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Conserved domains on  [gi|940687499|ref|WP_055021150|]
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MULTISPECIES: PHP domain-containing protein [unclassified Pseudoalteromonas]

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
nside_bi_sphtase super family cl49536
3',5'-nucleoside bisphosphate phosphatase;
1-276 7.24e-104

3',5'-nucleoside bisphosphate phosphatase;


The actual alignment was detected with superfamily member NF041577:

Pssm-ID: 469462 [Multi-domain]  Cd Length: 276  Bit Score: 303.36  E-value: 7.24e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499   1 MIKYDLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDHDTLNAIKPARQviADDNLPLKLIAGVEVSTKWESFEIHIVG 80
Cdd:NF041577   1 MLNVDLHCHSTVSDGLLSPAEVVRRAAARGVELLALTDHDDVGGLAEARA--AAAELGLRFVNGVEISVTWGGHTVHIVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499  81 LNVDDENDALLSLLQAQQAKREERALEIGRRLAKNGFEGIYDQAKTFAENAQ-ITRAHFARALIERGVAKNFPGVFKKYL 159
Cdd:NF041577  79 LGIDPAHPALVAGLASIRAGRIERARRMAASLAKVGIEGAFEGAMRYADNPEmISRTHFARFLVETGVAKDVRSVFKKYL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499 160 GRGKTGYVPSSWCDMQTAIAAIHQAGGVAVLAHPGRYQMSNKWLRKLIIEFKDAGGDAMEVAQPQQAPSERQFLGELSRE 239
Cdd:NF041577 159 VKGKPGYVEHEWASLADAVGWIRAAGGVAVIAHPGRYDLGRTTLERLLTEFKALGGEAIEVVSGSHSADDVGRFARLARE 238
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 940687499 240 YGLLASQGSDFHFP-TSWLELGKNLYLPKDCQGVWQAW 276
Cdd:NF041577 239 FGLLASRGSDFHGPgESYRDLGRLPPLPPGCTPVWERW 276
 
Name Accession Description Interval E-value
nside_bi_sphtase NF041577
3',5'-nucleoside bisphosphate phosphatase;
1-276 7.24e-104

3',5'-nucleoside bisphosphate phosphatase;


Pssm-ID: 469462 [Multi-domain]  Cd Length: 276  Bit Score: 303.36  E-value: 7.24e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499   1 MIKYDLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDHDTLNAIKPARQviADDNLPLKLIAGVEVSTKWESFEIHIVG 80
Cdd:NF041577   1 MLNVDLHCHSTVSDGLLSPAEVVRRAAARGVELLALTDHDDVGGLAEARA--AAAELGLRFVNGVEISVTWGGHTVHIVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499  81 LNVDDENDALLSLLQAQQAKREERALEIGRRLAKNGFEGIYDQAKTFAENAQ-ITRAHFARALIERGVAKNFPGVFKKYL 159
Cdd:NF041577  79 LGIDPAHPALVAGLASIRAGRIERARRMAASLAKVGIEGAFEGAMRYADNPEmISRTHFARFLVETGVAKDVRSVFKKYL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499 160 GRGKTGYVPSSWCDMQTAIAAIHQAGGVAVLAHPGRYQMSNKWLRKLIIEFKDAGGDAMEVAQPQQAPSERQFLGELSRE 239
Cdd:NF041577 159 VKGKPGYVEHEWASLADAVGWIRAAGGVAVIAHPGRYDLGRTTLERLLTEFKALGGEAIEVVSGSHSADDVGRFARLARE 238
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 940687499 240 YGLLASQGSDFHFP-TSWLELGKNLYLPKDCQGVWQAW 276
Cdd:NF041577 239 FGLLASRGSDFHGPgESYRDLGRLPPLPPGCTPVWERW 276
YciV COG0613
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ...
1-257 5.94e-70

