NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|495164185|ref|WP_007888983|]
View 

MULTISPECIES: phosphatase [Cronobacter]

Protein Classification

phosphatase( domain architecture ID 11483686)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK09248 PRK09248
putative hydrolase; Validated
 1-245 7.34e-168

putative hydrolase; Validated


:

Pssm-ID: 236429 [Multi-domain]  Cd Length: 246  Bit Score: 462.77  E-value: 7.34e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185   1 MYPVDLHMHTVASTHAYSNLHDYIAAAKQKGVRLLAITDHGPDMADAPHHWHFINMRIWPRVVDGVGILRGIEANIKNRE 80
Cdd:PRK09248   2 KYPVDTHTHTIASGHAYSTLHENAAEAKQKGLKLFAITDHGPDMPGAPHYWHFGNLRVLPRKVDGVGILRGIEANIKNYD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185  81 GEIDCTGPMLDSLDLIVAGFHEPVFAPQDKDANTEAMIATMASGTVHIISHPGNPKYPVDIPAVAAAAAKYQVALEINNS 160
Cdd:PRK09248  82 GEIDLPGDMLKKLDIVIAGFHEPVFAPGDKETNTQALINAIKNGRVDIIGHPGNPKYPIDIEAVVKAAKEHNVALEINNS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185 161 SFTHSRKGSGPNCKAIAAAVRDAGGWVALGSDSHTAFTLGDFHECRKVLDEVDFPEDRILNVSPRRLLDFLETRGMTPIA 240
Cdd:PRK09248 162 SFGHSRKGSEDNCRAIAALCKKAGVWVALGSDAHIAFDIGNFEEALKILDEVGFPEERILNVSPRRLLDFLESRGKAPIP 241


                 ....*
gi 495164185 241 EFAAL 245
Cdd:PRK09248 242 EFADL 246
 
Name Accession Description Interval E-value
PRK09248 PRK09248
putative hydrolase; Validated
 1-245 7.34e-168

putative hydrolase; Validated


Pssm-ID: 236429 [Multi-domain]  Cd Length: 246  Bit Score: 462.77  E-value: 7.34e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185   1 MYPVDLHMHTVASTHAYSNLHDYIAAAKQKGVRLLAITDHGPDMADAPHHWHFINMRIWPRVVDGVGILRGIEANIKNRE 80
Cdd:PRK09248   2 KYPVDTHTHTIASGHAYSTLHENAAEAKQKGLKLFAITDHGPDMPGAPHYWHFGNLRVLPRKVDGVGILRGIEANIKNYD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185  81 GEIDCTGPMLDSLDLIVAGFHEPVFAPQDKDANTEAMIATMASGTVHIISHPGNPKYPVDIPAVAAAAAKYQVALEINNS 160
Cdd:PRK09248  82 GEIDLPGDMLKKLDIVIAGFHEPVFAPGDKETNTQALINAIKNGRVDIIGHPGNPKYPIDIEAVVKAAKEHNVALEINNS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185 161 SFTHSRKGSGPNCKAIAAAVRDAGGWVALGSDSHTAFTLGDFHECRKVLDEVDFPEDRILNVSPRRLLDFLETRGMTPIA 240
Cdd:PRK09248 162 SFGHSRKGSEDNCRAIAALCKKAGVWVALGSDAHIAFDIGNFEEALKILDEVGFPEERILNVSPRRLLDFLESRGKAPIP 241


                 ....*
gi 495164185 241 EFAAL 245
Cdd:PRK09248 242 EFADL 246
PHP_HisPPase_Ycdx_like cd07437
Polymerase and Histidinol Phosphatase domain of Ycdx like; PHP Ycdx-like is a stand alone PHP ...
 2-234 5.23e-119

