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Conserved domains on  [gi|6319719|ref|NP_009801|]
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5'-deoxynucleotidase [Saccharomyces cerevisiae S288C]

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.
55-200 2.03e-47

HD domain; HD domains are metal dependent phosphohydrolases.


:

Pssm-ID: 432939  Cd Length: 163  Bit Score: 154.30  E-value: 2.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319719     55 VQQLKIQRRTGYLDLGIKECESISDHMYRLSIITMLIKDS--RVNRDKCVRIALVHDIAESLVGDITPVDPIGKEEKHRR 132
Cdd:pfam13023   1 ADKLKFVKRQGWLQDGRVRPESVAEHSWRMALMAMLLAEYagPVDIARVIKMALIHDLVEILAGDIIPYDGVAKEEKEER 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6319719    133 EWETIKYLCNALIKPyneiAAKEIMDDWLAYENVTSLEARYVKDIDKYEMLVQCFEYEREYKGTKNFD 200
Cdd:pfam13023  81 EREAAERIFGLLPED----QGEELLALWDEFEARETPEAKFAKDLDKLEPLLQNLEYEGDSWAAFEAD 144
 
Name Accession Description Interval E-value
HD_3 pfam13023
HD domain; HD domains are metal dependent phosphohydrolases.
55-200 2.03e-47

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 432939  Cd Length: 163  Bit Score: 154.30  E-value: 2.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319719     55 VQQLKIQRRTGYLDLGIKECESISDHMYRLSIITMLIKDS--RVNRDKCVRIALVHDIAESLVGDITPVDPIGKEEKHRR 132
Cdd:pfam13023   1 ADKLKFVKRQGWLQDGRVRPESVAEHSWRMALMAMLLAEYagPVDIARVIKMALIHDLVEILAGDIIPYDGVAKEEKEER 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6319719    133 EWETIKYLCNALIKPyneiAAKEIMDDWLAYENVTSLEARYVKDIDKYEMLVQCFEYEREYKGTKNFD 200
Cdd:pfam13023  81 EREAAERIFGLLPED----QGEELLALWDEFEARETPEAKFAKDLDKLEPLLQNLEYEGDSWAAFEAD 144
YfbR COG1896
5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and ...
48-191 8.85e-29

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


Pssm-ID: 441500  Cd Length: 162  Bit Score: 106.10  E-value: 8.85e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319719   48 ILAFLNVVQQLK-IQRRTGYLDlgiKECESISDHMYRLSIITML---IKDSRVNRDKCVRIALVHDIAESLVGDITPVDP 123
Cdd:COG1896   1 QLDFLAELDRLKlIKRWGLLRN---SRPENVAEHSWHVALIAHLladIANEGVDPERVAKMALLHDLVEIDTGDIPTPVK 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6319719  124 IGKEEKHRREWETIKYLCNALIKPYneiaAKEIMDDWLAYENVTSLEARYVKDIDKYEMLVQCFEYER 191
Cdd:COG1896  78 YANEAKKEIERAAAERLFGLLPEEL----REEFRALWDEFEAGETPEARFVKAADKLEALLQALEEIG 141
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
73-192 5.19e-10

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 55.77  E-value: 5.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319719      73 ECESISDHMYRLSIITMLIKDS--RVNRDKCVRIALVHDIAESLVGDITPVDPIGKEEKHRREWETIK--YLCNALIKPY 148
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAALAEElgLLDIELLLLAALLHDIGKPGTPDSFLVKTSVLEDHHFIGAEILLeeEEPRILEEIL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 6319719     149 NEIAAKEIMDDWLAYENVTSLEARYVKDIDKYEMLVQCFEYERE 192
Cdd:smart00471  81 RTAILSHHERPDGLRGEPITLEARIVKVADRLDALRADRRYRRV 124
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
87-203 5.72e-05

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 41.94  E-value: 5.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319719   87 ITMLIKDSRVNRDKCVRIALVHDIAESLVGDITPVDPIGKEEKH-------------RREWETIKYLCNALIKPYNEIAA 153
Cdd:cd00077  17 LAEELGLSEEDIELLRLAALLHDIGKPGTPDAITEEESELEKDHaivgaeilrelllEEVIKLIDELILAVDASHHERLD 96
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6319719  154 KEIMDDWLAYENVTsLEARYVKDIDKYEMLVQCFEYEREYKGTKNFDDFF 203
Cdd:cd00077  97 GLGYPDGLKGEEIT-LEARIVKLADRLDALRRDSREKRRRIAEEDLEELL 145
 
Name Accession Description Interval E-value
HD_3 pfam13023
HD domain; HD domains are metal dependent phosphohydrolases.
55-200 2.03e-47