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


Pssm-ID: 440378 [Multi-domain]  Cd Length: 188  Bit Score: 214.00  E-value: 5.94e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499   1 MIKYDLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDHDTLNAIKPARQVIADDNlpLKLIAGVEVSTKWESFEIHIVG 80
Cdd:COG0613    1 WMKIDLHVHTTASDGSLSPEELVARAKAAGLDVLAITDHDTVAGYEEAAEAAKELG--LLVIPGVEISTRWEGREVHILG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499  81 LNVDDENDALLSLLQAQQAKREERaleigrrlakngfegiydqaktfaenaqitrahfaraliergvaknfpgvfkkylg 160
Cdd:COG0613   79 YGIDPEDPALEALLGIPVEKAERE-------------------------------------------------------- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499 161 rgktgyvpssWCDMQTAIAAIHQAGGVAVLAHPGRYQMSNkWLRKLIIEFKDAGGDAMEVAQPQQAPSERQFLGELSREY 240
Cdd:COG0613  103 ----------WLSLEEAIDLIREAGGVAVLAHPFRYKRGR-WLDDLLEELADAGLDGIEVYNGRHSPEDNERAAELAEEY 171
                        250
                 ....*....|....*..
gi 940687499 241 GLLASQGSDFHFPTSWL 257
Cdd:COG0613  172 GLLATGGSDAHGPEKPL 188
PHP_HisPPase_AMP cd07438
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) ...
4-251 8.63e-64

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: 197.23  E-value: 8.63e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499   4 YDLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDHDTLNAIKPARQVIADdnLPLKLIAGVEVSTKWESFEIHIVGlnv 83
Cdd:cd07438    1 IDLHTHSTASDGTLSPEELVELAKEAGLKVLAITDHDTVAGLEEALAAAKE--LGIELIPGVEISTEYEGREVHILG--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499  84 ddendallsllqaqqakreeraleigrrlakngfegiydqaktfaenaqitrahfaraliergvaknfpgvfkkylgrgk 163
Cdd:cd07438      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499 164 tgyvpsswcDMQTAIAAIHQAGGVAVLAHPGRYQMSNKWLRKLIIEFKDAGGDAMEVAQPQQAPSERQFLGELSREYGLL 243
Cdd:cd07438   76 ---------SPEEAIELIHAAGGVAVLAHPGLYKLSRKKLEELIEELKEAGLDGIEVYHPYHSPEDRERLLELAKEYGLL 146

                 ....*...
gi 940687499 244 ASQGSDFH 251
Cdd:cd07438  147 VTGGSDFH 154
POLIIIAc smart00481
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ...
5-71 6.35e-15

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: 67.68  E-value: 6.35e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940687499     5 DLHSHTTYS--DGQLSVEQLLHRAVEKNIDVFAITDHDTLNAIKPARQVIADDnlPLKLIAGVEVSTKW 71
Cdd:smart00481   1 DLHVHSDYSllDGALSPEELVKRAKELGLKAIAITDHGNLFGAVEFYKAAKKA--GIKPIIGLEANIVD 67
CehA_McbA_metalo NF038032
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ...
5-254 7.32e-12

