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Conserved domains on  [gi|16924327|gb|AAH17454|]
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5', 3'-nucleotidase, cytosolic [Homo sapiens]

Protein Classification

5'-3'-deoxyribonucleotidase( domain architecture ID 11552331)

5'-3'-deoxyribonucleotidase is a HAD (haloacid dehalogenase) family hydrolase that catalyzes the dephosphorylation of the 5' and 2'(3')-phosphates of deoxyribonucleotides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_5-3dNT cd02587
5'(3')-deoxyribonucleotidase; This family includes cytosolic 5'(3')-deoxyribonucleotidase (cdN) ...
 5-168 9.66e-86

5'(3')-deoxyribonucleotidase; This family includes cytosolic 5'(3')-deoxyribonucleotidase (cdN) and mitochondrial 5'(3')-deoxyribonucleotidase (mdN). cdN and mdN specifically dephosphorylate the deoxyribo form of nucleoside monophosphates helps maintain homeostasis of deoxynucleosides required for mitochondrial DNA synthesis. Their preferred substrates are dUMP and dTMP. cdN also dephosphorylates dGMP and dIMP efficiently. They can also dephosphorylate the 5'- or 3'-phosphates of pyrimidine ribonucleotides. This family belongs 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: 319786  Cd Length: 161  Bit Score: 250.00  E-value: 9.66e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16924327   5 VRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRAlrPDLADKVASVYEAPGFFLDLEPIPGALDAV 84
Cdd:cd02587   1 IVILVDMDGVLADFEGALVRAIRERFPDEPHVLLESRRGFWVIEQYKA--PELSRKAADILEEPGFFRNLEPIPGAVEAL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16924327  85 REMNDlPDTQVFICTSPLLKYHHCVGEKYRWVEQHLGPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFT 164
Cdd:cd02587  79 RELSD-EGTDVYICTSPLNKYPTCVEEKYEWVEEHFPPLFYQRIVLTRDKTVVLADILIDDNPENLEAFEGPGWEHILFT 157


                ....
gi 16924327 165 CCHN 168
Cdd:cd02587 158 ACHN 161
 
Name Accession Description Interval E-value
HAD_5-3dNT cd02587
5'(3')-deoxyribonucleotidase; This family includes cytosolic 5'(3')-deoxyribonucleotidase (cdN) ...
 5-168 9.66e-86

5'(3')-deoxyribonucleotidase; This family includes cytosolic 5'(3')-deoxyribonucleotidase (cdN) and mitochondrial 5'(3')-deoxyribonucleotidase (mdN). cdN and mdN specifically dephosphorylate the deoxyribo form of nucleoside monophosphates helps maintain homeostasis of deoxynucleosides required for mitochondrial DNA synthesis. Their preferred substrates are dUMP and dTMP. cdN also dephosphorylates dGMP and dIMP efficiently. They can also dephosphorylate the 5'- or 3'-phosphates of pyrimidine ribonucleotides. This family belongs 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: 319786  Cd Length: 161  Bit Score: 250.00  E-value: 9.66e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16924327   5 VRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRAlrPDLADKVASVYEAPGFFLDLEPIPGALDAV 84
Cdd:cd02587   1 IVILVDMDGVLADFEGALVRAIRERFPDEPHVLLESRRGFWVIEQYKA--PELSRKAADILEEPGFFRNLEPIPGAVEAL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16924327  85 REMNDlPDTQVFICTSPLLKYHHCVGEKYRWVEQHLGPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFT 164
Cdd:cd02587  79 RELSD-EGTDVYICTSPLNKYPTCVEEKYEWVEEHFPPLFYQRIVLTRDKTVVLADILIDDNPENLEAFEGPGWEHILFT 157


                ....
gi 16924327 165 CCHN 168
Cdd:cd02587 158 ACHN 161
YorC COG4502
5'(3')-deoxyribonucleotidase [Nucleotide transport and metabolism];
6-192 3.35e-52

5'(3')-deoxyribonucleotidase [Nucleotide transport and metabolism];


