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Conserved domains on  [gi|2185189940|ref|WP_236578892|]
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MULTISPECIES: PHP domain-containing protein [Sutterella]

Protein Classification

PHP domain-containing protein( domain architecture ID 11427581)

PHP (Polymerase and Histidinol Phosphatase) domain-containing protein has an invariant histidine that is involved in metal ion coordination, similar to Bifidobacterium adolescentis metal-dependent phosphoesterase

CATH:  3.20.20.140
Gene Ontology:  GO:0046872
PubMed:  9685491
SCOP:  4000443

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nside_bi_sphtase super family cl49536
3',5'-nucleoside bisphosphate phosphatase;
1-276 1.07e-113

3',5'-nucleoside bisphosphate phosphatase;


The actual alignment was detected with superfamily member NF041577:

Pssm-ID: 469462 [Multi-domain]  Cd Length: 276  Bit Score: 328.79  E-value: 1.07e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940   1 MTIDLHMHSNASDGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERLGIAFVPGIEISTRWGQKSIHVAAYNL 80
Cdd:NF041577    2 LNVDLHCHSTVSDGLLSPAEVVRRAAARGVELLALTDHDDVGGLAEARAAAAELGLRFVNGVEISVTWGGHTVHIVGLGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940  81 NPNTEAFKAFFKGVDKKRIERGERMGKLLAACGCKGAFEGAMALAVHPGSLSRTHFAQWLLDAGYVENYAQAFDKYLKPG 160
Cdd:NF041577   82 DPAHPALVAGLASIRAGRIERARRMAASLAKVGIEGAFEGAMRYADNPEMISRTHFARFLVETGVAKDVRSVFKKYLVKG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940 161 KPGYVQIEWPEIRDAVRFVKSEGGTASLAHPGRYNLKEGWMiDELLTAFQGAGGEAIEVASGSQTRDDDALFAAKAKQYG 240
Cdd:NF041577  162 KPGYVEHEWASLADAVGWIRAAGGVAVIAHPGRYDLGRTTL-ERLLTEFKALGGEAIEVVSGSHSADDVGRFARLAREFG 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2185189940 241 FLASTGSDWHSPRSPRPTPGSQPQVPADLTPIWTKF 276
Cdd:NF041577  241 LLASRGSDFHGPGESYRDLGRLPPLPPGCTPVWERW 276
 
Name Accession Description Interval E-value
nside_bi_sphtase NF041577
3',5'-nucleoside bisphosphate phosphatase;
1-276 1.07e-113

3',5'-nucleoside bisphosphate phosphatase;


Pssm-ID: 469462 [Multi-domain]  Cd Length: 276  Bit Score: 328.79  E-value: 1.07e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940   1 MTIDLHMHSNASDGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERLGIAFVPGIEISTRWGQKSIHVAAYNL 80
Cdd:NF041577    2 LNVDLHCHSTVSDGLLSPAEVVRRAAARGVELLALTDHDDVGGLAEARAAAAELGLRFVNGVEISVTWGGHTVHIVGLGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940  81 NPNTEAFKAFFKGVDKKRIERGERMGKLLAACGCKGAFEGAMALAVHPGSLSRTHFAQWLLDAGYVENYAQAFDKYLKPG 160
Cdd:NF041577   82 DPAHPALVAGLASIRAGRIERARRMAASLAKVGIEGAFEGAMRYADNPEMISRTHFARFLVETGVAKDVRSVFKKYLVKG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940 161 KPGYVQIEWPEIRDAVRFVKSEGGTASLAHPGRYNLKEGWMiDELLTAFQGAGGEAIEVASGSQTRDDDALFAAKAKQYG 240
Cdd:NF041577  162 KPGYVEHEWASLADAVGWIRAAGGVAVIAHPGRYDLGRTTL-ERLLTEFKALGGEAIEVVSGSHSADDVGRFARLAREFG 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2185189940 241 FLASTGSDWHSPRSPRPTPGSQPQVPADLTPIWTKF 276
Cdd:NF041577  241 LLASRGSDFHGPGESYRDLGRLPPLPPGCTPVWERW 276
YciV COG0613
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ...
 1-255 3.99e-61