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: 64.65  E-value: 7.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499   5 DLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDHDTL-NAIKPARQVIADDNLPlkLIAGVEVSTKWEsfeiHIVGLNV 83
Cdd:NF038032   6 DLHIHTNHSDGPTTPEELARAALAEGLDVIALTDHNTIsGRAYFAELLASERGLL--VIPGMEVTTFWG----HMNLLGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499  84 DdendallsllqaqqakreeraleigrrlakngfegiydqaktfaENAQITRahfaralieRGVAKNFPgvfkkylgrgk 163
Cdd:NF038032  80 D--------------------------------------------LDPYIDW---------RNTDPGSP----------- 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499 164 tgyvpsswcDMQTAIAAIHQAGGVAVLAHPGRYQMSN----KWlrkliiEFKDAGG---DAMEVAQPQQAPseRQFLGEL 236
Cdd:NF038032  96 ---------DIDEVIDEAHRQGGLVGIAHPFSPGGPLctgcGW------EALIDDLgkvDAIEVWNTPDPA--PTNERAL 158
                        250       260
                 ....*....|....*....|....*
gi 940687499 237 SREYGLL-------ASQGSDFHFPT 254
Cdd:NF038032 159 ALWYHLLnegfritATGGSDAHDDF 183
PHP pfam02811
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ...
5-67 2.19e-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: 55.24  E-value: 2.19e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940687499    5 DLHSHTTYS--DGQLSVEQLLHRAVEKNIDVFAITDHDTL-------NAIKPARqviaddnlpLKLIAGVEV 67
Cdd:pfam02811   1 HLHVHSEYSllDGAARIEELVKRAKELGMPAIAITDHGNLfgavefyKAAKKAG---------IKPIIGCEV 63
PRK08609 PRK08609
DNA polymerase/3'-5' exonuclease PolX;
2-39 1.00e-06

DNA polymerase/3'-5' exonuclease PolX;


Pssm-ID: 236311 [Multi-domain]  Cd Length: 570  Bit Score: 49.57  E-value: 1.00e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 940687499   2 IKYDLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDH 39
Cdd:PRK08609 334 IQGDLHMHTTWSDGAFSIEEMVEACIAKGYEYMAITDH 371
 
Name Accession Description Interval E-value
nside_bi_sphtase NF041577
3',5'-nucleoside bisphosphate phosphatase;
1-276 7.24e-104

3',5'-nucleoside bisphosphate phosphatase;


Pssm-ID: 469462 [Multi-domain]  Cd Length: 276  Bit Score: 303.36  E-value: 7.24e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499   1 MIKYDLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDHDTLNAIKPARQviADDNLPLKLIAGVEVSTKWESFEIHIVG 80
Cdd:NF041577   1 MLNVDLHCHSTVSDGLLSPAEVVRRAAARGVELLALTDHDDVGGLAEARA--AAAELGLRFVNGVEISVTWGGHTVHIVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499  81 LNVDDENDALLSLLQAQQAKREERALEIGRRLAKNGFEGIYDQAKTFAENAQ-ITRAHFARALIERGVAKNFPGVFKKYL 159
Cdd:NF041577  79 LGIDPAHPALVAGLASIRAGRIERARRMAASLAKVGIEGAFEGAMRYADNPEmISRTHFARFLVETGVAKDVRSVFKKYL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499 160 GRGKTGYVPSSWCDMQTAIAAIHQAGGVAVLAHPGRYQMSNKWLRKLIIEFKDAGGDAMEVAQPQQAPSERQFLGELSRE 239
Cdd:NF041577 159 VKGKPGYVEHEWASLADAVGWIRAAGGVAVIAHPGRYDLGRTTLERLLTEFKALGGEAIEVVSGSHSADDVGRFARLARE 238
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 940687499 240 YGLLASQGSDFHFP-TSWLELGKNLYLPKDCQGVWQAW 276
Cdd:NF041577 239 FGLLASRGSDFHGPgESYRDLGRLPPLPPGCTPVWERW 276
YciV COG0613
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ...
1-257 5.94e-70

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


Pssm-ID: 440378 [Multi-domain]  Cd Length: 188  Bit Score: 214.00  E-value: 5.94e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499   1 MIKYDLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDHDTLNAIKPARQVIADDNlpLKLIAGVEVSTKWESFEIHIVG 80
Cdd:COG0613    1 WMKIDLHVHTTASDGSLSPEELVARAKAAGLDVLAITDHDTVAGYEEAAEAAKELG--LLVIPGVEISTRWEGREVHILG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499  81 LNVDDENDALLSLLQAQQAKREERaleigrrlakngfegiydqaktfaenaqitrahfaraliergvaknfpgvfkkylg 160
Cdd:COG0613   79 YGIDPEDPALEALLGIPVEKAERE-------------------------------------------------------- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499 161 rgktgyvpssWCDMQTAIAAIHQAGGVAVLAHPGRYQMSNkWLRKLIIEFKDAGGDAMEVAQPQQAPSERQFLGELSREY 240
Cdd:COG0613  103 ----------WLSLEEAIDLIREAGGVAVLAHPFRYKRGR-WLDDLLEELADAGLDGIEVYNGRHSPEDNERAAELAEEY 171
                        250
                 ....*....|....*..
gi 940687499 241 GLLASQGSDFHFPTSWL 257
Cdd:COG0613  172 GLLATGGSDAHGPEKPL 188
PHP_HisPPase_AMP cd07438
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) ...
4-251 8.63e-64