Pssm-ID: 443586 [Multi-domain]  Cd Length: 177  Bit Score: 165.43  E-value: 3.35e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16924327   6 RVLVDMDGVLADFEAGLLRGFRRRFPEepHVPLEQRRGFlarEQYRALRPDLADKVASVYEAPGFFLDLEPIPGALDAVR 85
Cdd:COG4502   4 RIAVDMDGVLADFYAAFLDIYNKEYGT--NLTLEDLDGW---DLWELVPPEHRERIREFLNEPGFFRDLPPIPGAQEVLK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16924327  86 EMNDLPDtqVFICTSPLLkYHHCVGEKYRWVEQHLGPQFVERIILTRDKTVVLGDLLIDDKDTvrgQEETPSWEHILFTC 165
Cdd:COG4502  79 ELSDKYE--VYIVTAAME-FPNSLEEKYEWLDEHFPFIPWQNIIFCGDKSLVGGDYLIDDNPK---NLEEFKGKGILFDA 152

                       170       180
                ....*....|....*....|....*..
gi 16924327 166 CHNRHLvlpPTRRRLlswsDNWREILD 192
Cdd:COG4502 153 PHNRHI---TGYPRV----NNWKEVEA 172
NT5C pfam06941
5' nucleotidase, deoxy (Pyrimidine), cytosolic type C protein (NT5C); This family consists of ...
 7-194 4.90e-20

5' nucleotidase, deoxy (Pyrimidine), cytosolic type C protein (NT5C); This family consists of several 5' nucleotidase, deoxy (Pyrimidine), cytosolic type C (NT5C) proteins. 5'(3')-Deoxyribonucleotidase is a ubiquitous enzyme in mammalian cells whose physiological function is not known.


Pssm-ID: 284381 [Multi-domain]  Cd Length: 180  Bit Score: 83.04  E-value: 4.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16924327     7 VLVDMDGVLADFEAGLLRGFRRRFpEEPHVPlEQRRGFLAREqyrALRPDLADKVASVYEAPGFFLDLEPIPGALDAVRE 86
Cdd:pfam06941   4 IGVDLDGVCADFYGRMRQIANEWF-ERPLLP-EEVSSWGWSE---WTNPEQYDSLHRFVTQPGFFSDLEPIPGAREYLRQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16924327    87 MNDlpDTQVFICTSPLLKYHHCVGEKYRWVEQHLGPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSwehILFTCC 166
Cdd:pfam06941  79 LSD--EGRIVIITHRLFQHYTAVQQKVNWLDSHLPGIPYWNLCFVKEKTQVRGDIYIDDSPENLAQLRGRG---ILFGNP 153

                         170       180
                  ....*....|....*....|....*...
gi 16924327   167 HNRHLvlpPTRRRLLSWSDNWREILDSK 194
Cdd:pfam06941 154 TNRHI---EDELRAASWQEVYDMILVAK 178
 
Name Accession Description Interval E-value
HAD_5-3dNT cd02587
5'(3')-deoxyribonucleotidase; This family includes cytosolic 5'(3')-deoxyribonucleotidase (cdN) ...
 5-168 9.66e-86

5'(3')-deoxyribonucleotidase; This family includes cytosolic 5'(3')-deoxyribonucleotidase (cdN) and mitochondrial 5'(3')-deoxyribonucleotidase (mdN). cdN and mdN specifically dephosphorylate the deoxyribo form of nucleoside monophosphates helps maintain homeostasis of deoxynucleosides required for mitochondrial DNA synthesis. Their preferred substrates are dUMP and dTMP. cdN also dephosphorylates dGMP and dIMP efficiently. They can also dephosphorylate the 5'- or 3'-phosphates of pyrimidine ribonucleotides. This family belongs 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: 319786  Cd Length: 161  Bit Score: 250.00  E-value: 9.66e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16924327   5 VRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRAlrPDLADKVASVYEAPGFFLDLEPIPGALDAV 84
Cdd:cd02587   1 IVILVDMDGVLADFEGALVRAIRERFPDEPHVLLESRRGFWVIEQYKA--PELSRKAADILEEPGFFRNLEPIPGAVEAL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16924327  85 REMNDlPDTQVFICTSPLLKYHHCVGEKYRWVEQHLGPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFT 164
Cdd:cd02587  79 RELSD-EGTDVYICTSPLNKYPTCVEEKYEWVEEHFPPLFYQRIVLTRDKTVVLADILIDDNPENLEAFEGPGWEHILFT 157


