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Conserved domains on  [gi|1743416780|gb|KAA3602904|]
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PHP domain-containing protein [Calditrichaeota bacterium]

Protein Classification

PHP domain-containing protein( domain architecture ID 10165079)

uncharacterized protein containing a polymerase and histidinol phosphatase (PHP) domain, similar to the C-terminal PHP domain of bacterial polymerase X

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHP_PolX cd07436
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal ...
 156-390 5.23e-145

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: 410.66  E-value: 5.23e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 156 QEKEILGVFHNHTTWSDGSASLEEMAKEAQNLGYSYIGISDHSKTAFYANGLTESRIAEQHAEIDKLNEEMENFKIFKGI 235
Cdd:cd07436     1 ELKDIRGDLHVHTTWSDGRNSIEEMAEAARALGYEYIAITDHSKSLRVANGLSEERLREQIEEIDALNEKLPGIRILKGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 236 ESDILNDGSLDYDDSILENFDFVIASVHSNFKMSEEEMTKRLIKAIENPYTTMLGHLTGRLLLARPEYKLNMQKIIDACS 315
Cdd:cd07436    81 EVDILPDGSLDYPDEVLAELDVVVASVHSGFNQSEEEMTERLLKAIENPHVDILGHPTGRLLGRREGYEVDMERVIEAAA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743416780 316 QNDVCIELNASPHRLDLDWRLMQSAFEKGVKISINPDAHSLTGLQDVKYGIKVARRGGAQRENVLNTKNFETVLE 390
Cdd:cd07436   161 ETGTALEINANPDRLDLDDRHARRAKEAGVKIAINTDAHSTDGLDNMRYGVGTARRGWLEKEDVLNTLPLEELLK 235
 
Name Accession Description Interval E-value
PHP_PolX cd07436
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal ...
 156-390 5.23e-145

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: 410.66  E-value: 5.23e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 156 QEKEILGVFHNHTTWSDGSASLEEMAKEAQNLGYSYIGISDHSKTAFYANGLTESRIAEQHAEIDKLNEEMENFKIFKGI 235
Cdd:cd07436     1 ELKDIRGDLHVHTTWSDGRNSIEEMAEAARALGYEYIAITDHSKSLRVANGLSEERLREQIEEIDALNEKLPGIRILKGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 236 ESDILNDGSLDYDDSILENFDFVIASVHSNFKMSEEEMTKRLIKAIENPYTTMLGHLTGRLLLARPEYKLNMQKIIDACS 315
Cdd:cd07436    81 EVDILPDGSLDYPDEVLAELDVVVASVHSGFNQSEEEMTERLLKAIENPHVDILGHPTGRLLGRREGYEVDMERVIEAAA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743416780 316 QNDVCIELNASPHRLDLDWRLMQSAFEKGVKISINPDAHSLTGLQDVKYGIKVARRGGAQRENVLNTKNFETVLE 390
Cdd:cd07436   161 ETGTALEINANPDRLDLDDRHARRAKEAGVKIAINTDAHSTDGLDNMRYGVGTARRGWLEKEDVLNTLPLEELLK 235
HIS2 COG1387
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ...
 160-390 1.53e-113

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: 330.96  E-value: 1.53e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 160 ILGVFHNHTTWSDGSASLEEMAKEAQNLGYSYIGISDHSKTAFYANGLTESRIAEQHAEIDKLNEEMENFKIFKGIESDI 239
Cdd:COG1387     1 MRGDLHTHTTYSDGEGTIEEMVEAAIELGLEYIAITDHSPSLFVANGLSEERLLEYLEEIEELNEKYPDIKILKGIEVDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 240 LNDGSLDYDDSILENFDFVIASVHSNFKMSEEEMTKRLIKAIENPYTTMLGHLTGRLLLARPEYKLNMQKIIDACSQNDV 319
Cdd:COG1387    81 LPDGSLDYPDELLAPLDYVIGSVHSILEEDYEEYTERLLKAIENPLVDILGHPDGRLLGGRPGYEVDIEEVLEAAAENGV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743416780 320 CIELNASPHRLDLDWRLMQSAFEKGVKISINPDAHSLTGLQDVKYGIKVARRGGAQRENVLNTKNFETVLE 390
Cdd:COG1387   161 ALEINTRPLRLDPSDELLKLAKELGVKITIGSDAHSPEDLGDLEYGVALARRAGLTKEDVFNTLRKEELLK 231
PRK08609 PRK08609
DNA polymerase/3'-5' exonuclease PolX;
120-386 1.63e-93