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: 197.23  E-value: 8.63e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499   4 YDLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDHDTLNAIKPARQVIADdnLPLKLIAGVEVSTKWESFEIHIVGlnv 83
Cdd:cd07438    1 IDLHTHSTASDGTLSPEELVELAKEAGLKVLAITDHDTVAGLEEALAAAKE--LGIELIPGVEISTEYEGREVHILG--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499  84 ddendallsllqaqqakreeraleigrrlakngfegiydqaktfaenaqitrahfaraliergvaknfpgvfkkylgrgk 163
Cdd:cd07438      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499 164 tgyvpsswcDMQTAIAAIHQAGGVAVLAHPGRYQMSNKWLRKLIIEFKDAGGDAMEVAQPQQAPSERQFLGELSREYGLL 243
Cdd:cd07438   76 ---------SPEEAIELIHAAGGVAVLAHPGLYKLSRKKLEELIEELKEAGLDGIEVYHPYHSPEDRERLLELAKEYGLL 146

                 ....*...
gi 940687499 244 ASQGSDFH 251
Cdd:cd07438  147 VTGGSDFH 154
PHP_HisPPase cd07432
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ...
4-68 5.63e-17

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: 75.35  E-value: 5.63e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940687499   4 YDLHSHTTYS-DGQLSVEQLLHRAVEKNIDVFAITDHDTLNAIKPARQVIADDNlpLKLIAGVEVS 68
Cdd:cd07432    1 ADLHIHSVFSpDSDMTPEEIVERAIELGLDGIAITDHNTIDGAEEALKEAYKDG--LLVIPGVEVT 64
POLIIIAc smart00481
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ...
5-71 6.35e-15

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: 67.68  E-value: 6.35e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940687499     5 DLHSHTTYS--DGQLSVEQLLHRAVEKNIDVFAITDHDTLNAIKPARQVIADDnlPLKLIAGVEVSTKW 71
Cdd:smart00481   1 DLHVHSDYSllDGALSPEELVKRAKELGLKAIAITDHGNLFGAVEFYKAAKKA--GIKPIIGLEANIVD 67
HIS2 COG1387
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ...
2-148 1.41e-12

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: 65.56  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499   2 IKYDLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDHDTLNAIKPArqvIADDNLP--LKLIAgvEVSTKWESFEIhIV 79
Cdd:COG1387    1 MRGDLHTHTTYSDGEGTIEEMVEAAIELGLEYIAITDHSPSLFVANG---LSEERLLeyLEEIE--ELNEKYPDIKI-LK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499  80 GLNVD-------DENDALLS--------------LLQAQQAKREERALE------IG-----RRLAKNGFEGIYDQAktf 127
Cdd:COG1387   75 GIEVDilpdgslDYPDELLApldyvigsvhsileEDYEEYTERLLKAIEnplvdiLGhpdgrLLGGRPGYEVDIEEV--- 151
                        170       180
                 ....*....|....*....|.
gi 940687499 128 aenaqitrahfARALIERGVA 148
Cdd:COG1387  152 -----------LEAAAENGVA 161
CehA_McbA_metalo NF038032
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ...
5-254 7.32e-12

