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Conserved domains on  [gi|2102586674|ref|WP_223907691|]
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PHP domain-containing protein [Actinomyces capricornis]

Protein Classification

PHP domain-containing protein( domain architecture ID 11427581)

PHP (Polymerase and Histidinol Phosphatase) domain-containing protein similar to 3',5'-nucleoside bisphosphate phosphatase, which hydrolyzes 3',5'-bisphosphonucleosides (pGp, pCp, pUp, and pIp) to nucleoside 5'-phosphate and orthophosphate

Gene Ontology:  GO:0046872

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YciV COG0613
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ...
 1-254 1.43e-54

5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and metabolism];


:

Pssm-ID: 440378 [Multi-domain]  Cd Length: 188  Bit Score: 174.71  E-value: 1.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102586674   1 MRIDPHTHSVCSDGTDTPAQLMAAAARAGLDVVGLTDHDTTQGWAEAGRAVARTGVSLLRGVEISCAADGVSLHLLAYLP 80
Cdd:COG0613     2 MKIDLHVHTTASDGSLSPEELVARAKAAGLDVLAITDHDTVAGYEEAAEAAKELGLLVIPGVEISTRWEGREVHILGYGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102586674  81 RPDDADLSAAferarssratrarrmverlsadypitwedvvaqtgqgatIGRPHLADAlvaagcfdnrsaafagplsprs 160
Cdd:COG0613    82 DPEDPALEAL---------------------------------------LGIPVEKAE---------------------- 100

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102586674 161 pyyvrHWALDPVEACRLVRAAGGVPVAAHPRAASRqgRLVPDEVFEAMAQAGLAALEVDHRDHGPLQREQARTLATRLGL 240
Cdd:COG0613   101 -----REWLSLEEAIDLIREAGGVAVLAHPFRYKR--GRWLDDLLEELADAGLDGIEVYNGRHSPEDNERAAELAEEYGL 173

                         250
                  ....*....|....
gi 2102586674 241 GRSGSSDYHGTGKP 254
Cdd:COG0613   174 LATGGSDAHGPEKP 187
 
Name Accession Description Interval E-value
YciV COG0613
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ...
 1-254 1.43e-54

5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and metabolism];


Pssm-ID: 440378 [Multi-domain]  Cd Length: 188  Bit Score: 174.71  E-value: 1.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102586674   1 MRIDPHTHSVCSDGTDTPAQLMAAAARAGLDVVGLTDHDTTQGWAEAGRAVARTGVSLLRGVEISCAADGVSLHLLAYLP 80
Cdd:COG0613     2 MKIDLHVHTTASDGSLSPEELVARAKAAGLDVLAITDHDTVAGYEEAAEAAKELGLLVIPGVEISTRWEGREVHILGYGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102586674  81 RPDDADLSAAferarssratrarrmverlsadypitwedvvaqtgqgatIGRPHLADAlvaagcfdnrsaafagplsprs 160
Cdd:COG0613    82 DPEDPALEAL---------------------------------------LGIPVEKAE---------------------- 100

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102586674 161 pyyvrHWALDPVEACRLVRAAGGVPVAAHPRAASRqgRLVPDEVFEAMAQAGLAALEVDHRDHGPLQREQARTLATRLGL 240
Cdd:COG0613   101 -----REWLSLEEAIDLIREAGGVAVLAHPFRYKR--GRWLDDLLEELADAGLDGIEVYNGRHSPEDNERAAELAEEYGL 173

                         250
                  ....*....|....
gi 2102586674 241 GRSGSSDYHGTGKP 254
Cdd:COG0613   174 LATGGSDAHGPEKP 187
PHP_HisPPase_AMP cd07438
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) ...
 3-250 5.86e-47

Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) AMP bound; The PHP domain of this HisPPase family has an unknown function. It has a second domain inserted in the middle that binds adenosine 5-monophosphate (AMP). The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to give histidinol. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to the other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.