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


Pssm-ID: 440378 [Multi-domain]  Cd Length: 188  Bit Score: 191.66  E-value: 3.99e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940   1 MTIDLHMHSNASDGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERLGIAFVPGIEISTRWGQKSIHVAAYNL 80
Cdd:COG0613     2 MKIDLHVHTTASDGSLSPEELVARAKAAGLDVLAITDHDTVAGYEEAAEAAKELGLLVIPGVEISTRWEGREVHILGYGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940  81 NPNTEAFKAFFkGVDKKRIERgermgkllaacgckgafegamalavhpgslsrthfaqwlldagyvenyaqafdkylkpg 160
Cdd:COG0613    82 DPEDPALEALL-GIPVEKAER----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940 161 kpgyvqiEWPEIRDAVRFVKSEGGTASLAHPGRYNLkeGWMIDELLTAFQGAGGEAIEVASGSQTRDDDALFAAKAKQYG 240
Cdd:COG0613   102 -------EWLSLEEAIDLIREAGGVAVLAHPFRYKR--GRWLDDLLEELADAGLDGIEVYNGRHSPEDNERAAELAEEYG 172

                         250
                  ....*....|....*
gi 2185189940 241 FLASTGSDWHSPRSP 255
Cdd:COG0613   173 LLATGGSDAHGPEKP 187
PHP_HisPPase_AMP cd07438
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) ...
 3-250 9.50e-57

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: 179.51  E-value: 9.50e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940   3 IDLHMHSNASDGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERLGIAFVPGIEISTRWGQKSIHvaaynlnp 82
Cdd:cd07438     1 IDLHTHSTASDGTLSPEELVELAKEAGLKVLAITDHDTVAGLEEALAAAKELGIELIPGVEISTEYEGREVH-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940  83 nteafkaffkgvdkkriergermgkLLAacgckgafegamalavhpgslsrthfaqwlldagyvenyaqafdkylkpgkp 162
Cdd:cd07438    73 -------------------------ILG---------------------------------------------------- 75

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940 163 gyvqiewpEIRDAVRFVKSEGGTASLAHPGRYNLKEGWMiDELLTAFQGAGGEAIEVASGSQTRDDDALFAAKAKQYGFL 242
Cdd:cd07438    76 --------SPEEAIELIHAAGGVAVLAHPGLYKLSRKKL-EELIEELKEAGLDGIEVYHPYHSPEDRERLLELAKEYGLL 146


                  ....*...
gi 2185189940 243 ASTGSDWH 250
Cdd:cd07438   147 VTGGSDFH 154
POLIIIAc smart00481
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ...
 4-68 7.29e-16

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: 70.37  E-value: 7.29e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2185189940    4 DLHMHSNAS--DGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERLGIAFVPGIEISTRW 68
Cdd:smart00481   1 DLHVHSDYSllDGALSPEELVKRAKELGLKAIAITDHGNLFGAVEFYKAAKKAGIKPIIGLEANIVD 67
CehA_McbA_metalo NF038032
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ...
 4-260 8.34e-15

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: 73.13  E-value: 8.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940   4 DLHMHSNASDGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERL-GIAFVPGIEISTRWGqksiHVAAYNLNP 82
Cdd:NF038032    6 DLHIHTNHSDGPTTPEELARAALAEGLDVIALTDHNTISGRAYFAELLASErGLLVIPGMEVTTFWG----HMNLLGLDL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940  83 NTeafkaffkgvdkkriergermgkllaacgckgafegamalavhpgslsrthFAQWlldagyvenyaqafdkylkpgkp 162
Cdd:NF038032   82 DP---------------------------------------------------YIDW----------------------- 87

