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Conserved domains on  [gi|1370477368|ref|XP_024308577|]
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5'-nucleotidase domain-containing protein 4 isoform X18 [Homo sapiens]

Protein Classification

Graphical summary

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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, ...
 103-333 5.63e-100

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: 302.52  E-value: 5.63e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477368 103 LGKIRCFGFDMDYTLAAYKSPAYEALTFELLLERLV-CIGYPHEILRYTYDPTFPTRRLVFDELYGNLLKVDAHGNVLLG 181
Cdd:pfam05761   1 LDNIKAYGFDMDYTLAQYKSPTFESLAYDLAKERLVeKLGYPEELLELEYDPDFAIRGLVYDKKRGNLLKVDRFGYIQVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477368 182 AYGFTFLSDlpllrAEIWSFYPSKFIQR-DDLQCFYILNMLFNLPETYLYACLVDFFSgcsrytncdtgyQHGNLFMSFR 260
Cdd:pfam05761  81 YHGFRPLSD-----EEVRELYGNTFIPLsFDEPRYVQLNTLFSLPEAYLLAQLVDYFD------------NGGNIDYDYE 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370477368 261 SLFQDVTDAMNNIHQSGCLKK-TLEDLEKYVKKDPRLPILLGKMKEVG-KVFLATNSSYNYTNAIMTYLFSISEP 333
Cdd:pfam05761 144 SLYQDVREAVDLVHRDGSLKKeVAADPEKYIEKDPELPPLLERLREAGkKLFLLTNSDYDYTNKGMNYLLGGFLP 218
 
Name Accession Description Interval E-value
5_nucleotid pfam05761
5' nucleotidase family; This family of eukaryotic proteins includes 5' nucleotidase enzymes, ...
 103-333 5.63e-100

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: 302.52  E-value: 5.63e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477368 103 LGKIRCFGFDMDYTLAAYKSPAYEALTFELLLERLV-CIGYPHEILRYTYDPTFPTRRLVFDELYGNLLKVDAHGNVLLG 181
Cdd:pfam05761   1 LDNIKAYGFDMDYTLAQYKSPTFESLAYDLAKERLVeKLGYPEELLELEYDPDFAIRGLVYDKKRGNLLKVDRFGYIQVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477368 182 AYGFTFLSDlpllrAEIWSFYPSKFIQR-DDLQCFYILNMLFNLPETYLYACLVDFFSgcsrytncdtgyQHGNLFMSFR 260
Cdd:pfam05761  81 YHGFRPLSD-----EEVRELYGNTFIPLsFDEPRYVQLNTLFSLPEAYLLAQLVDYFD------------NGGNIDYDYE 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370477368 261 SLFQDVTDAMNNIHQSGCLKK-TLEDLEKYVKKDPRLPILLGKMKEVG-KVFLATNSSYNYTNAIMTYLFSISEP 333
Cdd:pfam05761 144 SLYQDVREAVDLVHRDGSLKKeVAADPEKYIEKDPELPPLLERLREAGkKLFLLTNSDYDYTNKGMNYLLGGFLP 218
HAD-IG-Ncltidse TIGR02244
HAD superfamily (subfamily IG) hydrolase, 5'-nucleotidase; This model includes a 5 ...
 95-328 1.31e-89

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: 272.66  E-value: 1.31e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477368  95 IFVNRSLALGKIRCFGFDMDYTLAAYKSPAYEALTFELLLERLVCI-GYPHEILRYTYDPTFPTRRLVFDELYGNLLKVD 173
Cdd:TIGR02244   1 VFVNRELNLEKIQVFGFDMDYTLAQYKSPELEALIYDLAKERLVKRfGYPEELLSFAYDPTFAIRGLVFDKLKGNLLKLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477368 174 AHGNVLLGAYGFTFLSDlpllrAEIWSFYPSKFIQRDDLQCFYILNMLFNLPETYLYACLVDFFSGCSrytncdtgyqHG 253
Cdd:TIGR02244  81 RFGNILRGYHGLRPLSD-----KEVQEIYGNKYISRSNGDRYYLLDTLFSLPEACLIAQLVDYFDDHP----------KG 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370477368 254 NLFMSFRSLFQDVTDAMNNIHQSGCLK-KTLEDLEKYVKKDPRLPILLGKMKEVGK-VFLATNSSYNYTNAIMTYLF 328
Cdd:TIGR02244 146 PLAFDYRQIYQDVRDALDWVHRKGSLKkKVMENPEKYVLRDPKLPLFLSKLKEHGKkLFLLTNSDYDYTDKGMKYLL 222
HAD_cN-II cd07522
cytosolic 5'-nucleotidase II (cN-II) similar to human NT5DC1 (5'-nucleotidase ...
 96-333 1.58e-87