Pssm-ID: 213993 [Multi-domain]  Cd Length: 155  Bit Score: 154.09  E-value: 5.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102586674   3 IDPHTHSVCSDGTDTPAQLMAAAARAGLDVVGLTDHDTTQGWAEAGRAVARTGVSLLRGVEISCAADGVSLHLLAylprp 82
Cdd:cd07438     1 IDLHTHSTASDGTLSPEELVELAKEAGLKVLAITDHDTVAGLEEALAAAKELGIELIPGVEISTEYEGREVHILG----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102586674  83 ddadlsaaferarssratrarrmverlsadypitwedvvaqtgqgatigrphladalvaagcfdnrsaafagplsprspy 162
Cdd:cd07438       --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102586674 163 yvrhwalDPVEACRLVRAAGGVPVAAHPrAASRQGRLVPDEVFEAMAQAGLAALEVDHRDHGPLQREQARTLATRLGLGR 242
Cdd:cd07438    76 -------SPEEAIELIHAAGGVAVLAHP-GLYKLSRKKLEELIEELKEAGLDGIEVYHPYHSPEDRERLLELAKEYGLLV 147


                  ....*...
gi 2102586674 243 SGSSDYHG 250
Cdd:cd07438   148 TGGSDFHG 155
CehA_McbA_metalo NF038032
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ...
 2-65 3.28e-08

CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is found in several partially characterized metallohydrolases, including McbA and CehA. Both were studied as hydrolases of carbaryl, a xenobiotic compound that does not contain a phosphate group, suggesting that presuming members of this family to be phosphoesterases (like many PHP domain-containing proteins) may be incorrect.


Pssm-ID: 468321 [Multi-domain]  Cd Length: 315  Bit Score: 53.48  E-value: 3.28e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2102586674   2 RIDPHTHSVCSDGTDTPAQLMAAAARAGLDVVGLTDHDTTQGWAEAGRAVART-GVSLLRGVEIS 65
Cdd:NF038032    4 SGDLHIHTNHSDGPTTPEELARAALAEGLDVIALTDHNTISGRAYFAELLASErGLLVIPGMEVT 68
POLIIIAc smart00481
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ...
 4-65 4.69e-08

DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family of hypothetical proteins


Pssm-ID: 197753 [Multi-domain]  Cd Length: 67  Bit Score: 49.19  E-value: 4.69e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2102586674    4 DPHTHSVCS--DGTDTPAQLMAAAARAGLDVVGLTDHDTTQGWAEAGRAVARTGVSLLRGVEIS 65
Cdd:smart00481   1 DLHVHSDYSllDGALSPEELVKRAKELGLKAIAITDHGNLFGAVEFYKAAKKAGIKPIIGLEAN 64
PHP pfam02811
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ...
 6-64 4.08e-04

PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative phosphoesterase domain.


Pssm-ID: 460705 [Multi-domain]  Cd Length: 171  Bit Score: 40.22  E-value: 4.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2102586674   6 HTHSVCS--DGTDTPAQLMAAAARAGLDVVGLTDHDTTQGWAEAGRAVARTGVSLLRGVEI 64
Cdd:pfam02811   3 HVHSEYSllDGAARIEELVKRAKELGMPAIAITDHGNLFGAVEFYKAAKKAGIKPIIGCEV 63
 
Name Accession Description Interval E-value
YciV COG0613
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ...
 1-254 1.43e-54

5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and metabolism];


Pssm-ID: 440378 [Multi-domain]  Cd Length: 188  Bit Score: 174.71  E-value: 1.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102586674   1 MRIDPHTHSVCSDGTDTPAQLMAAAARAGLDVVGLTDHDTTQGWAEAGRAVARTGVSLLRGVEISCAADGVSLHLLAYLP 80
Cdd:COG0613     2 MKIDLHVHTTASDGSLSPEELVARAKAAGLDVLAITDHDTVAGYEEAAEAAKELGLLVIPGVEISTRWEGREVHILGYGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102586674  81 RPDDADLSAAferarssratrarrmverlsadypitwedvvaqtgqgatIGRPHLADAlvaagcfdnrsaafagplsprs 160
Cdd:COG0613    82 DPEDPALEAL---------------------------------------LGIPVEKAE---------------------- 100

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102586674 161 pyyvrHWALDPVEACRLVRAAGGVPVAAHPRAASRqgRLVPDEVFEAMAQAGLAALEVDHRDHGPLQREQARTLATRLGL 240
Cdd:COG0613   101 -----REWLSLEEAIDLIREAGGVAVLAHPFRYKR--GRWLDDLLEELADAGLDGIEVYNGRHSPEDNERAAELAEEYGL 173

                         250
                  ....*....|....
gi 2102586674 241 GRSGSSDYHGTGKP 254
Cdd:COG0613   174 LATGGSDAHGPEKP 187
PHP_HisPPase_AMP cd07438
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) ...
 3-250 5.86e-47

Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) AMP bound; The PHP domain of this HisPPase family has an unknown function. It has a second domain inserted in the middle that binds adenosine 5-monophosphate (AMP). The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to give histidinol. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to the other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.