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940 163 GYVQIEWPEIRDAVRFVKSEGGTASLAHPGRY--NLKEGWMIDELLTAFQGAggEAIEVASGSQTRDDDAlfAAKAKQYG 240
Cdd:NF038032   88 RNTDPGSPDIDEVIDEAHRQGGLVGIAHPFSPggPLCTGCGWEALIDDLGKV--DAIEVWNTPDPAPTNE--RALALWYH 163

                         250       260
                  ....*....|....*....|....*..
gi 2185189940 241 FL-------ASTGSDWHSPrsPRPTPG 260
Cdd:NF038032  164 LLnegfritATGGSDAHDD--FDERPG 188
PHP pfam02811
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ...
 4-158 8.29e-09

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


Pssm-ID: 460705 [Multi-domain]  Cd Length: 171  Bit Score: 53.70  E-value: 8.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940   4 DLHMHSNAS--DGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERLGIAFVPGIEISTRWGQK---------- 71
Cdd:pfam02811   1 HLHVHSEYSllDGAARIEELVKRAKELGMPAIAITDHGNLFGAVEFYKAAKKAGIKPIIGCEVYVAPGSReetekllaky 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940  72 ------SIHVAAYnLNPNTEAFKAFFKGvDKKRIERgermgKLLAACgckgaFEGAMALAvhPGSLSrtHFAQWLLDAGY 145
Cdd:pfam02811  81 fdlvllAVHEVGY-KNLIKLSSRAYLEG-FKPRIDK-----ELLEEY-----FEGLIALS--GCVLG--HLDLILLAPGD 144

                         170
                  ....*....|...
gi 2185189940 146 VENYAQAFDKYLK 158
Cdd:pfam02811 145 YEEAEELAEEYLE 157
PRK06361 PRK06361
histidinol phosphate phosphatase domain-containing protein;
7-64 3.80e-05

histidinol phosphate phosphatase domain-containing protein;


Pssm-ID: 180543 [Multi-domain]  Cd Length: 212  Bit Score: 43.79  E-value: 3.80e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2185189940   7 MHSNASDGILPPAEVVRLCAGNGVKLMSLTDH-------DTMKGIEEARAEAER-LGIAFVPGIEI 64
Cdd:PRK06361    1 THTIFSDGELIPSELVRRARVLGYRAIAITDHadasnleEILEKLVRAAEELELyWDIEVIPGVEL 66
 
Name Accession Description Interval E-value
nside_bi_sphtase NF041577
3',5'-nucleoside bisphosphate phosphatase;
1-276 1.07e-113

3',5'-nucleoside bisphosphate phosphatase;


Pssm-ID: 469462 [Multi-domain]  Cd Length: 276  Bit Score: 328.79  E-value: 1.07e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940   1 MTIDLHMHSNASDGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERLGIAFVPGIEISTRWGQKSIHVAAYNL 80
Cdd:NF041577    2 LNVDLHCHSTVSDGLLSPAEVVRRAAARGVELLALTDHDDVGGLAEARAAAAELGLRFVNGVEISVTWGGHTVHIVGLGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940  81 NPNTEAFKAFFKGVDKKRIERGERMGKLLAACGCKGAFEGAMALAVHPGSLSRTHFAQWLLDAGYVENYAQAFDKYLKPG 160
Cdd:NF041577   82 DPAHPALVAGLASIRAGRIERARRMAASLAKVGIEGAFEGAMRYADNPEMISRTHFARFLVETGVAKDVRSVFKKYLVKG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940 161 KPGYVQIEWPEIRDAVRFVKSEGGTASLAHPGRYNLKEGWMiDELLTAFQGAGGEAIEVASGSQTRDDDALFAAKAKQYG 240
Cdd:NF041577  162 KPGYVEHEWASLADAVGWIRAAGGVAVIAHPGRYDLGRTTL-ERLLTEFKALGGEAIEVVSGSHSADDVGRFARLAREFG 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2185189940 241 FLASTGSDWHSPRSPRPTPGSQPQVPADLTPIWTKF 276
Cdd:NF041577  241 LLASRGSDFHGPGESYRDLGRLPPLPPGCTPVWERW 276
YciV COG0613
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ...
 1-255 3.99e-61