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: 338.65  E-value: 5.23e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185   2 YPVDLHMHTVASTHAYSNLHDYIAAAKQKGVRLLAITDHGPDMADAPHHWHFINMRIWPRVVDGVGILRGIEANIKNREG 81
Cdd:cd07437    1 ILADLHTHTIASGHAYSTIEEMARAAAEKGLKLLGITDHGPAMPGAPHPWYFGNLKVIPREIYGVRILRGVEANIIDYDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185  82 EIDCTGPMLDSLDLIVAGFHEPVFAPQDKDANTEAMIATMASGTVHIISHPGNPKYPVDIPAVAAAAAKYQVALEINNSS 161
Cdd:cd07437   81 NLDLPERVLKRLDYVIASLHEPCFAPGTKEENTRAYINAMENPYVDIIGHPGNPRYPIDYEAVVKAAKEYNVLLEINNSS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495164185 162 FTHSRKGSGPNCKAIAAAVRDAGGWVALGSDSHTAFTLGDFHECRKVLDEVDFPEDRILNVSPRRLLDFLETR 234
Cdd:cd07437  161 LSPSRKGSRENCREIAELCKKYGVPVIVGSDAHIAYDIGNFDEALELLEEIGFPEELILNTSPERLLDFLKLR 233
HIS2 COG1387
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ...
 4-226 1.59e-35

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: 126.04  E-value: 1.59e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185   4 VDLHMHTVAStHAYSNLHDYIAAAKQKGVRLLAITDHGP--------DMADAPHHWHFIN-MRiwpRVVDGVGILRGIEA 74
Cdd:COG1387    3 GDLHTHTTYS-DGEGTIEEMVEAAIELGLEYIAITDHSPslfvanglSEERLLEYLEEIEeLN---EKYPDIKILKGIEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185  75 NIKNrEGEIDCTGPMLDSLDLIVAGFHEpvFAPQDKDANTEAMIATMASGTVHIISHPGNPK------YPVDIPAVAAAA 148
Cdd:COG1387   79 DILP-DGSLDYPDELLAPLDYVIGSVHS--ILEEDYEEYTERLLKAIENPLVDILGHPDGRLlggrpgYEVDIEEVLEAA 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495164185 149 AKYQVALEINNSSFthsRKGsgPNcKAIAAAVRDAGGWVALGSDSHTAFTLGDFHECRKVLDEVDFPEDRILNVSPRR 226
Cdd:COG1387  156 AENGVALEINTRPL---RLD--PS-DELLKLAKELGVKITIGSDAHSPEDLGDLEYGVALARRAGLTKEDVFNTLRKE 227
POLIIIAc smart00481
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ...
 5-78 1.67e-08

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


Pssm-ID: 197753 [Multi-domain]  Cd Length: 67  Bit Score: 49.96  E-value: 1.67e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495164185     5 DLHMHTVAS-THAYSNLHDYIAAAKQKGVRLLAITDHGpdmadapHHWHFINMRIWPRvVDGVGILRGIEANIKN 78
Cdd:smart00481   1 DLHVHSDYSlLDGALSPEELVKRAKELGLKAIAITDHG-------NLFGAVEFYKAAK-KAGIKPIIGLEANIVD 67
PHP pfam02811
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ...
 5-97 7.80e-07

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


Pssm-ID: 460705 [Multi-domain]  Cd Length: 171  Bit Score: 47.92  E-value: 7.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185    5 DLHMHTvasthAYSNLH------DYIAAAKQKGVRLLAITDHGPdMADAPHHW-HFINMRIWPRVvdgvgilrGIEANIK 77
Cdd:pfam02811   1 HLHVHS-----EYSLLDgaarieELVKRAKELGMPAIAITDHGN-LFGAVEFYkAAKKAGIKPII--------GCEVYVA 66

                          90       100
                  ....*....|....*....|
gi 495164185   78 NREGEiDCTGPMLDSLDLIV 97
Cdd:pfam02811  67 PGSRE-ETEKLLAKYFDLVL 85
CehA_McbA_metalo NF038032
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ...
 2-42 2.07e-03

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: 38.84  E-value: 2.07e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 495164185   2 YPVDLHMHTVAStHAYSNLHDYIAAAKQKGVRLLAITDHGP 42
Cdd:NF038032   3 YSGDLHIHTNHS-DGPTTPEELARAALAEGLDVIALTDHNT 42
hisJ_fam TIGR01856
histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate ...
 5-52 8.17e-03

