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Conserved domains on  [gi|727169850|ref|WP_033638063|]
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MULTISPECIES: phosphatase [Serratia]

Protein Classification

phosphatase( domain architecture ID 11483686)

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
PRK09248 PRK09248
putative hydrolase; Validated
 1-245 7.18e-168

putative hydrolase; Validated


:

Pssm-ID: 236429 [Multi-domain]  Cd Length: 246  Bit Score: 462.77  E-value: 7.18e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850   1 MYPVDLHMHTVASTHAYSTLHDYIAEAQQKGIKLFAITDHGPDMADAPHYWHFMNMHVWPRLVNGVGILRGIEANIKNLQ 80
Cdd:PRK09248   2 KYPVDTHTHTIASGHAYSTLHENAAEAKQKGLKLFAITDHGPDMPGAPHYWHFGNLRVLPRKVDGVGILRGIEANIKNYD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850  81 GDIDCTGPMLTATDVIIAGFHEPVFAPQDKASNTEAMIAAMAQGDVHIISHPGNPRYPIDIPAVAAAAAKYEVALELNNS 160
Cdd:PRK09248  82 GEIDLPGDMLKKLDIVIAGFHEPVFAPGDKETNTQALINAIKNGRVDIIGHPGNPKYPIDIEAVVKAAKEHNVALEINNS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850 161 SFTHSRKGSEANCRAIAAAVRDAGGWLALGSDSHVAFSLGNFEHCERIIEEVGFPQARILNVSPRRLLDFLERRGKPAIA 240
Cdd:PRK09248 162 SFGHSRKGSEDNCRAIAALCKKAGVWVALGSDAHIAFDIGNFEEALKILDEVGFPEERILNVSPRRLLDFLESRGKAPIP 241


                 ....*
gi 727169850 241 ELADL 245
Cdd:PRK09248 242 EFADL 246
 
Name Accession Description Interval E-value
PRK09248 PRK09248
putative hydrolase; Validated
 1-245 7.18e-168

putative hydrolase; Validated


Pssm-ID: 236429 [Multi-domain]  Cd Length: 246  Bit Score: 462.77  E-value: 7.18e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850   1 MYPVDLHMHTVASTHAYSTLHDYIAEAQQKGIKLFAITDHGPDMADAPHYWHFMNMHVWPRLVNGVGILRGIEANIKNLQ 80
Cdd:PRK09248   2 KYPVDTHTHTIASGHAYSTLHENAAEAKQKGLKLFAITDHGPDMPGAPHYWHFGNLRVLPRKVDGVGILRGIEANIKNYD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850  81 GDIDCTGPMLTATDVIIAGFHEPVFAPQDKASNTEAMIAAMAQGDVHIISHPGNPRYPIDIPAVAAAAAKYEVALELNNS 160
Cdd:PRK09248  82 GEIDLPGDMLKKLDIVIAGFHEPVFAPGDKETNTQALINAIKNGRVDIIGHPGNPKYPIDIEAVVKAAKEHNVALEINNS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850 161 SFTHSRKGSEANCRAIAAAVRDAGGWLALGSDSHVAFSLGNFEHCERIIEEVGFPQARILNVSPRRLLDFLERRGKPAIA 240
Cdd:PRK09248 162 SFGHSRKGSEDNCRAIAALCKKAGVWVALGSDAHIAFDIGNFEEALKILDEVGFPEERILNVSPRRLLDFLESRGKAPIP 241


                 ....*
gi 727169850 241 ELADL 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 5.29e-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: 5.29e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850   2 YPVDLHMHTVASTHAYSTLHDYIAEAQQKGIKLFAITDHGPDMADAPHYWHFMNMHVWPRLVNGVGILRGIEANIKNLQG 81
Cdd:cd07437    1 ILADLHTHTIASGHAYSTIEEMARAAAEKGLKLLGITDHGPAMPGAPHPWYFGNLKVIPREIYGVRILRGVEANIIDYDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850  82 DIDCTGPMLTATDVIIAGFHEPVFAPQDKASNTEAMIAAMAQGDVHIISHPGNPRYPIDIPAVAAAAAKYEVALELNNSS 161
Cdd:cd07437   81 NLDLPERVLKRLDYVIASLHEPCFAPGTKEENTRAYINAMENPYVDIIGHPGNPRYPIDYEAVVKAAKEYNVLLEINNSS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727169850 162 FTHSRKGSEANCRAIAAAVRDAGGWLALGSDSHVAFSLGNFEHCERIIEEVGFPQARILNVSPRRLLDFLERR 234
Cdd:cd07437  161 LSPSRKGSRENCREIAELCKKYGVPVIVGSDAHIAYDIGNFDEALELLEEIGFPEELILNTSPERLLDFLKLR 233
HIS2 COG1387
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ...
 4-226 1.01e-32