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: 64.65  E-value: 7.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499   5 DLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDHDTL-NAIKPARQVIADDNLPlkLIAGVEVSTKWEsfeiHIVGLNV 83
Cdd:NF038032   6 DLHIHTNHSDGPTTPEELARAALAEGLDVIALTDHNTIsGRAYFAELLASERGLL--VIPGMEVTTFWG----HMNLLGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499  84 DdendallsllqaqqakreeraleigrrlakngfegiydqaktfaENAQITRahfaralieRGVAKNFPgvfkkylgrgk 163
Cdd:NF038032  80 D--------------------------------------------LDPYIDW---------RNTDPGSP----------- 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499 164 tgyvpsswcDMQTAIAAIHQAGGVAVLAHPGRYQMSN----KWlrkliiEFKDAGG---DAMEVAQPQQAPseRQFLGEL 236
Cdd:NF038032  96 ---------DIDEVIDEAHRQGGLVGIAHPFSPGGPLctgcGW------EALIDDLgkvDAIEVWNTPDPA--PTNERAL 158
                        250       260
                 ....*....|....*....|....*
gi 940687499 237 SREYGLL-------ASQGSDFHFPT 254
Cdd:NF038032 159 ALWYHLLnegfritATGGSDAHDDF 183
PHP pfam02811
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ...
5-67 2.19e-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: 55.24  E-value: 2.19e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940687499    5 DLHSHTTYS--DGQLSVEQLLHRAVEKNIDVFAITDHDTL-------NAIKPARqviaddnlpLKLIAGVEV 67
Cdd:pfam02811   1 HLHVHSEYSllDGAARIEELVKRAKELGMPAIAITDHGNLfgavefyKAAKKAG---------IKPIIGCEV 63
PHP_HisPPase_Thermotoga_like cd12111
Polymerase and Histidinol Phosphatase domain of Thermotoga like; The PHP (also called ...
5-108 1.42e-07

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: 50.88  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499   5 DLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDH----DTLNAIKPARQVIADDNLPLK-------------------- 60
Cdd:cd12111    5 DFHIHTTYSDGALSLSEVVDLYGQHGFDVIAITDHvvdrASLIGKFPQGTHPGVTEANFEdymealkveakrawekyemi 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 940687499  61 LIAGVEVSTKWESFeiHIVGLNVDDENDALLSLLQAQQAKREERALEI 108
Cdd:cd12111   85 VIPGVELTNNTDSY--HILGIDVKEYIDPCLSVEEIIAEIHKQGGIAV 130
PHP_PolX cd07436
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal ...
2-39 2.14e-07

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: 50.50  E-value: 2.14e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 940687499   2 IKYDLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDH 39
Cdd:cd07436    5 IRGDLHVHTTWSDGRNSIEEMAEAARALGYEYIAITDH 42
PHP cd07309
Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2 ...
5-68 6.45e-07

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: 46.27  E-value: 6.45e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940687499   5 DLHSHTTYSDG-QLSVEQLLHRAVEKNIDVFAITDHD---------TLNAIKPARQVIADDnlpLKLIAGVEVS 68
Cdd:cd07309    2 DLHTHTVFSDGdHAKLTELVDKAKELGPDALAITDHGnlrglaefnTAGK*NHIKAAEAAG---IKIIIGSEVN 72
PRK08609 PRK08609
DNA polymerase/3'-5' exonuclease PolX;
2-39 1.00e-06

DNA polymerase/3'-5' exonuclease PolX;


Pssm-ID: 236311 [Multi-domain]  Cd Length: 570  Bit Score: 49.57  E-value: 1.00e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 940687499   2 IKYDLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDH 39
Cdd:PRK08609 334 IQGDLHMHTTWSDGAFSIEEMVEACIAKGYEYMAITDH 371
DnaE COG0587
DNA polymerase III, alpha subunit [Replication, recombination and repair];
6-67 1.39e-06

