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: 90.66  E-value: 1.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965461   11 DVVGFDLDHTLCRYNLPESARLIYNSFAQFLVKEKGYDEGLLTLTpEDWDFCCKGLALDLEDGTFIKLAADGTVLRASHG 90
Cdd:pfam05761   5 KAYGFDMDYTLAQYKSPTFESLAYDLAKERLVEKLGYPEELLELE-YDPDFAIRGLVYDKKRGNLLKVDRFGYIQVAYHG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965461   91 TKMMTPEALTEAFGKKewrhcvsdkrctsdkpgVSDIPCCSGKCYFYDNYFDLPGALLCARVVDSLTkqNRGQKTFDF-- 168
Cdd:pfam05761  84 FRPLSDEEVRELYGNT-----------------FIPLSFDEPRYVQLNTLFSLPEAYLLAQLVDYFD--NGGNIDYDYes 144

                         170
                  ....*....|.
gi 568965461  169 -WKDVVAGIQH 178
Cdd:pfam05761 145 lYQDVREAVDL 155
 
Name Accession Description Interval E-value
HAD_cN-II cd07522
cytosolic 5'-nucleotidase II (cN-II) similar to human NT5DC1 (5'-nucleotidase ...
 7-187 4.05e-50

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: 165.52  E-value: 4.05e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965461   7 LGACDVVGFDLDHTLCRYNLPESARLIYNSFAQFLVKEKGYDEGLLTLTPeDWDFCCKGLALDLEDGTFIKLAADGTVLR 86
Cdd:cd07522    8 LEKIKVFGFDMDYTLARYNSPELESLIYDLAKERLVEEKGYPEELLKFDY-DPNFPVRGLVFDKEKGNLLKLDAYGQILR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965461  87 ASHGTKMMTPEALTEAFGKKewrhcvsdkrctsdkpgVSDIPCCSGKCYFYDNYFDLPGALLCARVVDSLTKQNRG--QK 164
Cdd:cd07522   87 AYHGTRPLSDEEVREIYGSN-----------------NTGVRDDESRYYFLNTLFSLPEACLLAQLVDYFDNNPLEsdMS 149

                        170       180
                 ....*....|....*....|...
gi 568965461 165 TFDFWKDVVAGIQHNFKMSAFKE 187
Cdd:cd07522  150 YRSIYQDVRAAVDWVHSKGLLKK 172
5_nucleotid pfam05761
5' nucleotidase family; This family of eukaryotic proteins includes 5' nucleotidase enzymes, ...
 11-178 1.88e-21

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: 90.66  E-value: 1.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965461   11 DVVGFDLDHTLCRYNLPESARLIYNSFAQFLVKEKGYDEGLLTLTpEDWDFCCKGLALDLEDGTFIKLAADGTVLRASHG 90
Cdd:pfam05761   5 KAYGFDMDYTLAQYKSPTFESLAYDLAKERLVEKLGYPEELLELE-YDPDFAIRGLVYDKKRGNLLKVDRFGYIQVAYHG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965461   91 TKMMTPEALTEAFGKKewrhcvsdkrctsdkpgVSDIPCCSGKCYFYDNYFDLPGALLCARVVDSLTkqNRGQKTFDF-- 168
Cdd:pfam05761  84 FRPLSDEEVRELYGNT-----------------FIPLSFDEPRYVQLNTLFSLPEAYLLAQLVDYFD--NGGNIDYDYes 144

                         170
                  ....*....|.
gi 568965461  169 -WKDVVAGIQH 178
Cdd:pfam05761 145 lYQDVREAVDL 155
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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