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 432939  Cd Length: 163  Bit Score: 154.30  E-value: 2.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319719     55 VQQLKIQRRTGYLDLGIKECESISDHMYRLSIITMLIKDS--RVNRDKCVRIALVHDIAESLVGDITPVDPIGKEEKHRR 132
Cdd:pfam13023   1 ADKLKFVKRQGWLQDGRVRPESVAEHSWRMALMAMLLAEYagPVDIARVIKMALIHDLVEILAGDIIPYDGVAKEEKEER 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6319719    133 EWETIKYLCNALIKPyneiAAKEIMDDWLAYENVTSLEARYVKDIDKYEMLVQCFEYEREYKGTKNFD 200
Cdd:pfam13023  81 EREAAERIFGLLPED----QGEELLALWDEFEARETPEAKFAKDLDKLEPLLQNLEYEGDSWAAFEAD 144
YfbR COG1896
5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and ...
48-191 8.85e-29

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


Pssm-ID: 441500  Cd Length: 162  Bit Score: 106.10  E-value: 8.85e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319719   48 ILAFLNVVQQLK-IQRRTGYLDlgiKECESISDHMYRLSIITML---IKDSRVNRDKCVRIALVHDIAESLVGDITPVDP 123
Cdd:COG1896   1 QLDFLAELDRLKlIKRWGLLRN---SRPENVAEHSWHVALIAHLladIANEGVDPERVAKMALLHDLVEIDTGDIPTPVK 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6319719  124 IGKEEKHRREWETIKYLCNALIKPYneiaAKEIMDDWLAYENVTSLEARYVKDIDKYEMLVQCFEYER 191
Cdd:COG1896  78 YANEAKKEIERAAAERLFGLLPEEL----REEFRALWDEFEAGETPEARFVKAADKLEALLQALEEIG 141
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
79-183 4.45e-10

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 55.32  E-value: 4.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319719     79 DHMYRLSIITMLIKDS--RVNRDKCVRIALVHDIAESLVGDITPvdpiGKEEKHRREWETIKYLCNALIKPYNEIAAKEI 156
Cdd:pfam01966   3 EHSLRVALLARELAEElgELDRELLLLAALLHDIGKGPFGDEKP----EFEIFLGHAVVGAEILRELEKRLGLEDVLKLI 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 6319719    157 -----MDDWLAYENVTSLEARYVKDIDKYEML 183
Cdd:pfam01966  79 lehheSWEGAGYPEEISLEARIVKLADRLDAL 110
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
73-192 5.19e-10

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 55.77  E-value: 5.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319719      73 ECESISDHMYRLSIITMLIKDS--RVNRDKCVRIALVHDIAESLVGDITPVDPIGKEEKHRREWETIK--YLCNALIKPY 148
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAALAEElgLLDIELLLLAALLHDIGKPGTPDSFLVKTSVLEDHHFIGAEILLeeEEPRILEEIL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 6319719     149 NEIAAKEIMDDWLAYENVTSLEARYVKDIDKYEMLVQCFEYERE 192
Cdd:smart00471  81 RTAILSHHERPDGLRGEPITLEARIVKVADRLDALRADRRYRRV 124
YfbR-like pfam12917
5'-deoxynucleotidase YfbR-like; This entry contains Escherichia coli (strain K12) YfbR. It a 5 ...
75-201 1.11e-06

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: 47.50  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319719     75 ESISDHMYRLSIITM---LIKDSR----VNRDKCVRIALVHDIAESLVGDI-TPV---DPIGKEEKHRREWETIKYLCNA 143
Cdd:pfam12917  24 ENVAEHSLQVAMIAHalaLIENERfggnVDPERLAVLALYHDASEIITGDMpTPVkyfNPEIREAYKEVEKEAEERLLSM 103
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6319719    144 LIKPYneiaaKEIMDDWLAYENVTSLEARYVKDIDKYEMLVQCFEYEReyKGTKNFDD 201
Cdd:pfam12917 104 LPEEL-----REDYEPLLGDETIDPEEGRLVKAADKLSALIKCIEELR--AGNREFEE 154
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
87-203 5.72e-05

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 41.94  E-value: 5.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319719   87 ITMLIKDSRVNRDKCVRIALVHDIAESLVGDITPVDPIGKEEKH-------------RREWETIKYLCNALIKPYNEIAA 153
Cdd:cd00077  17 LAEELGLSEEDIELLRLAALLHDIGKPGTPDAITEEESELEKDHaivgaeilrelllEEVIKLIDELILAVDASHHERLD 96
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6319719  154 KEIMDDWLAYENVTsLEARYVKDIDKYEMLVQCFEYEREYKGTKNFDDFF 203
Cdd:cd00077  97 GLGYPDGLKGEEIT-LEARIVKLADRLDALRRDSREKRRRIAEEDLEELL 145
 
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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