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: 118.72  E-value: 1.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850   4 VDLHMHTVAStHAYSTLHDYIAEAQQKGIKLFAITDHGP--------DMADAPHYWHFMNmhvwpRL---VNGVGILRGI 72
Cdd:COG1387    3 GDLHTHTTYS-DGEGTIEEMVEAAIELGLEYIAITDHSPslfvanglSEERLLEYLEEIE-----ELnekYPDIKILKGI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850  73 EANIKNLqGDIDCTGPMLTATDVIIAGFHEpvFAPQDKASNTEAMIAAMAQGDVHIISHP------GNPRYPIDIPAVAA 146
Cdd:COG1387   77 EVDILPD-GSLDYPDELLAPLDYVIGSVHS--ILEEDYEEYTERLLKAIENPLVDILGHPdgrllgGRPGYEVDIEEVLE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850 147 AAAKYEVALELNNSSFthsRKGSeanCRAIAAAVRDAGGWLALGSDSHVAFSLGNFEHCERIIEEVGFPQARILNVSPRR 226
Cdd:COG1387  154 AAAENGVALEINTRPL---RLDP---SDELLKLAKELGVKITIGSDAHSPEDLGDLEYGVALARRAGLTKEDVFNTLRKE 227
POLIIIAc smart00481
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ...
 5-78 6.25e-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: 48.42  E-value: 6.25e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727169850     5 DLHMHTVAS-THAYSTLHDYIAEAQQKGIKLFAITDHGpdmadapHYWHFMNMHVWPRlVNGVGILRGIEANIKN 78
Cdd:smart00481   1 DLHVHSDYSlLDGALSPEELVKRAKELGLKAIAITDHG-------NLFGAVEFYKAAK-KAGIKPIIGLEANIVD 67
PHP pfam02811
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ...
 5-76 3.99e-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: 48.69  E-value: 3.99e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727169850    5 DLHMHTvasthAYSTLH------DYIAEAQQKGIKLFAITDHGPdMADAPHYWHFMNMHvwprlvnGVGILRGIEANI 76
Cdd:pfam02811   1 HLHVHS-----EYSLLDgaarieELVKRAKELGMPAIAITDHGN-LFGAVEFYKAAKKA-------GIKPIIGCEVYV 65
hisJ_fam TIGR01856
histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate ...
 5-52 2.47e-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: 41.23  E-value: 2.47e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 727169850    5 DLHMHTVASTHAYSTLHDYIAEAQQKGIKLFAITDHGPDMADAPHYWH 52
Cdd:TIGR01856   2 DSHSHSPFCAHGTDTLREVVQEAIQLGFEEICFTEHAPRPFYYPEEDF 49
 
Name Accession Description Interval E-value
PRK09248 PRK09248
putative hydrolase; Validated
 1-245 7.18e-168

putative hydrolase; Validated


Pssm-ID: 236429 [Multi-domain]  Cd Length: 246  Bit Score: 462.77  E-value: 7.18e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850   1 MYPVDLHMHTVASTHAYSTLHDYIAEAQQKGIKLFAITDHGPDMADAPHYWHFMNMHVWPRLVNGVGILRGIEANIKNLQ 80
Cdd:PRK09248   2 KYPVDTHTHTIASGHAYSTLHENAAEAKQKGLKLFAITDHGPDMPGAPHYWHFGNLRVLPRKVDGVGILRGIEANIKNYD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850  81 GDIDCTGPMLTATDVIIAGFHEPVFAPQDKASNTEAMIAAMAQGDVHIISHPGNPRYPIDIPAVAAAAAKYEVALELNNS 160
Cdd:PRK09248  82 GEIDLPGDMLKKLDIVIAGFHEPVFAPGDKETNTQALINAIKNGRVDIIGHPGNPKYPIDIEAVVKAAKEHNVALEINNS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850 161 SFTHSRKGSEANCRAIAAAVRDAGGWLALGSDSHVAFSLGNFEHCERIIEEVGFPQARILNVSPRRLLDFLERRGKPAIA 240
Cdd:PRK09248 162 SFGHSRKGSEDNCRAIAALCKKAGVWVALGSDAHIAFDIGNFEEALKILDEVGFPEERILNVSPRRLLDFLESRGKAPIP 241