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


Pssm-ID: 440378 [Multi-domain]  Cd Length: 188  Bit Score: 191.66  E-value: 3.99e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940   1 MTIDLHMHSNASDGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERLGIAFVPGIEISTRWGQKSIHVAAYNL 80
Cdd:COG0613     2 MKIDLHVHTTASDGSLSPEELVARAKAAGLDVLAITDHDTVAGYEEAAEAAKELGLLVIPGVEISTRWEGREVHILGYGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940  81 NPNTEAFKAFFkGVDKKRIERgermgkllaacgckgafegamalavhpgslsrthfaqwlldagyvenyaqafdkylkpg 160
Cdd:COG0613    82 DPEDPALEALL-GIPVEKAER----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940 161 kpgyvqiEWPEIRDAVRFVKSEGGTASLAHPGRYNLkeGWMIDELLTAFQGAGGEAIEVASGSQTRDDDALFAAKAKQYG 240
Cdd:COG0613   102 -------EWLSLEEAIDLIREAGGVAVLAHPFRYKR--GRWLDDLLEELADAGLDGIEVYNGRHSPEDNERAAELAEEYG 172

                         250
                  ....*....|....*
gi 2185189940 241 FLASTGSDWHSPRSP 255
Cdd:COG0613   173 LLATGGSDAHGPEKP 187
PHP_HisPPase_AMP cd07438
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) ...
 3-250 9.50e-57

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: 179.51  E-value: 9.50e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940   3 IDLHMHSNASDGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERLGIAFVPGIEISTRWGQKSIHvaaynlnp 82
Cdd:cd07438     1 IDLHTHSTASDGTLSPEELVELAKEAGLKVLAITDHDTVAGLEEALAAAKELGIELIPGVEISTEYEGREVH-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940  83 nteafkaffkgvdkkriergermgkLLAacgckgafegamalavhpgslsrthfaqwlldagyvenyaqafdkylkpgkp 162
Cdd:cd07438    73 -------------------------ILG---------------------------------------------------- 75

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940 163 gyvqiewpEIRDAVRFVKSEGGTASLAHPGRYNLKEGWMiDELLTAFQGAGGEAIEVASGSQTRDDDALFAAKAKQYGFL 242
Cdd:cd07438    76 --------SPEEAIELIHAAGGVAVLAHPGLYKLSRKKL-EELIEELKEAGLDGIEVYHPYHSPEDRERLLELAKEYGLL 146


                  ....*...
gi 2185189940 243 ASTGSDWH 250
Cdd:cd07438   147 VTGGSDFH 154
PHP_HisPPase cd07432
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ...
 3-113 1.15e-19

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: 82.67  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940   3 IDLHMHSNAS-DGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERLGIAFVPGIEIstrwgqkSIHVAA---- 77
Cdd:cd07432     1 ADLHIHSVFSpDSDMTPEEIVERAIELGLDGIAITDHNTIDGAEEALKEAYKDGLLVIPGVEV-------TLVVLAhpdr 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2185189940  78 -YNLNPNTEAFKAFFKGVD-------KKRIERGERMGKLLAACG 113
Cdd:cd07432    74 pSRYGLSDLILKPLIKNGDaievnnsRLRYGLNNLAAKRYAELG 117
POLIIIAc smart00481
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ...
 4-68 7.29e-16

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: 70.37  E-value: 7.29e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2185189940    4 DLHMHSNAS--DGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERLGIAFVPGIEISTRW 68
Cdd:smart00481   1 DLHVHSDYSllDGALSPEELVKRAKELGLKAIAITDHGNLFGAVEFYKAAKKAGIKPIIGLEANIVD 67
CehA_McbA_metalo NF038032
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ...
 4-260 8.34e-15