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: 36.61  E-value: 8.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 495164185    5 DLHMHTVASTHAYSNLHDYIAAAKQKGVRLLAITDHGPDMADAPHHWH 52
Cdd:TIGR01856   2 DSHSHSPFCAHGTDTLREVVQEAIQLGFEEICFTEHAPRPFYYPEEDF 49
 
Name Accession Description Interval E-value
PRK09248 PRK09248
putative hydrolase; Validated
 1-245 7.34e-168

putative hydrolase; Validated


Pssm-ID: 236429 [Multi-domain]  Cd Length: 246  Bit Score: 462.77  E-value: 7.34e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185   1 MYPVDLHMHTVASTHAYSNLHDYIAAAKQKGVRLLAITDHGPDMADAPHHWHFINMRIWPRVVDGVGILRGIEANIKNRE 80
Cdd:PRK09248   2 KYPVDTHTHTIASGHAYSTLHENAAEAKQKGLKLFAITDHGPDMPGAPHYWHFGNLRVLPRKVDGVGILRGIEANIKNYD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185  81 GEIDCTGPMLDSLDLIVAGFHEPVFAPQDKDANTEAMIATMASGTVHIISHPGNPKYPVDIPAVAAAAAKYQVALEINNS 160
Cdd:PRK09248  82 GEIDLPGDMLKKLDIVIAGFHEPVFAPGDKETNTQALINAIKNGRVDIIGHPGNPKYPIDIEAVVKAAKEHNVALEINNS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185 161 SFTHSRKGSGPNCKAIAAAVRDAGGWVALGSDSHTAFTLGDFHECRKVLDEVDFPEDRILNVSPRRLLDFLETRGMTPIA 240
Cdd:PRK09248 162 SFGHSRKGSEDNCRAIAALCKKAGVWVALGSDAHIAFDIGNFEEALKILDEVGFPEERILNVSPRRLLDFLESRGKAPIP 241


                 ....*
gi 495164185 241 EFAAL 245
Cdd:PRK09248 242 EFADL 246
PHP_HisPPase_Ycdx_like cd07437
Polymerase and Histidinol Phosphatase domain of Ycdx like; PHP Ycdx-like is a stand alone PHP ...
 2-234 5.23e-119

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: 338.65  E-value: 5.23e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185   2 YPVDLHMHTVASTHAYSNLHDYIAAAKQKGVRLLAITDHGPDMADAPHHWHFINMRIWPRVVDGVGILRGIEANIKNREG 81
Cdd:cd07437    1 ILADLHTHTIASGHAYSTIEEMARAAAEKGLKLLGITDHGPAMPGAPHPWYFGNLKVIPREIYGVRILRGVEANIIDYDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185  82 EIDCTGPMLDSLDLIVAGFHEPVFAPQDKDANTEAMIATMASGTVHIISHPGNPKYPVDIPAVAAAAAKYQVALEINNSS 161
Cdd:cd07437   81 NLDLPERVLKRLDYVIASLHEPCFAPGTKEENTRAYINAMENPYVDIIGHPGNPRYPIDYEAVVKAAKEYNVLLEINNSS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495164185 162 FTHSRKGSGPNCKAIAAAVRDAGGWVALGSDSHTAFTLGDFHECRKVLDEVDFPEDRILNVSPRRLLDFLETR 234
Cdd:cd07437  161 LSPSRKGSRENCREIAELCKKYGVPVIVGSDAHIAYDIGNFDEALELLEEIGFPEELILNTSPERLLDFLKLR 233
HIS2 COG1387
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ...
 4-226 1.59e-35