                ....
gi 16924327 165 CCHN 168
Cdd:cd02587 158 ACHN 161
YorC COG4502
5'(3')-deoxyribonucleotidase [Nucleotide transport and metabolism];
6-192 3.35e-52

5'(3')-deoxyribonucleotidase [Nucleotide transport and metabolism];


Pssm-ID: 443586 [Multi-domain]  Cd Length: 177  Bit Score: 165.43  E-value: 3.35e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16924327   6 RVLVDMDGVLADFEAGLLRGFRRRFPEepHVPLEQRRGFlarEQYRALRPDLADKVASVYEAPGFFLDLEPIPGALDAVR 85
Cdd:COG4502   4 RIAVDMDGVLADFYAAFLDIYNKEYGT--NLTLEDLDGW---DLWELVPPEHRERIREFLNEPGFFRDLPPIPGAQEVLK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16924327  86 EMNDLPDtqVFICTSPLLkYHHCVGEKYRWVEQHLGPQFVERIILTRDKTVVLGDLLIDDKDTvrgQEETPSWEHILFTC 165
Cdd:COG4502  79 ELSDKYE--VYIVTAAME-FPNSLEEKYEWLDEHFPFIPWQNIIFCGDKSLVGGDYLIDDNPK---NLEEFKGKGILFDA 152

                       170       180
                ....*....|....*....|....*..
gi 16924327 166 CHNRHLvlpPTRRRLlswsDNWREILD 192
Cdd:COG4502 153 PHNRHI---TGYPRV----NNWKEVEA 172
NT5C pfam06941
5' nucleotidase, deoxy (Pyrimidine), cytosolic type C protein (NT5C); This family consists of ...
 7-194 4.90e-20

5' nucleotidase, deoxy (Pyrimidine), cytosolic type C protein (NT5C); This family consists of several 5' nucleotidase, deoxy (Pyrimidine), cytosolic type C (NT5C) proteins. 5'(3')-Deoxyribonucleotidase is a ubiquitous enzyme in mammalian cells whose physiological function is not known.


Pssm-ID: 284381 [Multi-domain]  Cd Length: 180  Bit Score: 83.04  E-value: 4.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16924327     7 VLVDMDGVLADFEAGLLRGFRRRFpEEPHVPlEQRRGFLAREqyrALRPDLADKVASVYEAPGFFLDLEPIPGALDAVRE 86
Cdd:pfam06941   4 IGVDLDGVCADFYGRMRQIANEWF-ERPLLP-EEVSSWGWSE---WTNPEQYDSLHRFVTQPGFFSDLEPIPGAREYLRQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16924327    87 MNDlpDTQVFICTSPLLKYHHCVGEKYRWVEQHLGPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSwehILFTCC 166
Cdd:pfam06941  79 LSD--EGRIVIITHRLFQHYTAVQQKVNWLDSHLPGIPYWNLCFVKEKTQVRGDIYIDDSPENLAQLRGRG---ILFGNP 153

                         170       180
                  ....*....|....*....|....*...
gi 16924327   167 HNRHLvlpPTRRRLLSWSDNWREILDSK 194
Cdd:pfam06941 154 TNRHI---EDELRAASWQEVYDMILVAK 178
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
7-106 3.32e-04

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 39.91  E-value: 3.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16924327   7 VLVDMDGVLADFEAGLLRGFRRRFPEE--PHVPLEQRRGFL---AREQYRAL--------RPDLADKVASVYEApGFFLD 73
Cdd:COG0546   4 VLFDLDGTLVDSAPDIAAALNEALAELglPPLDLEELRALIglgLRELLRRLlgedpdeeLEELLARFRELYEE-ELLDE 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 16924327  74 LEPIPGALDAVREMNDLpDTQVFICTS-------PLLKYH 106
Cdd:COG0546  83 TRLFPGVRELLEALKAR-GIKLAVVTNkprefaeRLLEAL 121
 
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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