DNA polymerase/3'-5' exonuclease PolX;


Pssm-ID: 236311 [Multi-domain]  Cd Length: 570  Bit Score: 291.09  E-value: 1.63e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 120 FRTEEEVFQVKKIKYIFPEVRHFG--VEKGSKVSEnLVQEKEILGVFHNHTTWSDGSASLEEMAKEAQNLGYSYIGISDH 197
Cdd:PRK08609  293 FESEEAFFAHFGLPFIPPEVREDGseFERYKDLSN-LITLSDIQGDLHMHTTWSDGAFSIEEMVEACIAKGYEYMAITDH 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 198 SKTAFYANGLTESRIAEQHAEIDKLNEEMENFKIFKGIESDILNDGSLDYDDSILENFDFVIASVHSNFKMSEEEMTKRL 277
Cdd:PRK08609  372 SQYLKVANGLTEERLLEQAEEIKALNEKYPEIDILSGIEMDILPDGSLDYDDEVLAELDYVIAAIHSSFSQSEEEIMKRL 451

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 278 IKAIENPYTTMLGHLTGRLLLARPEYKLNMQKIIDACSQNDVCIELNASPHRLDLDWRLMQSAFEKGVKISINPDAHSLT 357
Cdd:PRK08609  452 ENACRNPYVRLIAHPTGRLIGRRDGYDVNIDQLIELAKETNTALELNANPNRLDLSAEHLKKAQEAGVKLAINTDAHHTE 531

                         250       260
                  ....*....|....*....|....*....
gi 1743416780 358 GLQDVKYGIKVARRGGAQRENVLNTKNFE 386
Cdd:PRK08609  532 MLDDMKYGVATARKGWIQKDRVINTWSRE 560
PHP pfam02811
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ...
 164-326 1.52e-09

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


Pssm-ID: 460705 [Multi-domain]  Cd Length: 171  Bit Score: 56.78  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 164 FHNHTTWS--DGSASLEEMAKEAQNLGYSYIGISDHSktAFYanGLTESRIAEQHAEIdklneemenfKIFKGIESDILN 241
Cdd:pfam02811   2 LHVHSEYSllDGAARIEELVKRAKELGMPAIAITDHG--NLF--GAVEFYKAAKKAGI----------KPIIGCEVYVAP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 242 DGSLDYDDSILENFDFVIASVH---------SNFKMSEEEMTKRLIKAIENPYT--------TMLGHLtGRLLLAR---P 301
Cdd:pfam02811  68 GSREETEKLLAKYFDLVLLAVHevgyknlikLSSRAYLEGFKPRIDKELLEEYFeglialsgCVLGHL-DLILLAPgdyE 146

                         170       180
                  ....*....|....*....|....*
gi 1743416780 302 EYKLNMQKIIDACSQNDVCIELNAS 326
Cdd:pfam02811 147 EAEELAEEYLEIFGEDGFYLEINTH 171
POLIIIAc smart00481
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ...
 164-241 1.25e-07

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: 1.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780  164 FHNHTTWS--DGSASLEEMAKEAQNLGYSYIGISDHSKtafyANGLTESRIAEQHAEIdklneemenfKIFKGIESDILN 241
Cdd:smart00481   2 LHVHSDYSllDGALSPEELVKRAKELGLKAIAITDHGN----LFGAVEFYKAAKKAGI----------KPIIGLEANIVD 67
hisJ_fam TIGR01856
histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate ...
 164-370 1.08e-06

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: 49.32  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 164 FHNHTTWS-DGSASLEEMAKEAQNLGYSYIGISDHSKTAFYANGLT-------ESRIAEQHAEIDKLNEEMEN-FKIFKG 234
Cdd:TIGR01856   3 SHSHSPFCaHGTDTLREVVQEAIQLGFEEICFTEHAPRPFYYPEEDflkkemlFLSLPEYFQEINQLKQEYADkIKILIG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 235 IESDILnDGSLDYDDSILE--NFDFVIASVH-----------SNFKMSEEEMTKRL--------------IKAIENPytT 287
Cdd:TIGR01856  83 LEVDYI-PGFEEEIKDFLDsyNLDFVIGSVHhlggipidfdiEEFDETLFSFQKNLeqaqrdyfesqydsIQNLFKP--L 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 288 MLGHLT-----GRLLLARPEYKLNM---QKIIDACSQNDVCIELNASPHRLDL------DWrLMQSAFEKGVKISINPDA 353
Cdd:TIGR01856 160 VIGHLDlvkkfGPLTDVSSKSDEVRellQRILKAVASYGKALEINTSGFRKPLeeaypsKE-LLNLAKELGIPLVLGSDA 238

