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Conserved domains on  [gi|497581755|ref|WP_009895939|]
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phosphatase [Clostridioides difficile]

Protein Classification

phosphatase( domain architecture ID 10165080)

putative phosphatase of the PHP superfamily, related to Escherichia coli YcdX

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHP_HisPPase_Ycdx_like cd07437
Polymerase and Histidinol Phosphatase domain of Ycdx like; PHP Ycdx-like is a stand alone PHP ...
 5-235 3.34e-126

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: 356.75  E-value: 3.34e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755   5 IMDVHCHTLISGHAHSTFKENVEEASKKNIKYLGISDHGPNMPGGPHPFYFYNLHLLPREVQGVKILRGIEGNIMDYNGN 84
Cdd:cd07437    2 LADLHTHTIASGHAYSTIEEMARAAAEKGLKLLGITDHGPAMPGAPHPWYFGNLKVIPREIYGVRILRGVEANIIDYDGN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755  85 LDVQEDMLQHLDYIIASLHRPCIASGTKEENTNAILKVMDKPKVKIIGHPDDSRYPLDYEPIVKKAKDKNILLEInnSSL 164
Cdd:cd07437   82 LDLPERVLKRLDYVIASLHEPCFAPGTKEENTRAYINAMENPYVDIIGHPGNPRYPIDYEAVVKAAKEYNVLLEI--NNS 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497581755 165 SSNSHRTGTWENVSHMLTLCKTYGARVILGTDSHICYSIGEFENAEKVLEAVDFPDELVINYHEDEIIEFF 235
Cdd:cd07437  160 SLSPSRKGSRENCREIAELCKKYGVPVIVGSDAHIAYDIGNFDEALELLEEIGFPEELILNTSPERLLDFL 230
 
Name Accession Description Interval E-value
PHP_HisPPase_Ycdx_like cd07437
Polymerase and Histidinol Phosphatase domain of Ycdx like; PHP Ycdx-like is a stand alone PHP ...
 5-235 3.34e-126

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: 356.75  E-value: 3.34e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755   5 IMDVHCHTLISGHAHSTFKENVEEASKKNIKYLGISDHGPNMPGGPHPFYFYNLHLLPREVQGVKILRGIEGNIMDYNGN 84
Cdd:cd07437    2 LADLHTHTIASGHAYSTIEEMARAAAEKGLKLLGITDHGPAMPGAPHPWYFGNLKVIPREIYGVRILRGVEANIIDYDGN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755  85 LDVQEDMLQHLDYIIASLHRPCIASGTKEENTNAILKVMDKPKVKIIGHPDDSRYPLDYEPIVKKAKDKNILLEInnSSL 164
Cdd:cd07437   82 LDLPERVLKRLDYVIASLHEPCFAPGTKEENTRAYINAMENPYVDIIGHPGNPRYPIDYEAVVKAAKEYNVLLEI--NNS 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497581755 165 SSNSHRTGTWENVSHMLTLCKTYGARVILGTDSHICYSIGEFENAEKVLEAVDFPDELVINYHEDEIIEFF 235
Cdd:cd07437  160 SLSPSRKGSRENCREIAELCKKYGVPVIVGSDAHIAYDIGNFDEALELLEEIGFPEELILNTSPERLLDFL 230
PRK09248 PRK09248
putative hydrolase; Validated
 3-235 3.47e-123

putative hydrolase; Validated


Pssm-ID: 236429 [Multi-domain]  Cd Length: 246  Bit Score: 349.52  E-value: 3.47e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755   3 KSIMDVHCHTLISGHAHSTFKENVEEASKKNIKYLGISDHGPNMPGGPHPFYFYNLHLLPREVQGVKILRGIEGNIMDYN 82
Cdd:PRK09248   2 KYPVDTHTHTIASGHAYSTLHENAAEAKQKGLKLFAITDHGPDMPGAPHYWHFGNLRVLPRKVDGVGILRGIEANIKNYD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755  83 GNLDVQEDMLQHLDYIIASLHRPCIASGTKEENTNAILKVMDKPKVKIIGHPDDSRYPLDYEPIVKKAKDKNILLEINNS 162
Cdd:PRK09248  82 GEIDLPGDMLKKLDIVIAGFHEPVFAPGDKETNTQALINAIKNGRVDIIGHPGNPKYPIDIEAVVKAAKEHNVALEINNS 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497581755 163 SLSSNshRTGTWENVSHMLTLCKTYGARVILGTDSHICYSIGEFENAEKVLEAVDFPDELVINYHEDEIIEFF 235
Cdd:PRK09248 162 SFGHS--RKGSEDNCRAIAALCKKAGVWVALGSDAHIAFDIGNFEEALKILDEVGFPEERILNVSPRRLLDFL 232
HIS2 COG1387
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ...
 7-234 9.16e-39