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: 73.13  E-value: 8.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940   4 DLHMHSNASDGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERL-GIAFVPGIEISTRWGqksiHVAAYNLNP 82
Cdd:NF038032    6 DLHIHTNHSDGPTTPEELARAALAEGLDVIALTDHNTISGRAYFAELLASErGLLVIPGMEVTTFWG----HMNLLGLDL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940  83 NTeafkaffkgvdkkriergermgkllaacgckgafegamalavhpgslsrthFAQWlldagyvenyaqafdkylkpgkp 162
Cdd:NF038032   82 DP---------------------------------------------------YIDW----------------------- 87

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940 163 GYVQIEWPEIRDAVRFVKSEGGTASLAHPGRY--NLKEGWMIDELLTAFQGAggEAIEVASGSQTRDDDAlfAAKAKQYG 240
Cdd:NF038032   88 RNTDPGSPDIDEVIDEAHRQGGLVGIAHPFSPggPLCTGCGWEALIDDLGKV--DAIEVWNTPDPAPTNE--RALALWYH 163

                         250       260
                  ....*....|....*....|....*..
gi 2185189940 241 FL-------ASTGSDWHSPrsPRPTPG 260
Cdd:NF038032  164 LLnegfritATGGSDAHDD--FDERPG 188
PHP cd07309
Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2 ...
 3-70 1.49e-09

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: 53.97  E-value: 1.49e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2185189940   3 IDLHMHSNASDG-ILPPAEVVRLCAGNGVKLMSLTDH--------DTMKGIEEARAEAERLGIAFVPGIEIS-TRWGQ 70
Cdd:cd07309     1 VDLHTHTVFSDGdHAKLTELVDKAKELGPDALAITDHgnlrglaeFNTAGK*NHIKAAEAAGIKIIIGSEVNlTVLAH 78
PHP pfam02811
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ...
 4-158 8.29e-09

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


Pssm-ID: 460705 [Multi-domain]  Cd Length: 171  Bit Score: 53.70  E-value: 8.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940   4 DLHMHSNAS--DGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERLGIAFVPGIEISTRWGQK---------- 71
Cdd:pfam02811   1 HLHVHSEYSllDGAARIEELVKRAKELGMPAIAITDHGNLFGAVEFYKAAKKAGIKPIIGCEVYVAPGSReetekllaky 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940  72 ------SIHVAAYnLNPNTEAFKAFFKGvDKKRIERgermgKLLAACgckgaFEGAMALAvhPGSLSrtHFAQWLLDAGY 145
Cdd:pfam02811  81 fdlvllAVHEVGY-KNLIKLSSRAYLEG-FKPRIDK-----ELLEEY-----FEGLIALS--GCVLG--HLDLILLAPGD 144

                         170
                  ....*....|...
gi 2185189940 146 VENYAQAFDKYLK 158
Cdd:pfam02811 145 YEEAEELAEEYLE 157
HIS2 COG1387
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ...
 1-64 1.19e-08

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: 54.39  E-value: 1.19e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2185189940   1 MTIDLHMHSNASDGILPPAEVVRLCAGNGVKLMSLTDHD---------TMKGIEEARAEAERL-----GIAFVPGIEI 64
Cdd:COG1387     1 MRGDLHTHTTYSDGEGTIEEMVEAAIELGLEYIAITDHSpslfvanglSEERLLEYLEEIEELnekypDIKILKGIEV 78
PHP_HisPPase_Thermotoga_like cd12111
Polymerase and Histidinol Phosphatase domain of Thermotoga like; The PHP (also called ...
 4-154 1.02e-06

