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Conserved domains on  [gi|116875826|ref|NP_057147|]
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5'-deoxynucleotidase HDDC2 [Homo sapiens]

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.
24-180 1.92e-50

HD domain; HD domains are metal dependent phosphohydrolases.


:

Pssm-ID: 432939  Cd Length: 163  Bit Score: 160.84  E-value: 1.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875826   24 VGQLKRVPRTGWVYRNVQRPESVSDHMYRMAVMAMVIKD--DRLNKDRCVRLALVHDMAECIVGDIAPADNIPKEEKHRR 101
Cdd:pfam13023   1 ADKLKFVKRQGWLQDGRVRPESVAEHSWRMALMAMLLAEyaGPVDIARVIKMALIHDLVEILAGDIIPYDGVAKEEKEER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875826  102 EEEAMKQITQLLPEDLRKELYELWEEYETQSSAEAKFVKQLDQCEMILQASEYEDLEHKPG--RLQDFYDSTAGKF--NH 177
Cdd:pfam13023  81 EREAAERIFGLLPEDQGEELLALWDEFEARETPEAKFAKDLDKLEPLLQNLEYEGDSWAAFeaDLSQFYGRNSTILaeGS 160

                  ...
gi 116875826  178 PEI 180
Cdd:pfam13023 161 PEL 163
 
Name Accession Description Interval E-value
HD_3 pfam13023
HD domain; HD domains are metal dependent phosphohydrolases.
24-180 1.92e-50

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 432939  Cd Length: 163  Bit Score: 160.84  E-value: 1.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875826   24 VGQLKRVPRTGWVYRNVQRPESVSDHMYRMAVMAMVIKD--DRLNKDRCVRLALVHDMAECIVGDIAPADNIPKEEKHRR 101
Cdd:pfam13023   1 ADKLKFVKRQGWLQDGRVRPESVAEHSWRMALMAMLLAEyaGPVDIARVIKMALIHDLVEILAGDIIPYDGVAKEEKEER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875826  102 EEEAMKQITQLLPEDLRKELYELWEEYETQSSAEAKFVKQLDQCEMILQASEYEDLEHKPG--RLQDFYDSTAGKF--NH 177
Cdd:pfam13023  81 EREAAERIFGLLPEDQGEELLALWDEFEARETPEAKFAKDLDKLEPLLQNLEYEGDSWAAFeaDLSQFYGRNSTILaeGS 160

                  ...
gi 116875826  178 PEI 180
Cdd:pfam13023 161 PEL 163
YfbR COG1896
5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and ...
17-174 6.81e-32

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


Pssm-ID: 441500  Cd Length: 162  Bit Score: 113.04  E-value: 6.81e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875826  17 LLQFLRLVGQLKRVPRTGWVYRNvqRPESVSDHMYRMAVMAMV---IKDDRLNKDRCVRLALVHDMAECIVGDIAPADNI 93
Cdd:COG1896    1 QLDFLAELDRLKLIKRWGLLRNS--RPENVAEHSWHVALIAHLladIANEGVDPERVAKMALLHDLVEIDTGDIPTPVKY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875826  94 PKEEKHRREEEAMKQITQLLPEDLRKELYELWEEYETQSSAEAKFVKQLDQCEMILQASEYEDLEHKPGRLQDFYDSTAG 173
Cdd:COG1896   79 ANEAKKEIERAAAERLFGLLPEELREEFRALWDEFEAGETPEARFVKAADKLEALLQALEEIGAGNKENTFEQAYERLLK 158

                 .
gi 116875826 174 K 174
Cdd:COG1896  159 K 159
PRK03826 PRK03826
5'-nucleotidase; Provisional
20-143 1.60e-04

5'-nucleotidase; Provisional


Pssm-ID: 235165  Cd Length: 195  Bit Score: 40.75  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875826  20 FLRLVGQLKRVPRTGwVYRNVqRPESVSDHMYRMAVMA---MVIKDDR----LNKDRCVRLALVHDMAECIVGDIapadN 92
Cdd:PRK03826   5 FFAHLSRLKLINRWP-LMRNV-RTENVSEHSLQVAMVAhalAVIKNRKfggnLNAERIALLAMYHDASEVLTGDL----P 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 116875826  93 IPKEEKHRREEEAMKQITQ--------LLPEDLRKELYELWEEYETqSSAEAKFVKQLD 143
Cdd:PRK03826  79 TPVKYFNPEIAHEYKKIEKiaeqklldMLPEELQEDFRPLLDSHAA-SEEEKAIVKQAD 136
 