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: 126.04  E-value: 1.59e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185   4 VDLHMHTVAStHAYSNLHDYIAAAKQKGVRLLAITDHGP--------DMADAPHHWHFIN-MRiwpRVVDGVGILRGIEA 74
Cdd:COG1387    3 GDLHTHTTYS-DGEGTIEEMVEAAIELGLEYIAITDHSPslfvanglSEERLLEYLEEIEeLN---EKYPDIKILKGIEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185  75 NIKNrEGEIDCTGPMLDSLDLIVAGFHEpvFAPQDKDANTEAMIATMASGTVHIISHPGNPK------YPVDIPAVAAAA 148
Cdd:COG1387   79 DILP-DGSLDYPDELLAPLDYVIGSVHS--ILEEDYEEYTERLLKAIENPLVDILGHPDGRLlggrpgYEVDIEEVLEAA 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495164185 149 AKYQVALEINNSSFthsRKGsgPNcKAIAAAVRDAGGWVALGSDSHTAFTLGDFHECRKVLDEVDFPEDRILNVSPRR 226
Cdd:COG1387  156 AENGVALEINTRPL---RLD--PS-DELLKLAKELGVKITIGSDAHSPEDLGDLEYGVALARRAGLTKEDVFNTLRKE 227
PHP_PolX cd07436
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal ...
 5-203 1.32e-21

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: 89.79  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185   5 DLHMHTVASTHAYSnLHDYIAAAKQKGVRLLAITDH--------GPDMADAPHHWHFInmRIWPRVVDGVGILRGIEANI 76
Cdd:cd07436    8 DLHVHTTWSDGRNS-IEEMAEAARALGYEYIAITDHskslrvanGLSEERLREQIEEI--DALNEKLPGIRILKGIEVDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185  77 KNrEGEIDCTGPMLDSLDLIVA----GFHepvfapQDKDANTEAMIATMASGTVHIISHP------GNPKYPVDIPAVAA 146
Cdd:cd07436   85 LP-DGSLDYPDEVLAELDVVVAsvhsGFN------QSEEEMTERLLKAIENPHVDILGHPtgrllgRREGYEVDMERVIE 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495164185 147 AAAKYQVALEINnssfthsrkgSGP-----NCKAIAAAvRDAGGWVALGSDSHTAFTLGDFH 203
Cdd:cd07436  158 AAAETGTALEIN----------ANPdrldlDDRHARRA-KEAGVKIAINTDAHSTDGLDNMR 208
PHP cd07309
Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2 ...
 4-76 2.51e-21

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: 84.79  E-value: 2.51e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495164185   4 VDLHMHTVASTHAYSNLHDYIAAAKQKGVRLLAITDHGPDMADAPHHWHFINMRIWPRVVDGVGILRGIEANI 76
Cdd:cd07309    1 VDLHTHTVFSDGDHAKLTELVDKAKELGPDALAITDHGNLRGLAEFNTAGK*NHIKAAEAAGIKIIIGSEVNL 73
PHP_HisPPase cd07432
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ...
 4-195 1.84e-11

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: 59.95  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185   4 VDLHMHTVASTHAYSNLHDYIAAAKQKGVRLLAITDHgpDMADAPHHWhfinmrIWPRVVDGVGILRGIEAniknregei 83
Cdd:cd07432    1 ADLHIHSVFSPDSDMTPEEIVERAIELGLDGIAITDH--NTIDGAEEA------LKEAYKDGLLVIPGVEV--------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185  84 dctgpmldsldlivagfhepvfapqdkdanteamiatmasgTVHIISHPGNPKYPVDIPAVAAAAAKYQVALEINNSSFT 163
Cdd:cd07432   64 -----------------------------------------TLVVLAHPDRPSRYGLSDLILKPLIKNGDAIEVNNSRLR 102

                        170       180       190
                 ....*....|....*....|....*....|..
gi 495164185 164 HsrkgsGPNCKAIAAAVRDAGGWVALGSDSHT 195
Cdd:cd07432  103 Y-----GLNNLAAKRYAELGGLPITGGSDAHT 129
PRK08609 PRK08609
DNA polymerase/3'-5' exonuclease PolX;
5-232 1.08e-10

DNA polymerase/3'-5' exonuclease PolX;


Pssm-ID: 236311 [Multi-domain]  Cd Length: 570  Bit Score: 61.13  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185   5 DLHMHTVASTHAYSnLHDYIAAAKQKGVRLLAITDHGPDMadaphhwhfinmriwpRVVDG------------------- 65
Cdd:PRK08609 337 DLHMHTTWSDGAFS-IEEMVEACIAKGYEYMAITDHSQYL----------------KVANGlteerlleqaeeikalnek 399