                 ....*
gi 727169850 241 ELADL 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 5.29e-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: 5.29e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850   2 YPVDLHMHTVASTHAYSTLHDYIAEAQQKGIKLFAITDHGPDMADAPHYWHFMNMHVWPRLVNGVGILRGIEANIKNLQG 81
Cdd:cd07437    1 ILADLHTHTIASGHAYSTIEEMARAAAEKGLKLLGITDHGPAMPGAPHPWYFGNLKVIPREIYGVRILRGVEANIIDYDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850  82 DIDCTGPMLTATDVIIAGFHEPVFAPQDKASNTEAMIAAMAQGDVHIISHPGNPRYPIDIPAVAAAAAKYEVALELNNSS 161
Cdd:cd07437   81 NLDLPERVLKRLDYVIASLHEPCFAPGTKEENTRAYINAMENPYVDIIGHPGNPRYPIDYEAVVKAAKEYNVLLEINNSS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727169850 162 FTHSRKGSEANCRAIAAAVRDAGGWLALGSDSHVAFSLGNFEHCERIIEEVGFPQARILNVSPRRLLDFLERR 234
Cdd:cd07437  161 LSPSRKGSRENCREIAELCKKYGVPVIVGSDAHIAYDIGNFDEALELLEEIGFPEELILNTSPERLLDFLKLR 233
HIS2 COG1387
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ...
 4-226 1.01e-32

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: 118.72  E-value: 1.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850   4 VDLHMHTVAStHAYSTLHDYIAEAQQKGIKLFAITDHGP--------DMADAPHYWHFMNmhvwpRL---VNGVGILRGI 72
Cdd:COG1387    3 GDLHTHTTYS-DGEGTIEEMVEAAIELGLEYIAITDHSPslfvanglSEERLLEYLEEIE-----ELnekYPDIKILKGI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850  73 EANIKNLqGDIDCTGPMLTATDVIIAGFHEpvFAPQDKASNTEAMIAAMAQGDVHIISHP------GNPRYPIDIPAVAA 146
Cdd:COG1387   77 EVDILPD-GSLDYPDELLAPLDYVIGSVHS--ILEEDYEEYTERLLKAIENPLVDILGHPdgrllgGRPGYEVDIEEVLE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850 147 AAAKYEVALELNNSSFthsRKGSeanCRAIAAAVRDAGGWLALGSDSHVAFSLGNFEHCERIIEEVGFPQARILNVSPRR 226
Cdd:COG1387  154 AAAENGVALEINTRPL---RLDP---SDELLKLAKELGVKITIGSDAHSPEDLGDLEYGVALARRAGLTKEDVFNTLRKE 227
PHP cd07309
Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2 ...
 4-76 1.46e-19

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: 80.16  E-value: 1.46e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727169850   4 VDLHMHTVASTHAYSTLHDYIAEAQQKGIKLFAITDHGPDMADAPHYWHFMNMHVWPRLVNGVGILRGIEANI 76
Cdd:cd07309    1 VDLHTHTVFSDGDHAKLTELVDKAKELGPDALAITDHGNLRGLAEFNTAGK*NHIKAAEAAGIKIIIGSEVNL 73
PHP_PolX cd07436
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal ...
 5-203 8.83e-17

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: 76.69  E-value: 8.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850   5 DLHMHTVASTHAySTLHDYIAEAQQKGIKLFAITDHGPDmadaphywhfmnmhvwPRLVNGVG----------------- 67
Cdd:cd07436    8 DLHVHTTWSDGR-NSIEEMAEAARALGYEYIAITDHSKS----------------LRVANGLSeerlreqieeidalnek 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850  68 -----ILRGIEANIKNlQGDIDCTGPMLTATDVIIA----GFHepvfapQDKASNTEAMIAAMAQGDVHIISHP------ 132
Cdd:cd07436   71 lpgirILKGIEVDILP-DGSLDYPDEVLAELDVVVAsvhsGFN------QSEEEMTERLLKAIENPHVDILGHPtgrllg 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727169850 133 GNPRYPIDIPAVAAAAAKYEVALELNNSSfthSRkgSEANCRAIAAAvRDAGGWLALGSDSHVAFSLGNFE 203
Cdd:cd07436  144 RREGYEVDMERVIEAAAETGTALEINANP---DR--LDLDDRHARRA-KEAGVKIAINTDAHSTDGLDNMR 208
PRK08392 PRK08392
hypothetical protein; Provisional
 5-213 2.70e-13