Name Accession Description Interval E-value
HD_3 pfam13023
HD domain; HD domains are metal dependent phosphohydrolases.
24-180 1.92e-50

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 432939  Cd Length: 163  Bit Score: 160.84  E-value: 1.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875826   24 VGQLKRVPRTGWVYRNVQRPESVSDHMYRMAVMAMVIKD--DRLNKDRCVRLALVHDMAECIVGDIAPADNIPKEEKHRR 101
Cdd:pfam13023   1 ADKLKFVKRQGWLQDGRVRPESVAEHSWRMALMAMLLAEyaGPVDIARVIKMALIHDLVEILAGDIIPYDGVAKEEKEER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875826  102 EEEAMKQITQLLPEDLRKELYELWEEYETQSSAEAKFVKQLDQCEMILQASEYEDLEHKPG--RLQDFYDSTAGKF--NH 177
Cdd:pfam13023  81 EREAAERIFGLLPEDQGEELLALWDEFEARETPEAKFAKDLDKLEPLLQNLEYEGDSWAAFeaDLSQFYGRNSTILaeGS 160

                  ...
gi 116875826  178 PEI 180
Cdd:pfam13023 161 PEL 163
YfbR COG1896
5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and ...
17-174 6.81e-32

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


Pssm-ID: 441500  Cd Length: 162  Bit Score: 113.04  E-value: 6.81e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875826  17 LLQFLRLVGQLKRVPRTGWVYRNvqRPESVSDHMYRMAVMAMV---IKDDRLNKDRCVRLALVHDMAECIVGDIAPADNI 93
Cdd:COG1896    1 QLDFLAELDRLKLIKRWGLLRNS--RPENVAEHSWHVALIAHLladIANEGVDPERVAKMALLHDLVEIDTGDIPTPVKY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875826  94 PKEEKHRREEEAMKQITQLLPEDLRKELYELWEEYETQSSAEAKFVKQLDQCEMILQASEYEDLEHKPGRLQDFYDSTAG 173
Cdd:COG1896   79 ANEAKKEIERAAAERLFGLLPEELREEFRALWDEFEAGETPEARFVKAADKLEALLQALEEIGAGNKENTFEQAYERLLK 158

                 .
gi 116875826 174 K 174
Cdd:COG1896  159 K 159
YfbR-like pfam12917
5'-deoxynucleotidase YfbR-like; This entry contains Escherichia coli (strain K12) YfbR. It a 5 ...
38-87 1.47e-05

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: 43.65  E-value: 1.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116875826   38 RNVqRPESVSDHMYRMAVMAM---VIKDDRLNK----DRCVRLALVHDMAECIVGDI 87
Cdd:pfam12917  19 RNT-RPENVAEHSLQVAMIAHalaLIENERFGGnvdpERLAVLALYHDASEIITGDM 74
PRK03826 PRK03826
5'-nucleotidase; Provisional
20-143 1.60e-04

5'-nucleotidase; Provisional


Pssm-ID: 235165  Cd Length: 195  Bit Score: 40.75  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875826  20 FLRLVGQLKRVPRTGwVYRNVqRPESVSDHMYRMAVMA---MVIKDDR----LNKDRCVRLALVHDMAECIVGDIapadN 92
Cdd:PRK03826   5 FFAHLSRLKLINRWP-LMRNV-RTENVSEHSLQVAMVAhalAVIKNRKfggnLNAERIALLAMYHDASEVLTGDL----P 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 116875826  93 IPKEEKHRREEEAMKQITQ--------LLPEDLRKELYELWEEYETqSSAEAKFVKQLD 143
Cdd:PRK03826  79 TPVKYFNPEIAHEYKKIEKiaeqklldMLPEELQEDFRPLLDSHAA-SEEEKAIVKQAD 136
 
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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