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185  66 ---VGILRGIEANIKNrEGEIDCTGPMLDSLDLIVAGFHEPvFApQDKDANTEAMIATMASGTVHIISHP-----GNPK- 136
Cdd:PRK08609 400 ypeIDILSGIEMDILP-DGSLDYDDEVLAELDYVIAAIHSS-FS-QSEEEIMKRLENACRNPYVRLIAHPtgrliGRRDg 476

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185 137 YPVDIPAVAAAAAKYQVALEINnssfthsrkgSGPN----CKAIAAAVRDAGGWVALGSDSHTAFTLgDFHE-----CRK 207
Cdd:PRK08609 477 YDVNIDQLIELAKETNTALELN----------ANPNrldlSAEHLKKAQEAGVKLAINTDAHHTEML-DDMKygvatARK 545

                        250       260
                 ....*....|....*....|....*.
gi 495164185 208 VLdevdFPEDRILNVSPR-RLLDFLE 232
Cdd:PRK08609 546 GW----IQKDRVINTWSReEFKDFIK 567
PRK08392 PRK08392
hypothetical protein; Provisional
 5-194 3.78e-10

hypothetical protein; Provisional


Pssm-ID: 169423 [Multi-domain]  Cd Length: 215  Bit Score: 57.87  E-value: 3.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185   5 DLHMHTVASThAYSNLHDYIAAAKQKGVRLLAITDHGPDMADAPHHWHFINMRIWPRVVDGVgILRGIEANIKnrEGEID 84
Cdd:PRK08392   2 DLHTHTVYSD-GIGSVRDNIAEAERKGLRLVGISDHIHYFTPSKFNAYINEIRQWGEESEIV-VLAGIEANIT--PNGVD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185  85 CTGPMLDSLDLIVAGFHEPVFAPQDKDANTEAMIATMASgTVHIISHPGNPKYPVDIPAVAAAAAKYQVAlEINNSSFTH 164
Cdd:PRK08392  78 ITDDFAKKLDYVIASVHEWFGRPEHHEYIELVKLALMDE-NVDIIGHFGNSFPYIGYPSEEELKEILDLA-EAYGKAFEI 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 495164185 165 SRKGSGPNCKAIAAAVRdAGGWVALGSDSH 194
Cdd:PRK08392 156 SSRYRVPDLEFIRECIK-RGIKLTFASDAH 184
YciV COG0613
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ...
 1-194 6.29e-10

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


Pssm-ID: 440378 [Multi-domain]  Cd Length: 188  Bit Score: 56.84  E-value: 6.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185   1 MYPVDLHMHTVAStHAYSNLHDYIAAAKQKGVRLLAITDHgpD----MADAPHHWHFINMRIWPrvvdgvgilrGIEANI 76
Cdd:COG0613    1 WMKIDLHVHTTAS-DGSLSPEELVARAKAAGLDVLAITDH--DtvagYEEAAEAAKELGLLVIP----------GVEIST 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185  77 KNREGEIDCTGPMLD-SLDLIVAGFHEPVFAPQDKDANTEAMIATM-ASGTVHIISHPGNPKYPVDIPAVAAAAAKYQV- 153
Cdd:COG0613   68 RWEGREVHILGYGIDpEDPALEALLGIPVEKAEREWLSLEEAIDLIrEAGGVAVLAHPFRYKRGRWLDDLLEELADAGLd 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 495164185 154 ALEINNSSFThsrkgsgPNCKAIAAAVRDAGGWVAL-GSDSH 194
Cdd:COG0613  148 GIEVYNGRHS-------PEDNERAAELAEEYGLLATgGSDAH 182
PHP_HisPPase_Hisj_like cd12110
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; ...
 4-207 1.06e-09

