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Conserved domains on  [gi|489531215|ref|WP_003435947|]
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PHP domain-containing protein [Clostridioides difficile]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09248 super family cl35794
putative hydrolase; Validated
 1-247 1.84e-121

putative hydrolase; Validated


The actual alignment was detected with superfamily member PRK09248:

Pssm-ID: 236429 [Multi-domain]  Cd Length: 246  Bit Score: 345.67  E-value: 1.84e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215   1 MNFLSDLHTHSIVSGHGYSTLLENINYCKENGIKILGTSEHGPKMPGSPHKWYFHNIQNIPRIINNIIILRGCEANILDI 80
Cdd:PRK09248   1 MKYPVDTHTHTIASGHAYSTLHENAAEAKQKGLKLFAITDHGPDMPGAPHYWHFGNLRVLPRKVDGVGILRGIEANIKNY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215  81 KGNIDLEPFVIPRLDYLILSFHEAVFSPNTLENNTKALINAInKHDNIEILGHLGNSNYPIDYELIIKLAIEKNILIEIN 160
Cdd:PRK09248  81 DGEIDLPGDMLKKLDIVIAGFHEPVFAPGDKETNTQALINAI-KNGRVDIIGHPGNPKYPIDIEAVVKAAKEHNVALEIN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215 161 NCSIkGVSRNGSSDNCKYIATLCKKYGAKIILTSDAHICFDIGNYEYSENILKEINFPDELIMNY-PKKLINHFHQKGKL 239
Cdd:PRK09248 160 NSSF-GHSRKGSEDNCRAIAALCKKAGVWVALGSDAHIAFDIGNFEEALKILDEVGFPEERILNVsPRRLLDFLESRGKA 238


                 ....*...
gi 489531215 240 LDVDYTNI 247
Cdd:PRK09248 239 PIPEFADL 246
 
Name Accession Description Interval E-value
PRK09248 PRK09248
putative hydrolase; Validated
 1-247 1.84e-121

putative hydrolase; Validated


Pssm-ID: 236429 [Multi-domain]  Cd Length: 246  Bit Score: 345.67  E-value: 1.84e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215   1 MNFLSDLHTHSIVSGHGYSTLLENINYCKENGIKILGTSEHGPKMPGSPHKWYFHNIQNIPRIINNIIILRGCEANILDI 80
Cdd:PRK09248   1 MKYPVDTHTHTIASGHAYSTLHENAAEAKQKGLKLFAITDHGPDMPGAPHYWHFGNLRVLPRKVDGVGILRGIEANIKNY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215  81 KGNIDLEPFVIPRLDYLILSFHEAVFSPNTLENNTKALINAInKHDNIEILGHLGNSNYPIDYELIIKLAIEKNILIEIN 160
Cdd:PRK09248  81 DGEIDLPGDMLKKLDIVIAGFHEPVFAPGDKETNTQALINAI-KNGRVDIIGHPGNPKYPIDIEAVVKAAKEHNVALEIN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215 161 NCSIkGVSRNGSSDNCKYIATLCKKYGAKIILTSDAHICFDIGNYEYSENILKEINFPDELIMNY-PKKLINHFHQKGKL 239
Cdd:PRK09248 160 NSSF-GHSRKGSEDNCRAIAALCKKAGVWVALGSDAHIAFDIGNFEEALKILDEVGFPEERILNVsPRRLLDFLESRGKA 238


                 ....*...
gi 489531215 240 LDVDYTNI 247
Cdd:PRK09248 239 PIPEFADL 246
PHP_HisPPase_Ycdx_like cd07437
Polymerase and Histidinol Phosphatase domain of Ycdx like; PHP Ycdx-like is a stand alone PHP ...
 3-236 1.82e-109