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: 134.13  E-value: 9.16e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755   7 DVHCHTLISgHAHSTFKENVEEASKKNIKYLGISDHGP--NMPGGPHP----FYFYNLHLLPREVQGVKILRGIEGNIMD 80
Cdd:COG1387    4 DLHTHTTYS-DGEGTIEEMVEAAIELGLEYIAITDHSPslFVANGLSEerllEYLEEIEELNEKYPDIKILKGIEVDILP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755  81 yNGNLDVQEDMLQHLDYIIASLHrpCIASGTKEENTNAILKVMDKPKVKIIGHPD------DSRYPLDYEPIVKKAKDKN 154
Cdd:COG1387   83 -DGSLDYPDELLAPLDYVIGSVH--SILEEDYEEYTERLLKAIENPLVDILGHPDgrllggRPGYEVDIEEVLEAAAENG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755 155 ILLEInnsslSSNSHRTGTWEnvsHMLTLCKTYGARVILGTDSHICYSIGEFENAEKVLEAVDFPDELVIN-YHEDEIIE 233
Cdd:COG1387  160 VALEI-----NTRPLRLDPSD---ELLKLAKELGVKITIGSDAHSPEDLGDLEYGVALARRAGLTKEDVFNtLRKEELLK 231


                 .
gi 497581755 234 F 234
Cdd:COG1387  232 L 232
PHP pfam02811
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ...
 7-104 8.52e-06

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


Pssm-ID: 460705 [Multi-domain]  Cd Length: 171  Bit Score: 44.84  E-value: 8.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755    7 DVHCHTLIS-GHAHSTFKENVEEASKKNIKYLGISDHGpNMPGGPHpFYfynlhllpREVQ--GVKILRGIEGNIMDYNG 83
Cdd:pfam02811   1 HLHVHSEYSlLDGAARIEELVKRAKELGMPAIAITDHG-NLFGAVE-FY--------KAAKkaGIKPIIGCEVYVAPGSR 70

                          90       100
                  ....*....|....*....|.
gi 497581755   84 NlDVQEDMLQHLDYIIASLHR 104
Cdd:pfam02811  71 E-ETEKLLAKYFDLVLLAVHE 90
POLIIIAc smart00481
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ...
 7-78 1.20e-05

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: 41.87  E-value: 1.20e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497581755     7 DVHCHTLISG-HAHSTFKENVEEASKKNIKYLGISDHGpnmpggpHPFYFYNLHLLPREVqGVKILRGIEGNI 78
Cdd:smart00481   1 DLHVHSDYSLlDGALSPEELVKRAKELGLKAIAITDHG-------NLFGAVEFYKAAKKA-GIKPIIGLEANI 65
hisJ_fam TIGR01856
histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate ...
 7-103 1.75e-04

histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate phosphatase HisJ of Bacillus subtilis, and related proteins from a number of species within a larger family of phosphatases in the PHP hydrolase family. HisJ catalyzes the penultimate step of histidine biosynthesis but shows no homology to the functionally equivalent sequence in E. coli, a domain of the bifunctional HisB protein. Note, however, that many species have two members and that Clostridium perfringens, predicted not to make histidine, has five members of this family; this family is designated subfamily rather than equivalog to indicate that members may not all act as HisJ.