hypothetical protein; Provisional


Pssm-ID: 169423 [Multi-domain]  Cd Length: 215  Bit Score: 66.73  E-value: 2.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850   5 DLHMHTVASThAYSTLHDYIAEAQQKGIKLFAITDHgpdmadaPHYWHFMNMHVWPRLVNGVG------ILRGIEANIkn 78
Cdd:PRK08392   2 DLHTHTVYSD-GIGSVRDNIAEAERKGLRLVGISDH-------IHYFTPSKFNAYINEIRQWGeeseivVLAGIEANI-- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850  79 LQGDIDCTGPMLTATDVIIAGFHEpVFAPQDKASNTEAMIAAMAQGDVHIISHPGNPRYPIDIPAVAAAAAKYEVAlELN 158
Cdd:PRK08392  72 TPNGVDITDDFAKKLDYVIASVHE-WFGRPEHHEYIELVKLALMDENVDIIGHFGNSFPYIGYPSEEELKEILDLA-EAY 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 727169850 159 NSSFTHSRKGSEANCRAIAAAVRdAGGWLALGSDSHVAFSLGNFEHCERIIEEVG 213
Cdd:PRK08392 150 GKAFEISSRYRVPDLEFIRECIK-RGIKLTFASDAHRPEDVGNVSWSLKVFKKAG 203
PHP_HisPPase cd07432
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ...
 4-195 2.37e-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: 59.56  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850   4 VDLHMHTVASTHAYSTLHDYIAEAQQKGIKLFAITDHgpDMADAPHYwhfmnmHVWPRLVNGVGILRGIEANIknlqgdi 83
Cdd:cd07432    1 ADLHIHSVFSPDSDMTPEEIVERAIELGLDGIAITDH--NTIDGAEE------ALKEAYKDGLLVIPGVEVTL------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850  84 dctgpmltatdviiagfhepvfapqdkasnteamiaamaqgdvHIISHPGNPRYPIDIPAVAAAAAKYEVALELNNSSFT 163
Cdd:cd07432   66 -------------------------------------------VVLAHPDRPSRYGLSDLILKPLIKNGDAIEVNNSRLR 102

                        170       180       190
                 ....*....|....*....|....*....|..
gi 727169850 164 HsrkgsEANCRAIAAAVRDAGGWLALGSDSHV 195
Cdd:cd07432  103 Y-----GLNNLAAKRYAELGGLPITGGSDAHT 129
PRK08609 PRK08609
DNA polymerase/3'-5' exonuclease PolX;
5-233 7.58e-10

DNA polymerase/3'-5' exonuclease PolX;


Pssm-ID: 236311 [Multi-domain]  Cd Length: 570  Bit Score: 58.43  E-value: 7.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850   5 DLHMHTVASTHAYSTlhDYIAEA-QQKGIKLFAITDHGpdmadapHYWHFMNMHVWPRL-------------VNGVGILR 70
Cdd:PRK08609 337 DLHMHTTWSDGAFSI--EEMVEAcIAKGYEYMAITDHS-------QYLKVANGLTEERLleqaeeikalnekYPEIDILS 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850  71 GIEANIKNlQGDIDCTGPMLTATDVIIAGFHEPVFAPQDKAsnTEAMIAAMAQGDVHIISHPG------NPRYPIDIPAV 144
Cdd:PRK08609 408 GIEMDILP-DGSLDYDDEVLAELDYVIAAIHSSFSQSEEEI--MKRLENACRNPYVRLIAHPTgrligrRDGYDVNIDQL 484

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850 145 AAAAAKYEVALELNnssfthsrkgseAN------CRAIAAAVRDAGGWLALGSDSHvafslgNFEHCERIieEVGFPQAR 218
Cdd:PRK08609 485 IELAKETNTALELN------------ANpnrldlSAEHLKKAQEAGVKLAINTDAH------HTEMLDDM--KYGVATAR 544