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: 314.77  E-value: 1.82e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215   3 FLSDLHTHSIVSGHGYSTLLENINYCKENGIKILGTSEHGPKMPGSPHKWYFHNIQNIPRIINNIIILRGCEANILDIKG 82
Cdd:cd07437    1 ILADLHTHTIASGHAYSTIEEMARAAAEKGLKLLGITDHGPAMPGAPHPWYFGNLKVIPREIYGVRILRGVEANIIDYDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215  83 NIDLEPFVIPRLDYLILSFHEAVFSPNTLENNTKALINAInKHDNIEILGHLGNSNYPIDYELIIKLAIEKNILIEINNC 162
Cdd:cd07437   81 NLDLPERVLKRLDYVIASLHEPCFAPGTKEENTRAYINAM-ENPYVDIIGHPGNPRYPIDYEAVVKAAKEYNVLLEINNS 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489531215 163 SIKGvSRNGSSDNCKYIATLCKKYGAKIILTSDAHICFDIGNYEYSENILKEINFPDELIMNYPKKLINHFHQK 236
Cdd:cd07437  160 SLSP-SRKGSRENCREIAELCKKYGVPVIVGSDAHIAYDIGNFDEALELLEEIGFPEELILNTSPERLLDFLKL 232
HIS2 COG1387
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ...
 4-224 5.30e-33

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: 119.49  E-value: 5.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215   4 LSDLHTHSIVSgHGYSTLLENINYCKENGIKILGTSEHGPkMPGSPH-------KWYFHNIQNIPRIINNIIILRGCEAN 76
Cdd:COG1387    2 RGDLHTHTTYS-DGEGTIEEMVEAAIELGLEYIAITDHSP-SLFVANglseerlLEYLEEIEELNEKYPDIKILKGIEVD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215  77 ILDiKGNIDLEPFVIPRLDYLILSFHeavFSPNTL-ENNTKALINAInKHDNIEILGHL------GNSNYPIDYELIIKL 149
Cdd:COG1387   80 ILP-DGSLDYPDELLAPLDYVIGSVH---SILEEDyEEYTERLLKAI-ENPLVDILGHPdgrllgGRPGYEVDIEEVLEA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489531215 150 AIEKNILIEINncsikgvSRNGSSDNCKYIATLCKKYGAKIILTSDAHICFDIGNYEYSENILKEINFPDELIMN 224
Cdd:COG1387  155 AAENGVALEIN-------TRPLRLDPSDELLKLAKELGVKITIGSDAHSPEDLGDLEYGVALARRAGLTKEDVFN 222
 
Name Accession Description Interval E-value
PRK09248 PRK09248
putative hydrolase; Validated
 1-247 1.84e-121

putative hydrolase; Validated


Pssm-ID: 236429 [Multi-domain]  Cd Length: 246  Bit Score: 345.67  E-value: 1.84e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215   1 MNFLSDLHTHSIVSGHGYSTLLENINYCKENGIKILGTSEHGPKMPGSPHKWYFHNIQNIPRIINNIIILRGCEANILDI 80
Cdd:PRK09248   1 MKYPVDTHTHTIASGHAYSTLHENAAEAKQKGLKLFAITDHGPDMPGAPHYWHFGNLRVLPRKVDGVGILRGIEANIKNY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215  81 KGNIDLEPFVIPRLDYLILSFHEAVFSPNTLENNTKALINAInKHDNIEILGHLGNSNYPIDYELIIKLAIEKNILIEIN 160
Cdd:PRK09248  81 DGEIDLPGDMLKKLDIVIAGFHEPVFAPGDKETNTQALINAI-KNGRVDIIGHPGNPKYPIDIEAVVKAAKEHNVALEIN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215 161 NCSIkGVSRNGSSDNCKYIATLCKKYGAKIILTSDAHICFDIGNYEYSENILKEINFPDELIMNY-PKKLINHFHQKGKL 239
Cdd:PRK09248 160 NSSF-GHSRKGSEDNCRAIAALCKKAGVWVALGSDAHIAFDIGNFEEALKILDEVGFPEERILNVsPRRLLDFLESRGKA 238


                 ....*...
gi 489531215 240 LDVDYTNI 247
Cdd:PRK09248 239 PIPEFADL 246
PHP_HisPPase_Ycdx_like cd07437
Polymerase and Histidinol Phosphatase domain of Ycdx like; PHP Ycdx-like is a stand alone PHP ...
 3-236 1.82e-109

