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Conserved domains on  [gi|494931925|ref|WP_007657959|]
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HD domain-containing protein [Pontibacter sp. BAB1700]

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.
15-177 5.02e-52

HD domain; HD domains are metal dependent phosphohydrolases.


:

Pssm-ID: 432939  Cd Length: 163  Bit Score: 164.70  E-value: 5.02e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494931925   15 AEKIKFEMRHSWLSNG--RQESVAEHTWRMSLMAVLLEPYLEQrVDMARLLKMIIIHDLVEAEAGDVPAFDivnEETKLL 92
Cdd:pfam13023   1 ADKLKFVKRQGWLQDGrvRPESVAEHSWRMALMAMLLAEYAGP-VDIARVIKMALIHDLVEILAGDIIPYD---GVAKEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494931925   93 KQQREQQAILNLRDQLRESTGQEIYDLWYEFEEKETYEAKVANALDKLEVQIQHNHADISTWIEIEREFVFLMGRH-TSF 171
Cdd:pfam13023  77 KEEREREAAERIFGLLPEDQGEELLALWDEFEARETPEAKFAKDLDKLEPLLQNLEYEGDSWAAFEADLSQFYGRNsTIL 156

                  ....*.
gi 494931925  172 DKGLEE 177
Cdd:pfam13023 157 AEGSPE 162
 
Name Accession Description Interval E-value
HD_3 pfam13023
HD domain; HD domains are metal dependent phosphohydrolases.
15-177 5.02e-52

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 432939  Cd Length: 163  Bit Score: 164.70  E-value: 5.02e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494931925   15 AEKIKFEMRHSWLSNG--RQESVAEHTWRMSLMAVLLEPYLEQrVDMARLLKMIIIHDLVEAEAGDVPAFDivnEETKLL 92
Cdd:pfam13023   1 ADKLKFVKRQGWLQDGrvRPESVAEHSWRMALMAMLLAEYAGP-VDIARVIKMALIHDLVEILAGDIIPYD---GVAKEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494931925   93 KQQREQQAILNLRDQLRESTGQEIYDLWYEFEEKETYEAKVANALDKLEVQIQHNHADISTWIEIEREFVFLMGRH-TSF 171
Cdd:pfam13023  77 KEEREREAAERIFGLLPEDQGEELLALWDEFEARETPEAKFAKDLDKLEPLLQNLEYEGDSWAAFEADLSQFYGRNsTIL 156

                  ....*.
gi 494931925  172 DKGLEE 177
Cdd:pfam13023 157 AEGSPE 162
YfbR COG1896
5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and ...
8-163 5.63e-45

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


Pssm-ID: 441500  Cd Length: 162  Bit Score: 146.93  E-value: 5.63e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494931925   8 VLEVLTLAEKIKFEMRHSWLSNGRQESVAEHTWRMSLMAVLLEPYLEQRVDMARLLKMIIIHDLVEAEAGDVPAFDIVNE 87
Cdd:COG1896    1 QLDFLAELDRLKLIKRWGLLRNSRPENVAEHSWHVALIAHLLADIANEGVDPERVAKMALLHDLVEIDTGDIPTPVKYAN 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494931925  88 EtklLKQQREQQAILNLRDQLRESTGQEIYDLWYEFEEKETYEAKVANALDKLEVQIQHNHADISTWIEIEREFVF 163
Cdd:COG1896   81 E---AKKEIERAAAERLFGLLPEELREEFRALWDEFEAGETPEARFVKAADKLEALLQALEEIGAGNKENTFEQAY 153
 
Name Accession Description Interval E-value
HD_3 pfam13023
HD domain; HD domains are metal dependent phosphohydrolases.
15-177 5.02e-52

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 432939  Cd Length: 163  Bit Score: 164.70  E-value: 5.02e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494931925   15 AEKIKFEMRHSWLSNG--RQESVAEHTWRMSLMAVLLEPYLEQrVDMARLLKMIIIHDLVEAEAGDVPAFDivnEETKLL 92
Cdd:pfam13023   1 ADKLKFVKRQGWLQDGrvRPESVAEHSWRMALMAMLLAEYAGP-VDIARVIKMALIHDLVEILAGDIIPYD---GVAKEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494931925   93 KQQREQQAILNLRDQLRESTGQEIYDLWYEFEEKETYEAKVANALDKLEVQIQHNHADISTWIEIEREFVFLMGRH-TSF 171
Cdd:pfam13023  77 KEEREREAAERIFGLLPEDQGEELLALWDEFEARETPEAKFAKDLDKLEPLLQNLEYEGDSWAAFEADLSQFYGRNsTIL 156

                  ....*.
gi 494931925  172 DKGLEE 177
Cdd:pfam13023 157 AEGSPE 162
YfbR COG1896
5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and ...
8-163 5.63e-45

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


Pssm-ID: 441500  Cd Length: 162  Bit Score: 146.93  E-value: 5.63e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494931925   8 VLEVLTLAEKIKFEMRHSWLSNGRQESVAEHTWRMSLMAVLLEPYLEQRVDMARLLKMIIIHDLVEAEAGDVPAFDIVNE 87
Cdd:COG1896    1 QLDFLAELDRLKLIKRWGLLRNSRPENVAEHSWHVALIAHLLADIANEGVDPERVAKMALLHDLVEIDTGDIPTPVKYAN 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494931925  88 EtklLKQQREQQAILNLRDQLRESTGQEIYDLWYEFEEKETYEAKVANALDKLEVQIQHNHADISTWIEIEREFVF 163
Cdd:COG1896   81 E---AKKEIERAAAERLFGLLPEELREEFRALWDEFEAGETPEARFVKAADKLEALLQALEEIGAGNKENTFEQAY 153
YfbR-like pfam12917
5'-deoxynucleotidase YfbR-like; This entry contains Escherichia coli (strain K12) YfbR. It a 5 ...
29-140 3.90e-04

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: 39.80  E-value: 3.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494931925   29 NGRQESVAEHTWRMSL----MAVLLEPYLEQRVDMARLLKMIIIHDLVEAEAGDVPAFdiV---NEETKLLKQQREQQAI 101
Cdd:pfam12917  20 NTRPENVAEHSLQVAMiahaLALIENERFGGNVDPERLAVLALYHDASEIITGDMPTP--VkyfNPEIREAYKEVEKEAE 97
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 494931925  102 LNLRDQLRESTgQEIYDLWYEFEEKETYEAKVANALDKL 140
Cdd:pfam12917  98 ERLLSMLPEEL-REDYEPLLGDETIDPEEGRLVKAADKL 135
 
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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