                         250
                  ....*....|....*..
gi 1743416780 354 HsltGLQDVKYGIKVAR 370
Cdd:TIGR01856 239 H---GPGQVGLSYHKAK 252
CehA_McbA_metalo NF038032
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ...
 164-201 5.76e-04

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: 41.54  E-value: 5.76e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1743416780 164 FHNHTTWSDGSASLEEMAKEAQNLGYSYIGISDHSKTA 201
Cdd:NF038032    7 LHIHTNHSDGPTTPEELARAALAEGLDVIALTDHNTIS 44
 
Name Accession Description Interval E-value
PHP_PolX cd07436
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal ...
 156-390 5.23e-145

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: 410.66  E-value: 5.23e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 156 QEKEILGVFHNHTTWSDGSASLEEMAKEAQNLGYSYIGISDHSKTAFYANGLTESRIAEQHAEIDKLNEEMENFKIFKGI 235
Cdd:cd07436     1 ELKDIRGDLHVHTTWSDGRNSIEEMAEAARALGYEYIAITDHSKSLRVANGLSEERLREQIEEIDALNEKLPGIRILKGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 236 ESDILNDGSLDYDDSILENFDFVIASVHSNFKMSEEEMTKRLIKAIENPYTTMLGHLTGRLLLARPEYKLNMQKIIDACS 315
Cdd:cd07436    81 EVDILPDGSLDYPDEVLAELDVVVASVHSGFNQSEEEMTERLLKAIENPHVDILGHPTGRLLGRREGYEVDMERVIEAAA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743416780 316 QNDVCIELNASPHRLDLDWRLMQSAFEKGVKISINPDAHSLTGLQDVKYGIKVARRGGAQRENVLNTKNFETVLE 390
Cdd:cd07436   161 ETGTALEINANPDRLDLDDRHARRAKEAGVKIAINTDAHSTDGLDNMRYGVGTARRGWLEKEDVLNTLPLEELLK 235
HIS2 COG1387
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ...
 160-390 1.53e-113

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: 330.96  E-value: 1.53e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 160 ILGVFHNHTTWSDGSASLEEMAKEAQNLGYSYIGISDHSKTAFYANGLTESRIAEQHAEIDKLNEEMENFKIFKGIESDI 239
Cdd:COG1387     1 MRGDLHTHTTYSDGEGTIEEMVEAAIELGLEYIAITDHSPSLFVANGLSEERLLEYLEEIEELNEKYPDIKILKGIEVDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 240 LNDGSLDYDDSILENFDFVIASVHSNFKMSEEEMTKRLIKAIENPYTTMLGHLTGRLLLARPEYKLNMQKIIDACSQNDV 319
Cdd:COG1387    81 LPDGSLDYPDELLAPLDYVIGSVHSILEEDYEEYTERLLKAIENPLVDILGHPDGRLLGGRPGYEVDIEEVLEAAAENGV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743416780 320 CIELNASPHRLDLDWRLMQSAFEKGVKISINPDAHSLTGLQDVKYGIKVARRGGAQRENVLNTKNFETVLE 390
Cdd:COG1387   161 ALEINTRPLRLDPSDELLKLAKELGVKITIGSDAHSPEDLGDLEYGVALARRAGLTKEDVFNTLRKEELLK 231
PRK08609 PRK08609
DNA polymerase/3'-5' exonuclease PolX;
120-386 1.63e-93

DNA polymerase/3'-5' exonuclease PolX;


Pssm-ID: 236311 [Multi-domain]  Cd Length: 570  Bit Score: 291.09  E-value: 1.63e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 120 FRTEEEVFQVKKIKYIFPEVRHFG--VEKGSKVSEnLVQEKEILGVFHNHTTWSDGSASLEEMAKEAQNLGYSYIGISDH 197
Cdd:PRK08609  293 FESEEAFFAHFGLPFIPPEVREDGseFERYKDLSN-LITLSDIQGDLHMHTTWSDGAFSIEEMVEACIAKGYEYMAITDH 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 198 SKTAFYANGLTESRIAEQHAEIDKLNEEMENFKIFKGIESDILNDGSLDYDDSILENFDFVIASVHSNFKMSEEEMTKRL 277
Cdd:PRK08609  372 SQYLKVANGLTEERLLEQAEEIKALNEKYPEIDILSGIEMDILPDGSLDYDDEVLAELDYVIAAIHSSFSQSEEEIMKRL 451