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: 314.77  E-value: 1.82e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215   3 FLSDLHTHSIVSGHGYSTLLENINYCKENGIKILGTSEHGPKMPGSPHKWYFHNIQNIPRIINNIIILRGCEANILDIKG 82
Cdd:cd07437    1 ILADLHTHTIASGHAYSTIEEMARAAAEKGLKLLGITDHGPAMPGAPHPWYFGNLKVIPREIYGVRILRGVEANIIDYDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215  83 NIDLEPFVIPRLDYLILSFHEAVFSPNTLENNTKALINAInKHDNIEILGHLGNSNYPIDYELIIKLAIEKNILIEINNC 162
Cdd:cd07437   81 NLDLPERVLKRLDYVIASLHEPCFAPGTKEENTRAYINAM-ENPYVDIIGHPGNPRYPIDYEAVVKAAKEYNVLLEINNS 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489531215 163 SIKGvSRNGSSDNCKYIATLCKKYGAKIILTSDAHICFDIGNYEYSENILKEINFPDELIMNYPKKLINHFHQK 236
Cdd:cd07437  160 SLSP-SRKGSRENCREIAELCKKYGVPVIVGSDAHIAYDIGNFDEALELLEEIGFPEELILNTSPERLLDFLKL 232
HIS2 COG1387
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ...
 4-224 5.30e-33

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: 119.49  E-value: 5.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215   4 LSDLHTHSIVSgHGYSTLLENINYCKENGIKILGTSEHGPkMPGSPH-------KWYFHNIQNIPRIINNIIILRGCEAN 76
Cdd:COG1387    2 RGDLHTHTTYS-DGEGTIEEMVEAAIELGLEYIAITDHSP-SLFVANglseerlLEYLEEIEELNEKYPDIKILKGIEVD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215  77 ILDiKGNIDLEPFVIPRLDYLILSFHeavFSPNTL-ENNTKALINAInKHDNIEILGHL------GNSNYPIDYELIIKL 149
Cdd:COG1387   80 ILP-DGSLDYPDELLAPLDYVIGSVH---SILEEDyEEYTERLLKAI-ENPLVDILGHPdgrllgGRPGYEVDIEEVLEA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489531215 150 AIEKNILIEINncsikgvSRNGSSDNCKYIATLCKKYGAKIILTSDAHICFDIGNYEYSENILKEINFPDELIMN 224
Cdd:COG1387  155 AAENGVALEIN-------TRPLRLDPSDELLKLAKELGVKITIGSDAHSPEDLGDLEYGVALARRAGLTKEDVFN 222
PRK08392 PRK08392
hypothetical protein; Provisional
 6-214 2.82e-18

hypothetical protein; Provisional


Pssm-ID: 169423 [Multi-domain]  Cd Length: 215  Bit Score: 80.21  E-value: 2.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215   6 DLHTHSIVSgHGYSTLLENINYCKENGIKILGTSEHGPKMPGSPHKWYFHNIQNIPRIINNIIiLRGCEANILDikGNID 85
Cdd:PRK08392   2 DLHTHTVYS-DGIGSVRDNIAEAERKGLRLVGISDHIHYFTPSKFNAYINEIRQWGEESEIVV-LAGIEANITP--NGVD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215  86 LEPFVIPRLDYLILSFHEAVFSPNT---LENNTKALINainkhDNIEILGHLGNS----NYPIDYEL--IIKLAIEKNIL 156
Cdd:PRK08392  78 ITDDFAKKLDYVIASVHEWFGRPEHheyIELVKLALMD-----ENVDIIGHFGNSfpyiGYPSEEELkeILDLAEAYGKA 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489531215 157 IEINncsikgvSRNGSSDnCKYIaTLCKKYGAKIILTSDAHICFDIGNYEYSENILKE 214
Cdd:PRK08392 153 FEIS-------SRYRVPD-LEFI-RECIKRGIKLTFASDAHRPEDVGNVSWSLKVFKK 201
PHP_PolX cd07436
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal ...
 70-207 5.11e-12

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: 63.59  E-value: 5.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215  70 LRGCEANILDiKGNIDLEPFVIPRLDYLILSFHEAvFSPNTlENNTKALINAInKHDNIEILGH------LGNSNYPIDY 143
Cdd:cd07436   77 LKGIEVDILP-DGSLDYPDEVLAELDVVVASVHSG-FNQSE-EEMTERLLKAI-ENPHVDILGHptgrllGRREGYEVDM 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489531215 144 ELIIKLAIEKNILIEINncsikgvsrngSS--------DNCKYiatlCKKYGAKIILTSDAHICFDIGNYEY 207
Cdd:cd07436  153 ERVIEAAAETGTALEIN-----------ANpdrldlddRHARR----AKEAGVKIAINTDAHSTDGLDNMRY 209
PHP_HisPPase_Hisj_like cd12110
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; ...
 5-197 2.32e-08