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: 56.80  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185   4 VDLHMHTVASTHAYSNLHDYIAAAKQKGVRLLAITDHGPdMADAPHHWHFINMRI--WPRVV-----------DGVGILR 70
Cdd:cd12110    1 VDYHTHTPRCDHASGTLEEYVEAAIELGFTEIGFSEHAP-LPFEFDDYPESRMAEeeLEDYVeeirrlkekyaDQIEIKL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185  71 GIEAN-IKNREGEI--DCTGPMLDslDLI--------VAGFHEPVFAPQDKDANTEAMIAT--------MASGTVHIISH 131
Cdd:cd12110   80 GLEVDyFPGYEEELreLLYGYPLD--YVIgsvhflggWGFDFPEDGIAEYFEGDIDELYERyfdlvekaIESGLFDIIGH 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185 132 PGNPK--YPVDIPAVAAAAA---------KYQVALEINNSSFthsRKGSG---PNcKAIAAAVRDAGGWVALGSDSHTAF 197
Cdd:cd12110  158 PDLIKkfGKNDEPDEDYEELierilraiaEAGVALEINTAGL---RKPVGepyPS-PEFLELAKELGIPVTLGSDAHSPE 233

                        250
                 ....*....|.
gi 495164185 198 TLG-DFHECRK 207
Cdd:cd12110  234 DVGqGYDEALA 244
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
5-202 9.49e-09

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 55.20  E-value: 9.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185   5 DLHMHTVASThAYSNLHDYIAAAKQKGVRLLAITDH--------GPDMADAPHHWHFInmRIWPRVVDGVGILRGIEANI 76
Cdd:COG1796  339 DLHHHTTWSD-GGASIEEMAAAAAARGYYYIAITDHssslvvagGLDEERLLQQEEEI--DALNERLDGIILLLGGEEDI 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185  77 KNrEGEIDCTGPMLDSLDLIVAGFHepVFAPQDKDANTEAMIATMASGTVHIISHPG------NPKYPVDIPAVAAAAAK 150
Cdd:COG1796  416 LD-DGGLDDDDDLLLEDDDVVAAVH--HSFLLQDEEMTRRRLAAANEPVVVIIHHPTgrlllrRRPYYVDDEAIIAAAAA 492

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495164185 151 YQVALEINNSSFthsrkgSGPNCKAIAAAVRDAGGWVALGSDSHTAFTLGDF 202
Cdd:COG1796  493 AGALEEENNAPR------RLLLLDDLARAAAEGGVVIIIIDDAHHTDLLLDL 538
POLIIIAc smart00481
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ...
 5-78 1.67e-08

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


Pssm-ID: 197753 [Multi-domain]  Cd Length: 67  Bit Score: 49.96  E-value: 1.67e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495164185     5 DLHMHTVAS-THAYSNLHDYIAAAKQKGVRLLAITDHGpdmadapHHWHFINMRIWPRvVDGVGILRGIEANIKN 78
Cdd:smart00481   1 DLHVHSDYSlLDGALSPEELVKRAKELGLKAIAITDHG-------NLFGAVEFYKAAK-KAGIKPIIGLEANIVD 67
PRK07945 PRK07945
PHP domain-containing protein;
5-234 2.04e-08

PHP domain-containing protein;


Pssm-ID: 236135 [Multi-domain]  Cd Length: 335  Bit Score: 53.83  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185   5 DLHMHTVASTHAySNLHDYIAAAKQKGVRLLAITDHGPDMADAphhwhfiN------MRIWPRVVDGVG-------ILRG 71
Cdd:PRK07945  99 DLHTHSDWSDGG-SPIEEMARTAAALGHEYCALTDHSPRLTVA-------NglsaerLRKQLDVVAELNeelapfrILTG 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185  72 IEANIkNREGEIDCTGPMLDSLDLIVAGFHEPVFApqDKDANTEAMIATMASGTVHIISH----------PGNPKYPVDI 141
Cdd:PRK07945 171 IEVDI-LDDGSLDQEPELLDRLDVVVASVHSKLRM--DAAAMTRRMLAAVANPHTDVLGHctgrlvtgnrGTRPESKFDA 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185 142 PAVAAAAAKYQVALEINnssfthSR-KGSGPNCKAIAAAVrDAGGWVALGSDSHTAFTLgDF--HECRKVLdEVDFPEDR 218
Cdd:PRK07945 248 EAVFAACREHGTAVEIN------SRpERRDPPTRLLRLAL-DAGCLFSIDTDAHAPGQL-DWlgYGCERAE-EAGVPADR 318