Pssm-ID: 213993 [Multi-domain]  Cd Length: 155  Bit Score: 154.09  E-value: 5.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102586674   3 IDPHTHSVCSDGTDTPAQLMAAAARAGLDVVGLTDHDTTQGWAEAGRAVARTGVSLLRGVEISCAADGVSLHLLAylprp 82
Cdd:cd07438     1 IDLHTHSTASDGTLSPEELVELAKEAGLKVLAITDHDTVAGLEEALAAAKELGIELIPGVEISTEYEGREVHILG----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102586674  83 ddadlsaaferarssratrarrmverlsadypitwedvvaqtgqgatigrphladalvaagcfdnrsaafagplsprspy 162
Cdd:cd07438       --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102586674 163 yvrhwalDPVEACRLVRAAGGVPVAAHPrAASRQGRLVPDEVFEAMAQAGLAALEVDHRDHGPLQREQARTLATRLGLGR 242
Cdd:cd07438    76 -------SPEEAIELIHAAGGVAVLAHP-GLYKLSRKKLEELIEELKEAGLDGIEVYHPYHSPEDRERLLELAKEYGLLV 147


                  ....*...
gi 2102586674 243 SGSSDYHG 250
Cdd:cd07438   148 TGGSDFHG 155
PHP_HisPPase cd07432
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ...
 3-84 3.24e-12

Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to produce histidinol. HisPPase can be classified into two types: the bifunctional HisPPase found in proteobacteria that belongs to the DDDD superfamily and the monofunctional Bacillus subtilis type that is a member of the PHP family. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.


Pssm-ID: 213987 [Multi-domain]  Cd Length: 129  Bit Score: 62.26  E-value: 3.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102586674   3 IDPHTHSVCS-DGTDTPAQLMAAAARAGLDVVGLTDHDTTQGWAEAGRAVARTGVSLLRGVEIScaadgvslhlLAYLPR 81
Cdd:cd07432     1 ADLHIHSVFSpDSDMTPEEIVERAIELGLDGIAITDHNTIDGAEEALKEAYKDGLLVIPGVEVT----------LVVLAH 70


                  ...
gi 2102586674  82 PDD 84
Cdd:cd07432    71 PDR 73
CehA_McbA_metalo NF038032
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ...
 2-65 3.28e-08

CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is found in several partially characterized metallohydrolases, including McbA and CehA. Both were studied as hydrolases of carbaryl, a xenobiotic compound that does not contain a phosphate group, suggesting that presuming members of this family to be phosphoesterases (like many PHP domain-containing proteins) may be incorrect.


Pssm-ID: 468321 [Multi-domain]  Cd Length: 315  Bit Score: 53.48  E-value: 3.28e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2102586674   2 RIDPHTHSVCSDGTDTPAQLMAAAARAGLDVVGLTDHDTTQGWAEAGRAVART-GVSLLRGVEIS 65
Cdd:NF038032    4 SGDLHIHTNHSDGPTTPEELARAALAEGLDVIALTDHNTISGRAYFAELLASErGLLVIPGMEVT 68
POLIIIAc smart00481
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ...
 4-65 4.69e-08

DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family of hypothetical proteins


Pssm-ID: 197753 [Multi-domain]  Cd Length: 67  Bit Score: 49.19  E-value: 4.69e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2102586674    4 DPHTHSVCS--DGTDTPAQLMAAAARAGLDVVGLTDHDTTQGWAEAGRAVARTGVSLLRGVEIS 65
Cdd:smart00481   1 DLHVHSDYSllDGALSPEELVKRAKELGLKAIAITDHGNLFGAVEFYKAAKKAGIKPIIGLEAN 64
PHP cd07309
Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2 ...
 3-65 1.53e-05

Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. PHP in polymerases has trinuclear zinc/magnesium dependent proofreading activity. It has also been shown that the PHP domain functions in DNA repair. The PHP structures have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.