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 278 IKAIENPYTTMLGHLTGRLLLARPEYKLNMQKIIDACSQNDVCIELNASPHRLDLDWRLMQSAFEKGVKISINPDAHSLT 357
Cdd:PRK08609  452 ENACRNPYVRLIAHPTGRLIGRRDGYDVNIDQLIELAKETNTALELNANPNRLDLSAEHLKKAQEAGVKLAINTDAHHTE 531

                         250       260
                  ....*....|....*....|....*....
gi 1743416780 358 GLQDVKYGIKVARRGGAQRENVLNTKNFE 386
Cdd:PRK08609  532 MLDDMKYGVATARKGWIQKDRVINTWSRE 560
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
120-382 2.89e-73

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 238.55  E-value: 2.89e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 120 FRTEEEVFQVKKIKYIFPEVRhfgvekgskvsEN--------------LVQEKEILGVFHNHTTWSDGSASLEEMAKEAQ 185
Cdd:COG1796   293 GETEEEVYAALGLPYIPPELR-----------EDrgeieaaeegrlpeLVELDDIRGDLHHHTTWSDGGASIEEMAAAAA 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 186 NLGYSYIGISDHSKTAFYANGLTESRIAEQHAEIDKLNEEMENFKIFKGIESDILNDGSLDYDDSILENFDFVIASVHSN 265
Cdd:COG1796   362 ARGYYYIAITDHSSSLVVAGGLDEERLLQQEEEIDALNERLDGIILLLGGEEDILDDGGLDDDDDLLLEDDDVVAAVHHS 441

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 266 FKMSEEEMTKRLIKAIENPYTTMLGHLTGRLLLARPEYKLNMQKIIDACSQNDVCIELNASPHRLDLDWRLMQSAFEKGV 345
Cdd:COG1796   442 FLLQDEEMTRRRLAAANEPVVVIIHHPTGRLLLRRRPYYVDDEAIIAAAAAAGALEEENNAPRRLLLLDDLARAAAEGGV 521

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1743416780 346 KISINPDAHSLTGLQDVKYGIKVARRGGAQRENVLNT 382
Cdd:COG1796   522 VIIIIDDAHHTDLLLDLMGGGVAARRRWWLEKDVNNN 558
PRK07945 PRK07945
PHP domain-containing protein;
162-390 2.88e-71

PHP domain-containing protein;


Pssm-ID: 236135 [Multi-domain]  Cd Length: 335  Bit Score: 226.40  E-value: 2.88e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 162 GVFHNHTTWSDGSASLEEMAKEAQNLGYSYIGISDHSKTAFYANGLTESRIAEQHAEIDKLNEEMENFKIFKGIESDILN 241
Cdd:PRK07945   98 GDLHTHSDWSDGGSPIEEMARTAAALGHEYCALTDHSPRLTVANGLSAERLRKQLDVVAELNEELAPFRILTGIEVDILD 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 242 DGSLDYDDSILENFDFVIASVHSNFKMSEEEMTKRLIKAIENPYTTMLGHLTGRLLL----ARPEYKLNMQKIIDACSQN 317
Cdd:PRK07945  178 DGSLDQEPELLDRLDVVVASVHSKLRMDAAAMTRRMLAAVANPHTDVLGHCTGRLVTgnrgTRPESKFDAEAVFAACREH 257

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1743416780 318 DVCIELNASPHRLDLDWRLMQSAFEKGVKISINPDAHSLTGLQDVKYGIKVARRGGAQRENVLNTKNFETVLE 390
Cdd:PRK07945  258 GTAVEINSRPERRDPPTRLLRLALDAGCLFSIDTDAHAPGQLDWLGYGCERAEEAGVPADRIVNTWPADRLLA 330
PHP_HisPPase_Ycdx_like cd07437
Polymerase and Histidinol Phosphatase domain of Ycdx like; PHP Ycdx-like is a stand alone PHP ...
 165-390 1.38e-34