                        250
                 ....*....|....*..
gi 495164185 219 ILNVSPR-RLLDFLETR 234
Cdd:PRK07945 319 IVNTWPAdRLLAWTGSR 335
PHP pfam02811
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ...
 5-97 7.80e-07

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


Pssm-ID: 460705 [Multi-domain]  Cd Length: 171  Bit Score: 47.92  E-value: 7.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164185    5 DLHMHTvasthAYSNLH------DYIAAAKQKGVRLLAITDHGPdMADAPHHW-HFINMRIWPRVvdgvgilrGIEANIK 77
Cdd:pfam02811   1 HLHVHS-----EYSLLDgaarieELVKRAKELGMPAIAITDHGN-LFGAVEFYkAAKKAGIKPII--------GCEVYVA 66

                          90       100
                  ....*....|....*....|
gi 495164185   78 NREGEiDCTGPMLDSLDLIV 97
Cdd:pfam02811  67 PGSRE-ETEKLLAKYFDLVL 85
PHP_HisPPase_AMP cd07438
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) ...
 4-40 1.40e-06

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: 46.62  E-value: 1.40e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 495164185   4 VDLHMHTVASTHAYSnLHDYIAAAKQKGVRLLAITDH 40
Cdd:cd07438    1 IDLHTHSTASDGTLS-PEELVELAKEAGLKVLAITDH 36
PRK07328 PRK07328
histidinol-phosphatase; Provisional
 1-51 8.51e-06

histidinol-phosphatase; Provisional


Pssm-ID: 235992 [Multi-domain]  Cd Length: 269  Bit Score: 45.78  E-value: 8.51e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495164185   1 MYPVDLHMHTVASTHAYSNLHDYIAAAKQKGVRLLAITDHGPdMADAPHHW 51
Cdd:PRK07328   1 KMLVDYHMHTPLCGHAVGTPEEYVQAARRAGLKEIGFTDHLP-MYFLPPEW 50
polC PRK00448
DNA polymerase III PolC; Validated
 4-41 1.78e-03

DNA polymerase III PolC; Validated


Pssm-ID: 234767 [Multi-domain]  Cd Length: 1437  Bit Score: 39.44  E-value: 1.78e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 495164185    4 VDLHMHTVAST-HAYSNLHDYIAAAKQKGVRLLAITDHG 41
Cdd:PRK00448  335 VELHLHTKMSTmDAIPSVSELVKRAAKWGHKAIAITDHG 373
CehA_McbA_metalo NF038032
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ...
 2-42 2.07e-03

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: 38.84  E-value: 2.07e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 495164185   2 YPVDLHMHTVAStHAYSNLHDYIAAAKQKGVRLLAITDHGP 42
Cdd:NF038032   3 YSGDLHIHTNHS-DGPTTPEELARAALAEGLDVIALTDHNT 42
dnaE PRK06826
DNA polymerase III DnaE; Reviewed
 4-41 4.85e-03

DNA polymerase III DnaE; Reviewed


Pssm-ID: 235868 [Multi-domain]  Cd Length: 1151  Bit Score: 37.95  E-value: 4.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 495164185    4 VDLHMHTvasthAYSNL------HDYIAAAKQKGVRLLAITDHG 41
Cdd:PRK06826    6 VHLHVHT-----EYSLLdgsariKDLIKRAKELGMDSIAITDHG 44
PHP_PolIIIA_POLC cd07435
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III at ...
 4-47 6.58e-03

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: 37.07  E-value: 6.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 495164185   4 VDLHMHTVAST-HAYSNLHDYIAAAKQKGVRLLAITDHG-----PDMADA 47
Cdd:cd07435    2 VELHAHTKMSAmDGVTSVKELVKRAAEWGHKAIAITDHGvvqafPEAYEA 51
hisJ_fam TIGR01856
histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate ...
 5-52 8.17e-03

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: 36.61  E-value: 8.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 495164185    5 DLHMHTVASTHAYSNLHDYIAAAKQKGVRLLAITDHGPDMADAPHHWH 52
Cdd:TIGR01856   2 DSHSHSPFCAHGTDTLREVVQEAIQLGFEEICFTEHAPRPFYYPEEDF 49
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH