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Conserved domains on  [gi|1720362121|ref|XP_030101112|]
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5'-deoxynucleotidase HDDC2 isoform X2 [Mus musculus]

Protein Classification

HD domain-containing protein( domain architecture ID 10586555)

HD domain-containing protein may function as a metal dependent phosphohydrolase; similar to Homo sapiens 5'-deoxynucleotidase HDDC2, which catalyzes the dephosphorylation of the nucleoside 5'-monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and deoxythymidine monophosphate (dTMP)

CATH:  3.30.70.1370
EC:  3.1.-.-
Gene Ontology:  GO:0042578|GO:0046872
PubMed:  9868367
SCOP:  3000943

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HD_3 pfam13023
HD domain; HD domains are metal dependent phosphohydrolases.
 110-210 5.95e-37

HD domain; HD domains are metal dependent phosphohydrolases.


:

Pssm-ID: 432939  Cd Length: 163  Bit Score: 126.56  E-value: 5.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362121 110 LHRVPRTGWVYRNVEKPESVSDHMYRMAVMAMVTRD--DRLNKDRCIRLALVHDMAECIVGDIAPADNIPKEEKHRREEE 187
Cdd:pfam13023   4 LKFVKRQGWLQDGRVRPESVAEHSWRMALMAMLLAEyaGPVDIARVIKMALIHDLVEILAGDIIPYDGVAKEEKEERERE 83

                          90       100
                  ....*....|....*....|....
gi 1720362121 188 AMKQITQLLPEDLRKELYELW-EF 210
Cdd:pfam13023  84 AAERIFGLLPEDQGEELLALWdEF 107
 
Name Accession Description Interval E-value
HD_3 pfam13023
HD domain; HD domains are metal dependent phosphohydrolases.
 110-210 5.95e-37

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 432939  Cd Length: 163  Bit Score: 126.56  E-value: 5.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362121 110 LHRVPRTGWVYRNVEKPESVSDHMYRMAVMAMVTRD--DRLNKDRCIRLALVHDMAECIVGDIAPADNIPKEEKHRREEE 187
Cdd:pfam13023   4 LKFVKRQGWLQDGRVRPESVAEHSWRMALMAMLLAEyaGPVDIARVIKMALIHDLVEILAGDIIPYDGVAKEEKEERERE 83

                          90       100
                  ....*....|....*....|....
gi 1720362121 188 AMKQITQLLPEDLRKELYELW-EF 210
Cdd:pfam13023  84 AAERIFGLLPEDQGEELLALWdEF 107
YfbR COG1896
5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and ...
 110-214 3.12e-21

5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and metabolism, General function prediction only];


Pssm-ID: 441500  Cd Length: 162  Bit Score: 86.07  E-value: 3.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362121 110 LHRVPRTGWVYRNveKPESVSDHMYRMAVMAMV---TRDDRLNKDRCIRLALVHDMAECIVGDIAPADNIPKEEKHRREE 186
Cdd:COG1896    11 LKLIKRWGLLRNS--RPENVAEHSWHVALIAHLladIANEGVDPERVAKMALLHDLVEIDTGDIPTPVKYANEAKKEIER 88

                          90       100
                  ....*....|....*....|....*....
gi 1720362121 187 EAMKQITQLLPEDLRKELYELW-EFLQEK 214
Cdd:COG1896    89 AAAERLFGLLPEELREEFRALWdEFEAGE 117
 
Name Accession Description Interval E-value
HD_3 pfam13023
HD domain; HD domains are metal dependent phosphohydrolases.
 110-210 5.95e-37

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 432939  Cd Length: 163  Bit Score: 126.56  E-value: 5.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362121 110 LHRVPRTGWVYRNVEKPESVSDHMYRMAVMAMVTRD--DRLNKDRCIRLALVHDMAECIVGDIAPADNIPKEEKHRREEE 187
Cdd:pfam13023   4 LKFVKRQGWLQDGRVRPESVAEHSWRMALMAMLLAEyaGPVDIARVIKMALIHDLVEILAGDIIPYDGVAKEEKEERERE 83

                          90       100
                  ....*....|....*....|....
gi 1720362121 188 AMKQITQLLPEDLRKELYELW-EF 210
Cdd:pfam13023  84 AAERIFGLLPEDQGEELLALWdEF 107
YfbR COG1896
5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and ...
 110-214 3.12e-21

5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and metabolism, General function prediction only];


Pssm-ID: 441500  Cd Length: 162  Bit Score: 86.07  E-value: 3.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362121 110 LHRVPRTGWVYRNveKPESVSDHMYRMAVMAMV---TRDDRLNKDRCIRLALVHDMAECIVGDIAPADNIPKEEKHRREE 186
Cdd:COG1896    11 LKLIKRWGLLRNS--RPENVAEHSWHVALIAHLladIANEGVDPERVAKMALLHDLVEIDTGDIPTPVKYANEAKKEIER 88

                          90       100
                  ....*....|....*....|....*....
gi 1720362121 187 EAMKQITQLLPEDLRKELYELW-EFLQEK 214
Cdd:COG1896    89 AAAERLFGLLPEELREEFRALWdEFEAGE 117
YfbR-like pfam12917
5'-deoxynucleotidase YfbR-like; This entry contains Escherichia coli (strain K12) YfbR. It a 5 ...
 121-170 1.52e-03

5'-deoxynucleotidase YfbR-like; This entry contains Escherichia coli (strain K12) YfbR. It a 5'-deoxynucleotidase that functions as a dCMP phosphohydrolase in a salvage pathway for the synthesis of dUMP in a dcd/deoA mutant. YfbR contains a conserved HD domain. YfbR has phosphatase activity with deoxyribonucleoside 5'-monophosphates and does not hydrolyze ribonucleotides or deoxyribonucloside 3'-monophosphates. Crystal structures of YfbR have been solved, it was suggested that the biological unit is a dimer. This family also includes phage HD domain-containing hydrolase-like enzymes, such as A0A2H5BHG9 and A0A2L0V156 from Acinetobacter phage SH-Ab15497, which are associated with PurZ, an enzyme that catalyzes the synthesis of diaminopurine (Z), a DNA modification that gives phages an advantage for evading host restriction enzymes activity. They have 2'-deoxyadenine 5'-triphosphate triphosphohydrolase (dATPase) activity and catalyze the hydrolysis of 2'-deoxyadenine 5'-triphosphate dATP to 2'-deoxyadenine (dA) and triphosphate. These enzymes are highly specific for dATP and also catalyze the hydrolysis of dADP and dAMP into dA, releasing pyrophosphate and phosphate, respectively. Thus, these dATPases facilitate the synthesis of Z-genome synthesis removing dATP and dADP from the nucleotide pool of the host.


Pssm-ID: 432874  Cd Length: 182  Bit Score: 37.87  E-value: 1.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720362121 121 RNVEkPESVSDHMYRMAVMAM---VTRDDRLNK----DRCIRLALVHDMAECIVGDI 170
Cdd:pfam12917  19 RNTR-PENVAEHSLQVAMIAHalaLIENERFGGnvdpERLAVLALYHDASEIITGDM 74
 
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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