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: 127.56  E-value: 1.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 165 HNHTTWSdGSA--SLEEMAKEAQNLGYSYIGISDH------SKTAFYANGLtesriaeqhaeiDKLNEEMENFKIFKGIE 236
Cdd:cd07437     6 HTHTIAS-GHAysTIEEMARAAAEKGLKLLGITDHgpampgAPHPWYFGNL------------KVIPREIYGVRILRGVE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 237 SDILN-DGSLDYDDSILENFDFVIASVHSN--FKMSEEEMTKRLIKAIENPYTTMLGHLTgrlllaRPEYKLNMQKIIDA 313
Cdd:cd07437    73 ANIIDyDGNLDLPERVLKRLDYVIASLHEPcfAPGTKEENTRAYINAMENPYVDIIGHPG------NPRYPIDYEAVVKA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 314 CSQNDVCIELNAS---PHRL---DLDWRLMQSAFEKGVKISINPDAHSLTGLQDVKYGIKVARRGGAQRENVLNTkNFET 387
Cdd:cd07437   147 AKEYNVLLEINNSslsPSRKgsrENCREIAELCKKYGVPVIVGSDAHIAYDIGNFDEALELLEEIGFPEELILNT-SPER 225


                  ...
gi 1743416780 388 VLE 390
Cdd:cd07437   226 LLD 228
PRK09248 PRK09248
putative hydrolase; Validated
 165-382 1.42e-23

putative hydrolase; Validated


Pssm-ID: 236429 [Multi-domain]  Cd Length: 246  Bit Score: 97.99  E-value: 1.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 165 HNHTTWSdGSA--SLEEMAKEAQNLGYSYIGISDHSKT------AFYANGLtesRIaeqhaeidkLNEEMENFKIFKGIE 236
Cdd:PRK09248    8 HTHTIAS-GHAysTLHENAAEAKQKGLKLFAITDHGPDmpgaphYWHFGNL---RV---------LPRKVDGVGILRGIE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 237 SDILN-DGSLDYDDSILENFDFVIASVHSN-FKMS-EEEMTKRLIKAIENPYTTMLGHLtgrlllARPEYKLNMQKIIDA 313
Cdd:PRK09248   75 ANIKNyDGEIDLPGDMLKKLDIVIAGFHEPvFAPGdKETNTQALINAIKNGRVDIIGHP------GNPKYPIDIEAVVKA 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743416780 314 CSQNDVCIELNAS--PHR----LDLDWRLMQSAFEKGVKISINPDAHSLTGLQDVKYGIKVARRGGAQRENVLNT 382
Cdd:PRK09248  149 AKEHNVALEINNSsfGHSrkgsEDNCRAIAALCKKAGVWVALGSDAHIAFDIGNFEEALKILDEVGFPEERILNV 223
PHP_HisPPase_Hisj_like cd12110
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; ...
 164-355 2.34e-21

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: 91.85  E-value: 2.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 164 FHNHTTWSD-GSASLEEMAKEAQNLGYSYIGISDHSKTAFYANGLTESRIAEQ-----HAEIDKLNEEMEN-FKIFKGIE 236
Cdd:cd12110     3 YHTHTPRCDhASGTLEEYVEAAIELGFTEIGFSEHAPLPFEFDDYPESRMAEEeledyVEEIRRLKEKYADqIEIKLGLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 237 SDILNDGSLDYDDSILE-NFDFVIASVH---------------SNFKMSEEEMTKR----LIKAIENPYTTMLGHLT--- 293
Cdd:cd12110    83 VDYFPGYEEELRELLYGyPLDYVIGSVHflggwgfdfpedgiaEYFEGDIDELYERyfdlVEKAIESGLFDIIGHPDlik 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743416780 294 --GRLLLARPEYKLNMQKIIDACSQNDVCIELNAS----------PHRldldwRLMQSAFEKGVKISINPDAHS 355
Cdd:cd12110   163 kfGKNDEPDEDYEELIERILRAIAEAGVALEINTAglrkpvgepyPSP-----EFLELAKELGIPVTLGSDAHS 231
PRK08392 PRK08392
hypothetical protein; Provisional
 165-380 1.30e-18

hypothetical protein; Provisional


Pssm-ID: 169423 [Multi-domain]  Cd Length: 215  Bit Score: 83.68  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 165 HNHTTWSDGSASLEEMAKEAQNLGYSYIGISDHSktafyaNGLTESRIAEQHAEIDKLNEEMEnFKIFKGIESDILNDGs 244
Cdd:PRK08392    4 HTHTVYSDGIGSVRDNIAEAERKGLRLVGISDHI------HYFTPSKFNAYINEIRQWGEESE-IVVLAGIEANITPNG- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 245 LDYDDSILENFDFVIASVHSNFKMSEEEMTKRLIK-AIENPYTTMLGHLTGRL-LLARPEYKlNMQKIIDACSQNDVCIE 322
Cdd:PRK08392   76 VDITDDFAKKLDYVIASVHEWFGRPEHHEYIELVKlALMDENVDIIGHFGNSFpYIGYPSEE-ELKEILDLAEAYGKAFE 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1743416780 323 LNASPHRLDLDWrlMQSAFEKGVKISINPDAHSLTGLQDVKYGIKVARRGGAQRENVL 380
Cdd:PRK08392  155 ISSRYRVPDLEF--IRECIKRGIKLTFASDAHRPEDVGNVSWSLKVFKKAGGKKEDLL 210
PHP pfam02811
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ...
 164-326 1.52e-09

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


Pssm-ID: 460705 [Multi-domain]  Cd Length: 171  Bit Score: 56.78  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 164 FHNHTTWS--DGSASLEEMAKEAQNLGYSYIGISDHSktAFYanGLTESRIAEQHAEIdklneemenfKIFKGIESDILN 241
Cdd:pfam02811   2 LHVHSEYSllDGAARIEELVKRAKELGMPAIAITDHG--NLF--GAVEFYKAAKKAGI----------KPIIGCEVYVAP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 242 DGSLDYDDSILENFDFVIASVH---------SNFKMSEEEMTKRLIKAIENPYT--------TMLGHLtGRLLLAR---P 301
Cdd:pfam02811  68 GSREETEKLLAKYFDLVLLAVHevgyknlikLSSRAYLEGFKPRIDKELLEEYFeglialsgCVLGHL-DLILLAPgdyE 146

                         170       180
                  ....*....|....*....|....*
gi 1743416780 302 EYKLNMQKIIDACSQNDVCIELNAS 326
Cdd:pfam02811 147 EAEELAEEYLEIFGEDGFYLEINTH 171
POLIIIAc smart00481
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ...
 164-241 1.25e-07

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: 1.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780  164 FHNHTTWS--DGSASLEEMAKEAQNLGYSYIGISDHSKtafyANGLTESRIAEQHAEIdklneemenfKIFKGIESDILN 241
Cdd:smart00481   2 LHVHSDYSllDGALSPEELVKRAKELGLKAIAITDHGN----LFGAVEFYKAAKKAGI----------KPIIGLEANIVD 67
YciV COG0613
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ...
 164-236 1.65e-07

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


Pssm-ID: 440378 [Multi-domain]  Cd Length: 188  Bit Score: 51.06  E-value: 1.65e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1743416780 164 FHNHTTWSDGSASLEEMAKEAQNLGYSYIGISDHSKTAfyanGLTESRIAEQHaeidklneemENFKIFKGIE 236
Cdd:COG0613     6 LHVHTTASDGSLSPEELVARAKAAGLDVLAITDHDTVA----GYEEAAEAAKE----------LGLLVIPGVE 64
PHP cd07309
Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2 ...
 164-239 7.47e-07

Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. PHP in polymerases has trinuclear zinc/magnesium dependent proofreading activity. It has also been shown that the PHP domain functions in DNA repair. The PHP structures have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.


Pssm-ID: 213985 [Multi-domain]  Cd Length: 88  Bit Score: 46.65  E-value: 7.47e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1743416780 164 FHNHTTWSDG-SASLEEMAKEAQNLGYSYIGISDHSKTAFYANGLTesriAEQHAEIDKLneEMENFKIFKGIESDI 239
Cdd:cd07309     3 LHTHTVFSDGdHAKLTELVDKAKELGPDALAITDHGNLRGLAEFNT----AGK*NHIKAA--EAAGIKIIIGSEVNL 73
PRK07328 PRK07328
histidinol-phosphatase; Provisional
 164-354 8.16e-07

histidinol-phosphatase; Provisional


Pssm-ID: 235992 [Multi-domain]  Cd Length: 269  Bit Score: 50.02  E-value: 8.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 164 FHNHTTWSdGSA--SLEEMAKEAQNLGYSYIGISDHSKTAFYANG-------LTESRIAEQHAEIDKLNEEMENFKIFKG 234
Cdd:PRK07328    6 YHMHTPLC-GHAvgTPEEYVQAARRAGLKEIGFTDHLPMYFLPPEwrdpglaMRLEELPFYVSEVERLRARFPDLYVRLG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 235 IESDILnDGSLDYDDSILE--NFDFVIASVH-------SNFKMSEE-------EMTKRLIKAIENPYTTMLGHLTGRLLL 298
Cdd:PRK07328   85 IEADYH-PGTEEFLERLLEayPFDYVIGSVHylgawgfDNPDFVAEyeerdldELYRRYFALVEQAARSGLFDIIGHPDL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743416780 299 A-----RPE--YKLNMQKIIDACSQNDVCIELNASphrldlDWR-----------LMQSAFEKGVKISINPDAH 354
Cdd:PRK07328  164 IkkfghRPRedLTELYEEALDVIAAAGLALEVNTA------GLRkpvgeiypspaLLRACRERGIPVVLGSDAH 231
hisJ_fam TIGR01856
histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate ...
 164-370 1.08e-06

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: 49.32  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 164 FHNHTTWS-DGSASLEEMAKEAQNLGYSYIGISDHSKTAFYANGLT-------ESRIAEQHAEIDKLNEEMEN-FKIFKG 234
Cdd:TIGR01856   3 SHSHSPFCaHGTDTLREVVQEAIQLGFEEICFTEHAPRPFYYPEEDflkkemlFLSLPEYFQEINQLKQEYADkIKILIG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 235 IESDILnDGSLDYDDSILE--NFDFVIASVH-----------SNFKMSEEEMTKRL--------------IKAIENPytT 287
Cdd:TIGR01856  83 LEVDYI-PGFEEEIKDFLDsyNLDFVIGSVHhlggipidfdiEEFDETLFSFQKNLeqaqrdyfesqydsIQNLFKP--L 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 288 MLGHLT-----GRLLLARPEYKLNM---QKIIDACSQNDVCIELNASPHRLDL------DWrLMQSAFEKGVKISINPDA 353
Cdd:TIGR01856 160 VIGHLDlvkkfGPLTDVSSKSDEVRellQRILKAVASYGKALEINTSGFRKPLeeaypsKE-LLNLAKELGIPLVLGSDA 238

                         250
                  ....*....|....*..
gi 1743416780 354 HsltGLQDVKYGIKVAR 370
Cdd:TIGR01856 239 H---GPGQVGLSYHKAK 252
PHP_HisPPase cd07432
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ...
 164-355 2.04e-05

Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to produce histidinol. HisPPase can be classified into two types: the bifunctional HisPPase found in proteobacteria that belongs to the DDDD superfamily and the monofunctional Bacillus subtilis type that is a member of the PHP family. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.


Pssm-ID: 213987 [Multi-domain]  Cd Length: 129  Bit Score: 43.77  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 164 FHNHTTWSDGSA-SLEEMAKEAQNLGYSYIGISDHsktafyaNGLTESRIAEQHAEIDKLneemenfKIFKGIEsdilnd 242
Cdd:cd07432     3 LHIHSVFSPDSDmTPEEIVERAIELGLDGIAITDH-------NTIDGAEEALKEAYKDGL-------LVIPGVE------ 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 243 gsldyddsilenFDFVIasvhsnfkmseeemtkrlikaienpyttmLGHLTgrlllaRPEYKLNMQKIIDACSQNDVCIE 322
Cdd:cd07432    63 ------------VTLVV-----------------------------LAHPD------RPSRYGLSDLILKPLIKNGDAIE 95

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1743416780 323 LNASPHRLDLDWR-LMQSAFEKGVKISINPDAHS 355
Cdd:cd07432    96 VNNSRLRYGLNNLaAKRYAELGGLPITGGSDAHT 129
PHP_HisPPase_AMP cd07438
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) ...
 164-236 2.27e-05

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: 44.31  E-value: 2.27e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1743416780 164 FHNHTTWSDGSASLEEMAKEAQNLGYSYIGISDHSKTAfyanGLTEsriAEQHAeidklneEMENFKIFKGIE 236
Cdd:cd07438     3 LHTHSTASDGTLSPEELVELAKEAGLKVLAITDHDTVA----GLEE---ALAAA-------KELGIELIPGVE 61
CehA_McbA_metalo NF038032
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ...
 164-201 5.76e-04