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


Pssm-ID: 440352 [Multi-domain]  Cd Length: 1050  Bit Score: 49.30  E-value: 1.39e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940687499    6 LHSHTTYS--DGQLSVEQLLHRAVEKNIDVFAITDHDTL----NAIKPARQViaddnlPLKLIAGVEV 67
Cdd:COG0587     8 LHVHSEYSllDGASRPEELVARAAELGMPALAITDHGNLfgavRFYKAAKKA------GIKPIIGCEL 69
PRK06361 PRK06361
histidinol phosphate phosphatase domain-containing protein;
9-67 3.45e-06

histidinol phosphate phosphatase domain-containing protein;


Pssm-ID: 180543 [Multi-domain]  Cd Length: 212  Bit Score: 46.88  E-value: 3.45e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940687499   9 HTTYSDGQLSVEQLLHRAVEKNIDVFAITDH-------DTLNAIKPARQVIAdDNLPLKLIAGVEV 67
Cdd:PRK06361   2 HTIFSDGELIPSELVRRARVLGYRAIAITDHadasnleEILEKLVRAAEELE-LYWDIEVIPGVEL 66
PRK07945 PRK07945
PHP domain-containing protein;
5-67 9.62e-05

PHP domain-containing protein;


Pssm-ID: 236135 [Multi-domain]  Cd Length: 335  Bit Score: 43.04  E-value: 9.62e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940687499   5 DLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDHD----TLNAIKPAR-----QVIADDN---LPLKLIAGVEV 67
Cdd:PRK07945  99 DLHTHSDWSDGGSPIEEMARTAAALGHEYCALTDHSprltVANGLSAERlrkqlDVVAELNeelAPFRILTGIEV 173
dnaE2 PRK05672
error-prone DNA polymerase; Validated
6-68 1.12e-04

error-prone DNA polymerase; Validated


Pssm-ID: 235553 [Multi-domain]  Cd Length: 1046  Bit Score: 43.31  E-value: 1.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940687499    6 LHSHTTYS--DGQLSVEQLLHRAVEKNIDVFAITDHDTLNAIkpARQVIADDNLPLKLIAGVEVS 68
Cdd:PRK05672    8 LHCHSNFSflDGASHPEELVERAARLGLRALAITDECGLAGV--VRAAEAAKELGLRLVIGAELS 70
dnaE PRK06826
DNA polymerase III DnaE; Reviewed
6-47 1.84e-04

DNA polymerase III DnaE; Reviewed


Pssm-ID: 235868 [Multi-domain]  Cd Length: 1151  Bit Score: 42.95  E-value: 1.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 940687499    6 LHSHTTYS--DGQLSVEQLLHRAVEKNIDVFAITDHDTL------------NAIKP 47
Cdd:PRK06826    8 LHVHTEYSllDGSARIKDLIKRAKELGMDSIAITDHGVMygvvdfykaakkQGIKP 63
PHP_PolIIIA_POLC cd07435
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III at ...
6-66 2.67e-04

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: 41.69  E-value: 2.67e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940687499   6 LHSHTTYS--DGQLSVEQLLHRAVEKNIDVFAITDHDTLNAIkPARQVIADDNlPLKLIAGVE 66
Cdd:cd07435    4 LHAHTKMSamDGVTSVKELVKRAAEWGHKAIAITDHGVVQAF-PEAYEAAKKN-GIKVIYGVE 64
PHP_HisPPase_Chlorobi_like cd12112
Polymerase and Histidinol Phosphatase domain of Chlorobi like; The PHP (also called histidinol ...
3-68 3.58e-04

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: 41.16  E-value: 3.58e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940687499   3 KYDLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDH--------DTLN-----AIKPARQVIADdnLPLKLIAGVEVS 68
Cdd:cd12112   14 KCDFHTHTVFSDGHVWPEIRVREAWREGLDAIAITEHieyrphkeDIPHpdrnrSYKIAKEAAES--KGLLIIPGAEIT 90
PHP_PolIIIA_DnaE3 cd12113
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III ...
6-39 7.39e-04

Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III DnaE3; 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, the PolIIIA PHP 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 an activity has not been found. It has been shown that the PHP of PolIIIA has a trinuclear metal complex and is capable of proofreading activity. Bacterial genome replication and DNA repair mechanisms is related to the GC content of its genomes. There is a correlation between GC content variations and the dimeric combinations of PolIIIA subunits. Eubacteria can be grouped into different GC variable groups: the full-spectrum or dnaE1 group, the high-GC or dnaE2-dnaE1 group, and the low GC or polC-dnaE3 group.