Polymerase and Histidinol Phosphatase domain of Thermotoga 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. Thermotoga PHP is an uncharacterized protein. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to give 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: 213995 [Multi-domain]  Cd Length: 226  Bit Score: 48.57  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940   4 DLHMHSNASDGILPPAEVVRLCAGNGVKLMSLTDH-------------------------DTMKGIEEARAEA-ERLGIA 57
Cdd:cd12111     5 DFHIHTTYSDGALSLSEVVDLYGQHGFDVIAITDHvvdrasligkfpqgthpgvteanfeDYMEALKVEAKRAwEKYEMI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940  58 FVPGIEISTrwgqksihvaaynlnpNTEAFKAFfkGVD-KKRIERGERMGKLLAACgckgAFEGAMALAVHP--GSLSRT 134
Cdd:cd12111    85 VIPGVELTN----------------NTDSYHIL--GIDvKEYIDPCLSVEEIIAEI----HKQGGIAVAAHPhrKNLDGE 142

                         170       180
                  ....*....|....*....|
gi 2185189940 135 HFAQWLLDagYVENYAQAFD 154
Cdd:cd12111   143 HNSLYLWN--NRERYKHLFD 160
DnaE COG0587
DNA polymerase III, alpha subunit [Replication, recombination and repair];
1-64 1.08e-06

DNA polymerase III, alpha subunit [Replication, recombination and repair];


Pssm-ID: 440352 [Multi-domain]  Cd Length: 1050  Bit Score: 49.68  E-value: 1.08e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2185189940    1 MTID---LHMHSNAS--DGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERLGIAFVPGIEI 64
Cdd:COG0587      1 MSPSfvhLHVHSEYSllDGASRPEELVARAAELGMPALAITDHGNLFGAVRFYKAAKKAGIKPIIGCEL 69
PHP_HisPPase_Chlorobi_like cd12112
Polymerase and Histidinol Phosphatase domain of Chlorobi like; The PHP (also called histidinol ...
 4-67 7.64e-06

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: 46.17  E-value: 7.64e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2185189940   4 DLHMHSNASDGILPPAEVVRLCAGNGVKLMSLTDH-------------DTMKGIEEARAEAERLGIAFVPGIEIsTR 67
Cdd:cd12112    16 DFHTHTVFSDGHVWPEIRVREAWREGLDAIAITEHieyrphkediphpDRNRSYKIAKEAAESKGLLIIPGAEI-TR 91
PRK06361 PRK06361
histidinol phosphate phosphatase domain-containing protein;
7-64 3.80e-05

histidinol phosphate phosphatase domain-containing protein;


Pssm-ID: 180543 [Multi-domain]  Cd Length: 212  Bit Score: 43.79  E-value: 3.80e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2185189940   7 MHSNASDGILPPAEVVRLCAGNGVKLMSLTDH-------DTMKGIEEARAEAER-LGIAFVPGIEI 64
Cdd:PRK06361    1 THTIFSDGELIPSELVRRARVLGYRAIAITDHadasnleEILEKLVRAAEELELyWDIEVIPGVEL 66
PHP_PolIIIA_POLC cd07435
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III at ...
 3-64 7.21e-05

Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III at PolC gene; DNA polymerase III alphas (PolIIIAs) that contain a PHP domain have been classified into four basic groups based on phylogenetic and domain structural analyses: polC, dnaE1, dnaE2, and dnaE3. The PolC group is distinct from the other three and is clustered together. 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 are 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. PolC PHP is located in different location compare to dnaE1, 2, and 3. The PHP domain has four conserved sequence motifs and and contains an invariant histidine that is involved in metal ion coordination.The PHP domain of PolC 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. PHP domains found in dnaEs of thermophilic origin exhibit 3'-5' exonuclease activity. In contrast, PolC PHP lacks detectable nuclease activity.