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: 41.54  E-value: 5.76e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1743416780 164 FHNHTTWSDGSASLEEMAKEAQNLGYSYIGISDHSKTA 201
Cdd:NF038032    7 LHIHTNHSDGPTTPEELARAALAEGLDVIALTDHNTIS 44
DnaE COG0587
DNA polymerase III, alpha subunit [Replication, recombination and repair];
165-197 1.05e-03

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


Pssm-ID: 440352 [Multi-domain]  Cd Length: 1050  Bit Score: 41.21  E-value: 1.05e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1743416780  165 HNHTTWS--DGSASLEEMAKEAQNLGYSYIGISDH 197
Cdd:COG0587      9 HVHSEYSllDGASRPEELVARAAELGMPALAITDH 43
PHP_PolIIIA_DnaE3 cd12113
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III ...
 165-197 2.40e-03

Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III DnaE3; PolIIIAs that contain an N-terminal PHP domain have been classified into four basic groups based on genome composition, phylogenetic, and domain structural analysis: polC, dnaE1, dnaE2, and dnaE3. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. DNA polymerase III holoenzyme is one of the five eubacterial DNA polymerases that is responsible for the replication of the DNA duplex. The alpha subunit of DNA polymerase III core enzyme catalyzes the reaction for polymerizing both DNA strands. The PolIIIA PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination, and like other PHP structures, the PolIIIA PHP exhibits a distorted (beta/alpha) 7 barrel and coordinates up to 3 metals. Initially, it was proposed that PHP region might be involved in pyrophosphate hydrolysis, but such an activity has not been found. It has been shown that the PHP of PolIIIA has a trinuclear metal complex and is capable of proofreading activity. Bacterial genome replication and DNA repair mechanisms is related to the GC content of its genomes. There is a correlation between GC content variations and the dimeric combinations of PolIIIA subunits. Eubacteria can be grouped into different GC variable groups: the full-spectrum or dnaE1 group, the high-GC or dnaE2-dnaE1 group, and the low GC or polC-dnaE3 group.


Pssm-ID: 213997 [Multi-domain]  Cd Length: 283  Bit Score: 39.35  E-value: 2.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1743416780 165 HNHTTWS--DGSASLEEMAKEAQNLGYSYIGISDH 197
Cdd:cd12113     6 HVHTEYSllDGAIRIKDLVKRAKELGMPALAITDH 40
PRK00912 PRK00912
ribonuclease P protein component 3; Provisional
 172-241 4.88e-03

ribonuclease P protein component 3; Provisional


Pssm-ID: 234862 [Multi-domain]  Cd Length: 237  Bit Score: 38.07  E-value: 4.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743416780 172 DGSASLEEMAKEAQNLGYSYIGISDHSktafyangltesriaEQHAEIDKLNEEMENFKIFKGIESDILN 241
Cdd:PRK00912   13 DGYDTVLRLISEASHLGYSGIALSNHS---------------DKYPESKPELEDLLGFEIFRGVEIVASN 67
RPP1 COG1603
RNase P/RNase MRP subunit p30 [Translation, ribosomal structure and biogenesis];
171-236 5.28e-03

RNase P/RNase MRP subunit p30 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441211 [Multi-domain]  Cd Length: 231  Bit Score: 37.95  E-value: 5.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1743416780 171 SDGSASLEEMAKEAQNLGYSYIGISDHSktafyangltESRIAEQHAEIdklnEEMENFKIFKGIE 236
Cdd:COG1603    12 PDGDSTVARLALTAKRLGYDGIVVRNHS----------DARADYDAEAI----REEYGIDVVRGVE 63
PHP_HisPPase_Thermotoga_like cd12111
Polymerase and Histidinol Phosphatase domain of Thermotoga like; The PHP (also called ...
 164-197 5.93e-03

Polymerase and Histidinol Phosphatase domain of Thermotoga like; The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. Thermotoga PHP is an uncharacterized protein. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to give histidinol. The HisPPase can be classified into two types: the bifunctional HisPPase found in proteobacteria that belongs to the DDDD superfamily and the monofunctional Bacillus subtilis type that is a member of the PHP family. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.


Pssm-ID: 213995 [Multi-domain]  Cd Length: 226  Bit Score: 37.79  E-value: 5.93e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1743416780 164 FHNHTTWSDGSASLEEMAKEAQNLGYSYIGISDH 197
Cdd:cd12111     6 FHIHTTYSDGALSLSEVVDLYGQHGFDVIAITDH 39
 
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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