Pssm-ID: 213997 [Multi-domain]  Cd Length: 283  Bit Score: 40.12  E-value: 7.39e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 940687499   6 LHSHTTYS--DGQLSVEQLLHRAVEKNIDVFAITDH 39
Cdd:cd12113    5 LHVHTEYSllDGAIRIKDLVKRAKELGMPALAITDH 40
PRK08392 PRK08392
hypothetical protein; Provisional
5-66 1.12e-03

hypothetical protein; Provisional


Pssm-ID: 169423 [Multi-domain]  Cd Length: 215  Bit Score: 39.38  E-value: 1.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940687499   5 DLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDH------DTLNA-IKPARQVIADDNLPlkLIAGVE 66
Cdd:PRK08392   2 DLHTHTVYSDGIGSVRDNIAEAERKGLRLVGISDHihyftpSKFNAyINEIRQWGEESEIV--VLAGIE 68
PHP_PolIIIA cd07431
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III; ...
6-133 1.87e-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: 38.34  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687499   6 LHSHTTYS--DGQLSVEQLLHRAVEKNIDVFAITDHDTL------------NAIKParqviaddnlplklIAGVEVSTKW 71
Cdd:cd07431    3 LHVHSSYSllDSAIRPEDLVARAKELGYSALALTDRNVLygavrfykackkAGIKP--------------IIGLELTVEG 68
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940687499  72 ESFEIHIVglnVDDENDA-------LLSLLQAQQAKREERALEiGRRLAKNGFEGIY----DQAKTFAENAQI 133
Cdd:cd07431   69 DGEPYPLL---LLAKNNEgyqnllrLSTAAMLGEEKDGVPYLD-LEELAEAASGLLVvllgPLLLLLAAEQGL 137
PHP_HisPPase_Hisj_like cd12110
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; ...
4-39 2.17e-03

Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; Bacillus subtilis YtvP HisJ has strong histidinol phosphate phosphatase (HisPPase) 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. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to produce 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 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: 213994 [Multi-domain]  Cd Length: 244  Bit Score: 38.70  E-value: 2.17e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 940687499   4 YDLHSHTTYSD-GQLSVEQLLHRAVEKNIDVFAITDH 39
Cdd:cd12110    1 VDYHTHTPRCDhASGTLEEYVEAAIELGFTEIGFSEH 37
PHP_HisPPase_Ycdx_like cd07437
Polymerase and Histidinol Phosphatase domain of Ycdx like; PHP Ycdx-like is a stand alone PHP ...
5-39 3.45e-03

Polymerase and Histidinol Phosphatase domain of Ycdx like; PHP Ycdx-like is a stand alone PHP domain similar to Ycdx E. coli protein with an unknown physiological role. 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. 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. YcdX may be involved in swarming.


Pssm-ID: 213992 [Multi-domain]  Cd Length: 233  Bit Score: 37.81  E-value: 3.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 940687499   5 DLHSHT-----TYSdgqlSVEQLLHRAVEKNIDVFAITDH 39
Cdd:cd07437    4 DLHTHTiasghAYS----TIEEMARAAAEKGLKLLGITDH 39
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
2-39 9.35e-03

DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 37.09  E-value: 9.35e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 940687499   2 IKYDLHSHTTYSDGQLSVEQLLHRAVEKNIDVFAITDH 39
Cdd:COG1796  336 IRGDLHHHTTWSDGGASIEEMAAAAAARGYYYIAITDH 373
 
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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