                        250       260
                 ....*....|....*....|....
gi 727169850 219 --------ILNVSPR-RLLDFLER 233
Cdd:PRK08609 545 kgwiqkdrVINTWSReEFKDFIKR 568
YciV COG0613
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ...
 1-194 7.98e-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: 56.46  E-value: 7.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850   1 MYPVDLHMHTVAStHAYSTLHDYIAEAQQKGIKLFAITDHgpD----MADAPHYWHFMNMHVWPrlvngvgilrGIE--A 74
Cdd:COG0613    1 WMKIDLHVHTTAS-DGSLSPEELVARAKAAGLDVLAITDH--DtvagYEEAAEAAKELGLLVIP----------GVEisT 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169850  75 NIKNLQGDI-----DCTGPMLTATDVIiagfhePVFAPQDKASNTEAMIAAM-AQGDVHIISHPGNPRYPIDIPAVAAAA 148
Cdd:COG0613   68 RWEGREVHIlgygiDPEDPALEALLGI------PVEKAEREWLSLEEAIDLIrEAGGVAVLAHPFRYKRGRWLDDLLEEL 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 727169850 149 AKYEV-ALELNNSSFTHSRkgseancRAIAAAVRDAGGWLAL-GSDSH 194
Cdd:COG0613  142 ADAGLdGIEVYNGRHSPED-------NERAAELAEEYGLLATgGSDAH 182
POLIIIAc smart00481
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ...
 5-78 6.25e-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: 48.42  E-value: 6.25e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727169850     5 DLHMHTVAS-THAYSTLHDYIAEAQQKGIKLFAITDHGpdmadapHYWHFMNMHVWPRlVNGVGILRGIEANIKN 78
Cdd:smart00481   1 DLHVHSDYSlLDGALSPEELVKRAKELGLKAIAITDHG-------NLFGAVEFYKAAK-KAGIKPIIGLEANIVD 67
PHP pfam02811
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ...
 5-76 3.99e-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: 48.69  E-value: 3.99e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727169850    5 DLHMHTvasthAYSTLH------DYIAEAQQKGIKLFAITDHGPdMADAPHYWHFMNMHvwprlvnGVGILRGIEANI 76
Cdd:pfam02811   1 HLHVHS-----EYSLLDgaarieELVKRAKELGMPAIAITDHGN-LFGAVEFYKAAKKA-------GIKPIIGCEVYV 65
PHP_HisPPase_AMP cd07438
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) ...
 4-40 2.03e-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: 46.23  E-value: 2.03e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 727169850   4 VDLHMHTVASTHAYSTlHDYIAEAQQKGIKLFAITDH 40
Cdd:cd07438    1 IDLHTHSTASDGTLSP-EELVELAKEAGLKVLAITDH 36
PHP_HisPPase_Hisj_like cd12110
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; ...
 4-56 6.36e-06

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: 46.02  E-value: 6.36e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 727169850   4 VDLHMHTVASTHAYSTLHDYIAEAQQKGIKLFAITDHGPdMADAPHYWHFMNM 56
Cdd:cd12110    1 VDYHTHTPRCDHASGTLEEYVEAAIELGFTEIGFSEHAP-LPFEFDDYPESRM 52
PRK07328 PRK07328
histidinol-phosphatase; Provisional
 1-51 1.02e-05

histidinol-phosphatase; Provisional


Pssm-ID: 235992 [Multi-domain]  Cd Length: 269  Bit Score: 45.40  E-value: 1.02e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 727169850   1 MYPVDLHMHTVASTHAYSTLHDYIAEAQQKGIKLFAITDHGPdMADAPHYW 51
Cdd:PRK07328   1 KMLVDYHMHTPLCGHAVGTPEEYVQAARRAGLKEIGFTDHLP-MYFLPPEW 50
hisJ_fam TIGR01856
histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate ...
 5-52 2.47e-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: 41.23  E-value: 2.47e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 727169850    5 DLHMHTVASTHAYSTLHDYIAEAQQKGIKLFAITDHGPDMADAPHYWH 52
Cdd:TIGR01856   2 DSHSHSPFCAHGTDTLREVVQEAIQLGFEEICFTEHAPRPFYYPEEDF 49
polC PRK00448
DNA polymerase III PolC; Validated
 4-76 9.34e-03

DNA polymerase III PolC; Validated


Pssm-ID: 234767 [Multi-domain]  Cd Length: 1437  Bit Score: 37.12  E-value: 9.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727169850    4 VDLHMHTVAST-HAYSTLHDYIAEAQQKGIKLFAITDHG-----PDMADAPHYwhfmnmhvwprlvNGVGILRGIEANI 76
Cdd:PRK00448  335 VELHLHTKMSTmDAIPSVSELVKRAAKWGHKAIAITDHGvvqafPEAYNAAKK-------------AGIKVIYGVEANL 400
 
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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