Pssm-ID: 273837 [Multi-domain]  Cd Length: 253  Bit Score: 41.61  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755    7 DVHCHTLISGHAHSTFKENVEEASKKNIKYLGISDH-------------GPNMPGGPHPFYFYNLHLLPREVQG-VKILR 72
Cdd:TIGR01856   2 DSHSHSPFCAHGTDTLREVVQEAIQLGFEEICFTEHaprpfyypeedflKKEMLFLSLPEYFQEINQLKQEYADkIKILI 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 497581755   73 GIEgniMDYN-GNLDVQEDMLQ--HLDYIIASLH 103
Cdd:TIGR01856  82 GLE---VDYIpGFEEEIKDFLDsyNLDFVIGSVH 112
 
Name Accession Description Interval E-value
PHP_HisPPase_Ycdx_like cd07437
Polymerase and Histidinol Phosphatase domain of Ycdx like; PHP Ycdx-like is a stand alone PHP ...
 5-235 3.34e-126

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: 356.75  E-value: 3.34e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755   5 IMDVHCHTLISGHAHSTFKENVEEASKKNIKYLGISDHGPNMPGGPHPFYFYNLHLLPREVQGVKILRGIEGNIMDYNGN 84
Cdd:cd07437    2 LADLHTHTIASGHAYSTIEEMARAAAEKGLKLLGITDHGPAMPGAPHPWYFGNLKVIPREIYGVRILRGVEANIIDYDGN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755  85 LDVQEDMLQHLDYIIASLHRPCIASGTKEENTNAILKVMDKPKVKIIGHPDDSRYPLDYEPIVKKAKDKNILLEInnSSL 164
Cdd:cd07437   82 LDLPERVLKRLDYVIASLHEPCFAPGTKEENTRAYINAMENPYVDIIGHPGNPRYPIDYEAVVKAAKEYNVLLEI--NNS 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497581755 165 SSNSHRTGTWENVSHMLTLCKTYGARVILGTDSHICYSIGEFENAEKVLEAVDFPDELVINYHEDEIIEFF 235
Cdd:cd07437  160 SLSPSRKGSRENCREIAELCKKYGVPVIVGSDAHIAYDIGNFDEALELLEEIGFPEELILNTSPERLLDFL 230
PRK09248 PRK09248
putative hydrolase; Validated
 3-235 3.47e-123

putative hydrolase; Validated


Pssm-ID: 236429 [Multi-domain]  Cd Length: 246  Bit Score: 349.52  E-value: 3.47e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755   3 KSIMDVHCHTLISGHAHSTFKENVEEASKKNIKYLGISDHGPNMPGGPHPFYFYNLHLLPREVQGVKILRGIEGNIMDYN 82
Cdd:PRK09248   2 KYPVDTHTHTIASGHAYSTLHENAAEAKQKGLKLFAITDHGPDMPGAPHYWHFGNLRVLPRKVDGVGILRGIEANIKNYD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755  83 GNLDVQEDMLQHLDYIIASLHRPCIASGTKEENTNAILKVMDKPKVKIIGHPDDSRYPLDYEPIVKKAKDKNILLEINNS 162
Cdd:PRK09248  82 GEIDLPGDMLKKLDIVIAGFHEPVFAPGDKETNTQALINAIKNGRVDIIGHPGNPKYPIDIEAVVKAAKEHNVALEINNS 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497581755 163 SLSSNshRTGTWENVSHMLTLCKTYGARVILGTDSHICYSIGEFENAEKVLEAVDFPDELVINYHEDEIIEFF 235
Cdd:PRK09248 162 SFGHS--RKGSEDNCRAIAALCKKAGVWVALGSDAHIAFDIGNFEEALKILDEVGFPEERILNVSPRRLLDFL 232
HIS2 COG1387
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ...
 7-234 9.16e-39

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: 134.13  E-value: 9.16e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755   7 DVHCHTLISgHAHSTFKENVEEASKKNIKYLGISDHGP--NMPGGPHP----FYFYNLHLLPREVQGVKILRGIEGNIMD 80
Cdd:COG1387    4 DLHTHTTYS-DGEGTIEEMVEAAIELGLEYIAITDHSPslFVANGLSEerllEYLEEIEELNEKYPDIKILKGIEVDILP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755  81 yNGNLDVQEDMLQHLDYIIASLHrpCIASGTKEENTNAILKVMDKPKVKIIGHPD------DSRYPLDYEPIVKKAKDKN 154
Cdd:COG1387   83 -DGSLDYPDELLAPLDYVIGSVH--SILEEDYEEYTERLLKAIENPLVDILGHPDgrllggRPGYEVDIEEVLEAAAENG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755 155 ILLEInnsslSSNSHRTGTWEnvsHMLTLCKTYGARVILGTDSHICYSIGEFENAEKVLEAVDFPDELVIN-YHEDEIIE 233
Cdd:COG1387  160 VALEI-----NTRPLRLDPSD---ELLKLAKELGVKITIGSDAHSPEDLGDLEYGVALARRAGLTKEDVFNtLRKEELLK 231


                 .
gi 497581755 234 F 234
Cdd:COG1387  232 L 232
PHP_PolX cd07436
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal ...
 7-208 4.42e-24

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: 95.95  E-value: 4.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755   7 DVHCHTLIS-GHAhsTFKENVEEASKKNIKYLGISDHGPN--MPGGPHPFYFYNLHL----LPREVQGVKILRGIEGNIM 79
Cdd:cd07436    8 DLHVHTTWSdGRN--SIEEMAEAARALGYEYIAITDHSKSlrVANGLSEERLREQIEeidaLNEKLPGIRILKGIEVDIL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755  80 DyNGNLDVQEDMLQHLDYIIASLHrpciaSG---TKEENTNAILKVMDKPKVKIIGHPDD----SR--YPLDYEPIVKKA 150
Cdd:cd07436   86 P-DGSLDYPDEVLAELDVVVASVH-----SGfnqSEEEMTERLLKAIENPHVDILGHPTGrllgRRegYEVDMERVIEAA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 497581755 151 KDKNILLEInnsslSSNSHRTG-TWENVSHmltlCKTYGARVILGTDSHicySIGEFEN 208
Cdd:cd07436  160 AETGTALEI-----NANPDRLDlDDRHARR----AKEAGVKIAINTDAH---STDGLDN 206
PHP_HisPPase_Hisj_like cd12110
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; ...
 9-198 6.47e-17

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: 76.83  E-value: 6.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755   9 HCHTLISGHAHSTFKENVEEASKKNIKYLGISDHGPnMPggPHPFYFYNLHLLPREV---------------QGVKILRG 73
Cdd:cd12110    4 HTHTPRCDHASGTLEEYVEAAIELGFTEIGFSEHAP-LP--FEFDDYPESRMAEEELedyveeirrlkekyaDQIEIKLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755  74 IEgniMDYngnLDVQEDMLQH------LDYIIASLH--------RPCIASGTKEENT---------NAILKVMDKPKVKI 130
Cdd:cd12110   81 LE---VDY---FPGYEEELREllygypLDYVIGSVHflggwgfdFPEDGIAEYFEGDidelyeryfDLVEKAIESGLFDI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755 131 IGHPD-----------DSRYPLDYEPIVKKAKDKNILLEInnsslssnshrtgtweNVS-------------HMLTLCKT 186
Cdd:cd12110  155 IGHPDlikkfgkndepDEDYEELIERILRAIAEAGVALEI----------------NTAglrkpvgepypspEFLELAKE 218

                        250
                 ....*....|..
gi 497581755 187 YGARVILGTDSH 198
Cdd:cd12110  219 LGIPVTLGSDAH 230
PRK08392 PRK08392
hypothetical protein; Provisional
 6-214 2.23e-14

hypothetical protein; Provisional


Pssm-ID: 169423 [Multi-domain]  Cd Length: 215  Bit Score: 69.43  E-value: 2.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755   6 MDVHCHTLISGHAHSTFkENVEEASKKNIKYLGISDHGPNMPGGPHPFYFYNLHLLPREVQGVkILRGIEGNIMDyNGnL 85
Cdd:PRK08392   1 MDLHTHTVYSDGIGSVR-DNIAEAERKGLRLVGISDHIHYFTPSKFNAYINEIRQWGEESEIV-VLAGIEANITP-NG-V 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755  86 DVQEDMLQHLDYIIASLHRPCIASGTKEENTNAILKVMDKpKVKIIGHPDDS----RYPL--DYEPIVKKAKDKNILLEI 159
Cdd:PRK08392  77 DITDDFAKKLDYVIASVHEWFGRPEHHEYIELVKLALMDE-NVDIIGHFGNSfpyiGYPSeeELKEILDLAEAYGKAFEI 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 497581755 160 nnsslsSNSHRTGTWENVSHmltlCKTYGARVILGTDSHICYSIGEFENAEKVLE 214
Cdd:PRK08392 156 ------SSRYRVPDLEFIRE----CIKRGIKLTFASDAHRPEDVGNVSWSLKVFK 200
PRK08609 PRK08609
DNA polymerase/3'-5' exonuclease PolX;
7-159 3.03e-10

DNA polymerase/3'-5' exonuclease PolX;


Pssm-ID: 236311 [Multi-domain]  Cd Length: 570  Bit Score: 59.58  E-value: 3.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755   7 DVHCHTLISGHAHStFKENVEEASKKNIKYLGISDHGPNMpggphpfYFYN-------------LHLLPREVQGVKILRG 73
Cdd:PRK08609 337 DLHMHTTWSDGAFS-IEEMVEACIAKGYEYMAITDHSQYL-------KVANglteerlleqaeeIKALNEKYPEIDILSG 408

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755  74 IEGNIMDyNGNLDVQEDMLQHLDYIIASLHRPciASGTKEENTNAILKVMDKPKVKIIGHP------DDSRYPLDYEPIV 147
Cdd:PRK08609 409 IEMDILP-DGSLDYDDEVLAELDYVIAAIHSS--FSQSEEEIMKRLENACRNPYVRLIAHPtgrligRRDGYDVNIDQLI 485

                        170
                 ....*....|..
gi 497581755 148 KKAKDKNILLEI 159
Cdd:PRK08609 486 ELAKETNTALEL 497
PHP cd07309
Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2 ...
 7-78 9.70e-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: 51.27  E-value: 9.70e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497581755   7 DVHCHTLISGHAHSTFKENVEEASKKNIKYLGISDHGPNMPGGPHPFYFYNLHLLPREVQGVKILRGIEGNI 78
Cdd:cd07309    2 DLHTHTVFSDGDHAKLTELVDKAKELGPDALAITDHGNLRGLAEFNTAGK*NHIKAAEAAGIKIIIGSEVNL 73
PRK07328 PRK07328
histidinol-phosphatase; Provisional
 3-224 3.30e-07

histidinol-phosphatase; Provisional


Pssm-ID: 235992 [Multi-domain]  Cd Length: 269  Bit Score: 50.02  E-value: 3.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755   3 KSIMDVHCHTLISGHAHSTFKENVEEASKKNIKYLGISDHGP-------------NMPGGPHPFYFYNLHLLPREVQGVK 69
Cdd:PRK07328   1 KMLVDYHMHTPLCGHAVGTPEEYVQAARRAGLKEIGFTDHLPmyflppewrdpglAMRLEELPFYVSEVERLRARFPDLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755  70 ILRGIEGnimDYN-GNLDVQEDMLQH--LDYIIASLH--------RPCIASGTKEENTNAILK-------------VMDk 125
Cdd:PRK07328  81 VRLGIEA---DYHpGTEEFLERLLEAypFDYVIGSVHylgawgfdNPDFVAEYEERDLDELYRryfalveqaarsgLFD- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755 126 pkvkIIGHPD---------DSRYPLDYEPIVKKAKDKNILLEInnsslssnshRTGTWEN-------VSHMLTLCKTYGA 189
Cdd:PRK07328 157 ----IIGHPDlikkfghrpREDLTELYEEALDVIAAAGLALEV----------NTAGLRKpvgeiypSPALLRACRERGI 222

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 497581755 190 RVILGTDSHICYSIGE-FENAEKVLEAVDFpDELVI 224
Cdd:PRK07328 223 PVVLGSDAHRPEEVGFgFAEALALLKEVGY-TETVV 257
PHP pfam02811
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ...
 7-104 8.52e-06