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: 52.95  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215   5 SDLHTHSIVSGHGYSTLLENINYCKENGIKILGTSEHGPkMPGSPhKWYFHNIQNIPRIINNIIILR------------- 71
Cdd:cd12110    1 VDYHTHTPRCDHASGTLEEYVEAAIELGFTEIGFSEHAP-LPFEF-DDYPESRMAEEELEDYVEEIRrlkekyadqieik 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215  72 -GCEANILDIKGNIDLEPFVIPRLDYLILSFHeavFSPNTLENNTKALINAINKHDNIE-------------------IL 131
Cdd:cd12110   79 lGLEVDYFPGYEEELRELLYGYPLDYVIGSVH---FLGGWGFDFPEDGIAEYFEGDIDElyeryfdlvekaiesglfdII 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215 132 GHLG-----------NSNYPIDYELIIKLAIEKNILIEINncsIKGVSRNgssDNCKY----IATLCKKYGAKIILTSDA 196
Cdd:cd12110  156 GHPDlikkfgkndepDEDYEELIERILRAIAEAGVALEIN---TAGLRKP---VGEPYpspeFLELAKELGIPVTLGSDA 229


                 .
gi 489531215 197 H 197
Cdd:cd12110  230 H 230
PHP_HisPPase cd07432
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ...
 6-198 5.46e-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: 44.54  E-value: 5.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215   6 DLHTHSIVSGHGYSTLLENINYCKENGIKILGTSEHgpkmpgsphkwyfhniqnipriinniIILRGCEANILDIKGNid 85
Cdd:cd07432    2 DLHIHSVFSPDSDMTPEEIVERAIELGLDGIAITDH--------------------------NTIDGAEEALKEAYKD-- 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215  86 lEPFVIPRLDYlilsfheavfspntlenntkalinainkhdNIEILGHLGNSNYPIDYELIIKLAIEKNILIEINNcsik 165
Cdd:cd07432   54 -GLLVIPGVEV------------------------------TLVVLAHPDRPSRYGLSDLILKPLIKNGDAIEVNN---- 98

                        170       180       190
                 ....*....|....*....|....*....|...
gi 489531215 166 gvSRNGSSDNCKYIATLCKKYGAKIILTSDAHI 198
Cdd:cd07432   99 --SRLRYGLNNLAAKRYAELGGLPITGGSDAHT 129
PHP cd07309
Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2 ...
 6-77 2.14e-05

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: 42.03  E-value: 2.14e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489531215   6 DLHTHSIVSGHGYSTLLENINYCKENGIKILGTSEHGPKMPGSPHKWYFHNIQNIPRIINNIIILRGCEANI 77
Cdd:cd07309    2 DLHTHTVFSDGDHAKLTELVDKAKELGPDALAITDHGNLRGLAEFNTAGK*NHIKAAEAAGIKIIIGSEVNL 73
PRK06361 PRK06361
histidinol phosphate phosphatase domain-containing protein;
126-229 9.91e-05

histidinol phosphate phosphatase domain-containing protein;


Pssm-ID: 180543 [Multi-domain]  Cd Length: 212  Bit Score: 42.25  E-value: 9.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531215 126 DNIEILGHLGnsnyPIDYElIIKLAIEKNILIEINNCsiKGVSR-NGssdnckYIATLCKKYGAKIILTSDAHICFDIGN 204
Cdd:PRK06361 112 EDVDILAHPG----LITEE-EAELAAENGVFLEITAR--KGHSLtNG------HVARIAREAGAPLVINTDTHAPSDLIT 178

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489531215 205 YEYSENI-------LKEINfpdELIMNYPKKL 229
Cdd:PRK06361 179 YEFARKValgagltEKELE---EALENNPKLL 207
PRK00912 PRK00912
ribonuclease P protein component 3; Provisional
 148-202 2.43e-03

ribonuclease P protein component 3; Provisional


Pssm-ID: 234862 [Multi-domain]  Cd Length: 237  Bit Score: 38.07  E-value: 2.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489531215 148 KLAIEKNILIEINNCSI---KGVSRNGSSDNCKYIATLCKKYGAKIILTSDAHICFDI 202
Cdd:PRK00912 125 KEAARNNVAIEFNLRDIlksRGGRRARTLSNFRDNLALARKYDFPLVLTSGAMSCYDL 182
 
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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