Pssm-ID: 213990 [Multi-domain]  Cd Length: 268  Bit Score: 43.23  E-value: 7.21e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2185189940   3 IDLHMHSNAS--DGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERLGIAFVPGIEI 64
Cdd:cd07435     2 VELHAHTKMSamDGVTSVKELVKRAAEWGHKAIAITDHGVVQAFPEAYEAAKKNGIKVIYGVEA 65
PHP_PolX cd07436
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal ...
 4-38 1.72e-04

Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal X-family DNA polymerases (PolXs) have a PHP domain at their C-terminus. The bacterial/archaeal PolX core domain and PHP domain interact with each other and together are involved in metal dependent 3'-5' exonuclease activity. 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. PolX is found in all kingdoms, however bacterial PolXs have a completely different domain structure from eukaryotic PolXs. Bacterial PolX has an extended conformation in contrast to the common closed 'right hand' conformation for DNA polymerases. This extended conformation is stabilized by the PHP domain. The PHP domain of PolX is structurally homologous to other members of the PHP family that has a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.


Pssm-ID: 213991 [Multi-domain]  Cd Length: 237  Bit Score: 42.02  E-value: 1.72e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2185189940   4 DLHMHSNASDGILPPAEVVRLCAGNGVKLMSLTDH 38
Cdd:cd07436     8 DLHVHTTWSDGRNSIEEMAEAARALGYEYIAITDH 42
PRK08609 PRK08609
DNA polymerase/3'-5' exonuclease PolX;
4-64 2.41e-04

DNA polymerase/3'-5' exonuclease PolX;


Pssm-ID: 236311 [Multi-domain]  Cd Length: 570  Bit Score: 42.25  E-value: 2.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940   4 DLHMHSNASDGILPPAEVVRLCAGNGVKLMSLTDHD---------TMKGIEEARAEAERLGIAFvPGIEI 64
Cdd:PRK08609  337 DLHMHTTWSDGAFSIEEMVEACIAKGYEYMAITDHSqylkvanglTEERLLEQAEEIKALNEKY-PEIDI 405
polC PRK00448
DNA polymerase III PolC; Validated
 3-66 6.37e-04

DNA polymerase III PolC; Validated


Pssm-ID: 234767 [Multi-domain]  Cd Length: 1437  Bit Score: 41.36  E-value: 6.37e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2185189940    3 IDLHMHSNAS--DGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERLGIAFVPGIEIST 66
Cdd:PRK00448   335 VELHLHTKMStmDAIPSVSELVKRAAKWGHKAIAITDHGVVQAFPEAYNAAKKAGIKVIYGVEANL 400
PRK07945 PRK07945
PHP domain-containing protein;
4-38 2.00e-03

PHP domain-containing protein;


Pssm-ID: 236135 [Multi-domain]  Cd Length: 335  Bit Score: 39.19  E-value: 2.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2185189940   4 DLHMHSNASDGILPPAEVVRLCAGNGVKLMSLTDH 38
Cdd:PRK07945   99 DLHTHSDWSDGGSPIEEMARTAAALGHEYCALTDH 133
PHP_PolIIIA cd07431
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III; ...
 5-82 2.50e-03

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: 37.95  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185189940   5 LHMHSNAS--DGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERLGIAFVPGIEISTRWGQKSIHVAAYNLNP 82
Cdd:cd07431     3 LHVHSSYSllDSAIRPEDLVARAKELGYSALALTDRNVLYGAVRFYKACKKAGIKPIIGLELTVEGDGEPYPLLLLAKNN 82
dnaE2 PRK05672
error-prone DNA polymerase; Validated
 5-65 6.00e-03

error-prone DNA polymerase; Validated


Pssm-ID: 235553 [Multi-domain]  Cd Length: 1046  Bit Score: 38.30  E-value: 6.00e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2185189940    5 LHMHSNAS--DGILPPAEVVRLCAGNGVKLMSLTDHDTMKGIEEARAEAERLGIAFVPGIEIS 65
Cdd:PRK05672     8 LHCHSNFSflDGASHPEELVERAARLGLRALAITDECGLAGVVRAAEAAKELGLRLVIGAELS 70
 
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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