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


Pssm-ID: 460705 [Multi-domain]  Cd Length: 171  Bit Score: 44.84  E-value: 8.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755    7 DVHCHTLIS-GHAHSTFKENVEEASKKNIKYLGISDHGpNMPGGPHpFYfynlhllpREVQ--GVKILRGIEGNIMDYNG 83
Cdd:pfam02811   1 HLHVHSEYSlLDGAARIEELVKRAKELGMPAIAITDHG-NLFGAVE-FY--------KAAKkaGIKPIIGCEVYVAPGSR 70

                          90       100
                  ....*....|....*....|.
gi 497581755   84 NlDVQEDMLQHLDYIIASLHR 104
Cdd:pfam02811  71 E-ETEKLLAKYFDLVLLAVHE 90
PHP_HisPPase cd07432
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ...
 7-199 8.64e-06

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: 43.77  E-value: 8.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755   7 DVHCHTLISGHAHSTFKENVEEASKKNIKYLGISDHgpNMPGGPHPFYFYnlhllpREVQGVKILRGIEGNIMdyngnld 86
Cdd:cd07432    2 DLHIHSVFSPDSDMTPEEIVERAIELGLDGIAITDH--NTIDGAEEALKE------AYKDGLLVIPGVEVTLV------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755  87 vqedmlqhldyiiaslhrpciasgtkeentnailkvmdkpkvkIIGHPDDSRYPLDYEPIVKKAKDKNILLEINNSSLSS 166
Cdd:cd07432   67 -------------------------------------------VLAHPDRPSRYGLSDLILKPLIKNGDAIEVNNSRLRY 103

                        170       180       190
                 ....*....|....*....|....*....|...
gi 497581755 167 NshrtgtwENVSHMLTLCKTYGARVILGTDSHI 199
Cdd:cd07432  104 G-------LNNLAAKRYAELGGLPITGGSDAHT 129
POLIIIAc smart00481
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ...
 7-78 1.20e-05

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: 41.87  E-value: 1.20e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497581755     7 DVHCHTLISG-HAHSTFKENVEEASKKNIKYLGISDHGpnmpggpHPFYFYNLHLLPREVqGVKILRGIEGNI 78
Cdd:smart00481   1 DLHVHSDYSLlDGALSPEELVKRAKELGLKAIAITDHG-------NLFGAVEFYKAAKKA-GIKPIIGLEANI 65
hisJ_fam TIGR01856
histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate ...
 7-103 1.75e-04

histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate phosphatase HisJ of Bacillus subtilis, and related proteins from a number of species within a larger family of phosphatases in the PHP hydrolase family. HisJ catalyzes the penultimate step of histidine biosynthesis but shows no homology to the functionally equivalent sequence in E. coli, a domain of the bifunctional HisB protein. Note, however, that many species have two members and that Clostridium perfringens, predicted not to make histidine, has five members of this family; this family is designated subfamily rather than equivalog to indicate that members may not all act as HisJ.


Pssm-ID: 273837 [Multi-domain]  Cd Length: 253  Bit Score: 41.61  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581755    7 DVHCHTLISGHAHSTFKENVEEASKKNIKYLGISDH-------------GPNMPGGPHPFYFYNLHLLPREVQG-VKILR 72
Cdd:TIGR01856   2 DSHSHSPFCAHGTDTLREVVQEAIQLGFEEICFTEHaprpfyypeedflKKEMLFLSLPEYFQEINQLKQEYADkIKILI 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 497581755   73 GIEgniMDYN-GNLDVQEDMLQ--HLDYIIASLH 103
Cdd:TIGR01856  82 GLE---VDYIpGFEEEIKDFLDsyNLDFVIGSVH 112
PRK07945 PRK07945
PHP domain-containing protein;
61-133 2.26e-04

PHP domain-containing protein;


Pssm-ID: 236135 [Multi-domain]  Cd Length: 335  Bit Score: 41.50  E-value: 2.26e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497581755  61 LPREVQGVKILRGIEGNIMDyNGNLDVQEDMLQHLDYIIASLHrpciaSGTKEEN---TNAILKVMDKPKVKIIGH 133
Cdd:PRK07945 158 LNEELAPFRILTGIEVDILD-DGSLDQEPELLDRLDVVVASVH-----SKLRMDAaamTRRMLAAVANPHTDVLGH 227
 
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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