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: 267.60  E-value: 1.58e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477368  96 FVNRSLALGKIRCFGFDMDYTLAAYKSPAYEALTFELLLERLV-CIGYPHEILRYTYDPTFPTRRLVFDELYGNLLKVDA 174
Cdd:cd07522     1 FVNRSLNLEKIKVFGFDMDYTLARYNSPELESLIYDLAKERLVeEKGYPEELLKFDYDPNFPVRGLVFDKEKGNLLKLDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477368 175 HGNVLLGAYGFTFLSDLpllraEIWSFYPS-KFIQRDDLQCFYILNMLFNLPETYLYACLVDFFSGCSRYTncdtgyqhg 253
Cdd:cd07522    81 YGQILRAYHGTRPLSDE-----EVREIYGSnNTGVRDDESRYYFLNTLFSLPEACLLAQLVDYFDNNPLES--------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477368 254 nlFMSFRSLFQDVTDAMNNIHQSGCLKK-TLEDLEKYVKKDPRLPILLGKMKEVG-KVFLATNSSYNYTNAIMTYLFSIS 331
Cdd:cd07522   147 --DMSYRSIYQDVRAAVDWVHSKGLLKKkIMQDPERYVLRDPELPLLLSRLREAGkKLFLLTNSDYSYTNKGMKYLLGGF 224


                  ..
gi 1370477368 332 EP 333
Cdd:cd07522   225 LP 226
 
Name Accession Description Interval E-value
5_nucleotid pfam05761
5' nucleotidase family; This family of eukaryotic proteins includes 5' nucleotidase enzymes, ...
 103-333 5.63e-100

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: 302.52  E-value: 5.63e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477368 103 LGKIRCFGFDMDYTLAAYKSPAYEALTFELLLERLV-CIGYPHEILRYTYDPTFPTRRLVFDELYGNLLKVDAHGNVLLG 181
Cdd:pfam05761   1 LDNIKAYGFDMDYTLAQYKSPTFESLAYDLAKERLVeKLGYPEELLELEYDPDFAIRGLVYDKKRGNLLKVDRFGYIQVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477368 182 AYGFTFLSDlpllrAEIWSFYPSKFIQR-DDLQCFYILNMLFNLPETYLYACLVDFFSgcsrytncdtgyQHGNLFMSFR 260
Cdd:pfam05761  81 YHGFRPLSD-----EEVRELYGNTFIPLsFDEPRYVQLNTLFSLPEAYLLAQLVDYFD------------NGGNIDYDYE 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370477368 261 SLFQDVTDAMNNIHQSGCLKK-TLEDLEKYVKKDPRLPILLGKMKEVG-KVFLATNSSYNYTNAIMTYLFSISEP 333
Cdd:pfam05761 144 SLYQDVREAVDLVHRDGSLKKeVAADPEKYIEKDPELPPLLERLREAGkKLFLLTNSDYDYTNKGMNYLLGGFLP 218
HAD-IG-Ncltidse TIGR02244
HAD superfamily (subfamily IG) hydrolase, 5'-nucleotidase; This model includes a 5 ...
 95-328 1.31e-89

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: 272.66  E-value: 1.31e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477368  95 IFVNRSLALGKIRCFGFDMDYTLAAYKSPAYEALTFELLLERLVCI-GYPHEILRYTYDPTFPTRRLVFDELYGNLLKVD 173
Cdd:TIGR02244   1 VFVNRELNLEKIQVFGFDMDYTLAQYKSPELEALIYDLAKERLVKRfGYPEELLSFAYDPTFAIRGLVFDKLKGNLLKLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477368 174 AHGNVLLGAYGFTFLSDlpllrAEIWSFYPSKFIQRDDLQCFYILNMLFNLPETYLYACLVDFFSGCSrytncdtgyqHG 253
Cdd:TIGR02244  81 RFGNILRGYHGLRPLSD-----KEVQEIYGNKYISRSNGDRYYLLDTLFSLPEACLIAQLVDYFDDHP----------KG 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370477368 254 NLFMSFRSLFQDVTDAMNNIHQSGCLK-KTLEDLEKYVKKDPRLPILLGKMKEVGK-VFLATNSSYNYTNAIMTYLF 328
Cdd:TIGR02244 146 PLAFDYRQIYQDVRDALDWVHRKGSLKkKVMENPEKYVLRDPKLPLFLSKLKEHGKkLFLLTNSDYDYTDKGMKYLL 222
HAD_cN-II cd07522
cytosolic 5'-nucleotidase II (cN-II) similar to human NT5DC1 (5'-nucleotidase ...
 96-333 1.58e-87

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: 267.60  E-value: 1.58e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477368  96 FVNRSLALGKIRCFGFDMDYTLAAYKSPAYEALTFELLLERLV-CIGYPHEILRYTYDPTFPTRRLVFDELYGNLLKVDA 174
Cdd:cd07522     1 FVNRSLNLEKIKVFGFDMDYTLARYNSPELESLIYDLAKERLVeEKGYPEELLKFDYDPNFPVRGLVFDKEKGNLLKLDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477368 175 HGNVLLGAYGFTFLSDLpllraEIWSFYPS-KFIQRDDLQCFYILNMLFNLPETYLYACLVDFFSGCSRYTncdtgyqhg 253
Cdd:cd07522    81 YGQILRAYHGTRPLSDE-----EVREIYGSnNTGVRDDESRYYFLNTLFSLPEACLLAQLVDYFDNNPLES--------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477368 254 nlFMSFRSLFQDVTDAMNNIHQSGCLKK-TLEDLEKYVKKDPRLPILLGKMKEVG-KVFLATNSSYNYTNAIMTYLFSIS 331
Cdd:cd07522   147 --DMSYRSIYQDVRAAVDWVHSKGLLKKkIMQDPERYVLRDPELPLLLSRLREAGkKLFLLTNSDYSYTNKGMKYLLGGF 224


                  ..
gi 1370477368 332 EP 333
Cdd:cd07522   225 LP 226
 
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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