Pssm-ID: 213985 [Multi-domain]  Cd Length: 88  Bit Score: 42.41  E-value: 1.53e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2102586674   3 IDPHTHSVCSDG-TDTPAQLMAAAARAGLDVVGLTDHDTTQGWAEAG--------RAVARTGVSLLRGVEIS 65
Cdd:cd07309     1 VDLHTHTVFSDGdHAKLTELVDKAKELGPDALAITDHGNLRGLAEFNtagk*nhiKAAEAAGIKIIIGSEVN 72
HIS2 COG1387
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ...
 1-38 3.22e-05

Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and metabolism, General function prediction only]; Histidinol phosphatase or related hydrolase of the PHP family is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 440997 [Multi-domain]  Cd Length: 232  Bit Score: 43.99  E-value: 3.22e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2102586674   1 MRIDPHTHSVCSDGTDTPAQLMAAAARAGLDVVGLTDH 38
Cdd:COG1387     1 MRGDLHTHTTYSDGEGTIEEMVEAAIELGLEYIAITDH 38
PHP_HisPPase_Chlorobi_like cd12112
Polymerase and Histidinol Phosphatase domain of Chlorobi like; The PHP (also called histidinol ...
 4-65 8.47e-05

Polymerase and Histidinol Phosphatase domain of Chlorobi like; The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. Chlorobi PHP is uncharacterized protein. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to produce histidinol. The HisPPase can be classified into two types: the bifunctional Hisppase found in proteobacteria that belongs to the DDDD superfamily and the monofunctional Bacillus subtilis type that is a member of the PHP family. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.


Pssm-ID: 213996 [Multi-domain]  Cd Length: 235  Bit Score: 42.70  E-value: 8.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2102586674   4 DPHTHSVCSDGTDTPAQLMAAAARAGLDVVGLTDH-------------DTTQGWAEAGRAVARTGVSLLRGVEIS 65
Cdd:cd12112    16 DFHTHTVFSDGHVWPEIRVREAWREGLDAIAITEHieyrphkediphpDRNRSYKIAKEAAESKGLLIIPGAEIT 90
PHP pfam02811
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ...
 6-64 4.08e-04

PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative phosphoesterase domain.


Pssm-ID: 460705 [Multi-domain]  Cd Length: 171  Bit Score: 40.22  E-value: 4.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2102586674   6 HTHSVCS--DGTDTPAQLMAAAARAGLDVVGLTDHDTTQGWAEAGRAVARTGVSLLRGVEI 64
Cdd:pfam02811   3 HVHSEYSllDGAARIEELVKRAKELGMPAIAITDHGNLFGAVEFYKAAKKAGIKPIIGCEV 63
PHP_PolIIIA cd07431
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III; ...
 6-78 9.36e-04

Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III; PolIIIAs that contain an N-terminal PHP domain have been classified into four basic groups based on genome composition, phylogenetic, and domain structural analysis: polC, dnaE1, dnaE2, and dnaE3. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. DNA polymerase III holoenzyme is one of the five eubacterial DNA polymerases that is responsible for the replication of the DNA duplex. The alpha subunit of DNA polymerase III core enzyme catalyzes the reaction for polymerizing both DNA strands. The PolIIIA PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination, and like other PHP structures, exhibits a distorted (beta/alpha) 7 barrel and coordinates up to 3 metals. Initially, it was proposed that PHP region might be involved in pyrophosphate hydrolysis, but such activity has not been found. It has been shown that the PHP domain of PolIIIA has a trinuclear metal complex and is capable of proofreading activity.


Pssm-ID: 213986 [Multi-domain]  Cd Length: 179  Bit Score: 39.11  E-value: 9.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2102586674   6 HTHSVCS--DGTDTPAQLMAAAARAGLDVVGLTDHDTTQGWAEAGRAVARTGVSLLRGVEISCAADGVSLHLLAY 78
Cdd:cd07431     4 HVHSSYSllDSAIRPEDLVARAKELGYSALALTDRNVLYGAVRFYKACKKAGIKPIIGLELTVEGDGEPYPLLLL 78
 
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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