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Conserved domains on  [gi|1224461214|ref|WP_092483361|]
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histidinol-phosphatase [Desulfoscipio geothermicus]

Protein Classification

histidinol-phosphatase( domain architecture ID 10186795)

histidinol-phosphatase is a polymerase and histidinol-phosphatase (PHP) family protein that catalyzes the hydrolysis of histidinol-phosphate to form L-histidinol and phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PHP_HisPPase_Hisj_like cd12110
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; ...
8-266 3.42e-61

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: 194.32  E-value: 3.42e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214   8 VDYHVHPGYSiDAAPVGIDEYCVRAMQIGLAEICFTPHLEVDEarkhlDWFVRCNGRvMPMEDLqwlDFYFQEINMAREK 87
Cdd:cd12110     1 VDYHTHTPRC-DHASGTLEEYVEAAIELGFTEIGFSEHAPLPF-----EFDDYPESR-MAEEEL---EDYVEEIRRLKEK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214  88 FSPRLVIKAGIEVGYEPGREMYIEKILTGFPFDFVLGSIHCLNHVAISSKKECAVHFAGKTCAEVAQDYFTSLEAAVKSR 167
Cdd:cd12110    71 YADQIEIKLGLEVDYFPGYEEELRELLYGYPLDYVIGSVHFLGGWGFDFPEDGIAEYFEGDIDELYERYFDLVEKAIESG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214 168 LFDCMAHIDLYRRYGTVYLDRNNIEEmhrgYIEKIFKYMARHHIGLEINTSGLRRELGDLHPSKAIVQTALQQGVQIfTT 247
Cdd:cd12110   151 LFDIIGHPDLIKKFGKNDEPDEDYEE----LIERILRAIAEAGVALEINTAGLRKPVGEPYPSPEFLELAKELGIPV-TL 225
                         250
                  ....*....|....*....
gi 1224461214 248 GSDAHSLSEIGQGLQAAER 266
Cdd:cd12110   226 GSDAHSPEDVGQGYDEALA 244
 
Name Accession Description Interval E-value
PHP_HisPPase_Hisj_like cd12110
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; ...
8-266 3.42e-61

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: 194.32  E-value: 3.42e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214   8 VDYHVHPGYSiDAAPVGIDEYCVRAMQIGLAEICFTPHLEVDEarkhlDWFVRCNGRvMPMEDLqwlDFYFQEINMAREK 87
Cdd:cd12110     1 VDYHTHTPRC-DHASGTLEEYVEAAIELGFTEIGFSEHAPLPF-----EFDDYPESR-MAEEEL---EDYVEEIRRLKEK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214  88 FSPRLVIKAGIEVGYEPGREMYIEKILTGFPFDFVLGSIHCLNHVAISSKKECAVHFAGKTCAEVAQDYFTSLEAAVKSR 167
Cdd:cd12110    71 YADQIEIKLGLEVDYFPGYEEELRELLYGYPLDYVIGSVHFLGGWGFDFPEDGIAEYFEGDIDELYERYFDLVEKAIESG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214 168 LFDCMAHIDLYRRYGTVYLDRNNIEEmhrgYIEKIFKYMARHHIGLEINTSGLRRELGDLHPSKAIVQTALQQGVQIfTT 247
Cdd:cd12110   151 LFDIIGHPDLIKKFGKNDEPDEDYEE----LIERILRAIAEAGVALEINTAGLRKPVGEPYPSPEFLELAKELGIPV-TL 225
                         250
                  ....*....|....*....
gi 1224461214 248 GSDAHSLSEIGQGLQAAER 266
Cdd:cd12110   226 GSDAHSPEDVGQGYDEALA 244
PRK07328 PRK07328
histidinol-phosphatase; Provisional
7-285 4.48e-48

histidinol-phosphatase; Provisional


Pssm-ID: 235992 [Multi-domain]  Cd Length: 269  Bit Score: 161.34  E-value: 4.48e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214   7 LVDYHVHPGYSIDAapVG-IDEYCVRAMQIGLAEICFTPHL---EVDEARKHLDWfvrcngrVMPMEDLQwldFYFQEIN 82
Cdd:PRK07328    3 LVDYHMHTPLCGHA--VGtPEEYVQAARRAGLKEIGFTDHLpmyFLPPEWRDPGL-------AMRLEELP---FYVSEVE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214  83 MAREKFsPRLVIKAGIEVGYEPGREMYIEKILTGFPFDFVLGSIHCLNHVAISSKKECAvHFAGKTCAEVAQDYFTSLEA 162
Cdd:PRK07328   71 RLRARF-PDLYVRLGIEADYHPGTEEFLERLLEAYPFDYVIGSVHYLGAWGFDNPDFVA-EYEERDLDELYRRYFALVEQ 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214 163 AVKSRLFDCMAHIDLYRRYGtvYLDRNNIEEMHrgyiEKIFKYMARHHIGLEINTSGLRRELGDLHPSKAIVQTALQQGV 242
Cdd:PRK07328  149 AARSGLFDIIGHPDLIKKFG--HRPREDLTELY----EEALDVIAAAGLALEVNTAGLRKPVGEIYPSPALLRACRERGI 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1224461214 243 QiFTTGSDAHSLSEIGQGLQAAERLLKQFDL-QAATFTGRKPDP 285
Cdd:PRK07328  223 P-VVLGSDAHRPEEVGFGFAEALALLKEVGYtETVVFRARKRRA 265
HIS2 COG1387
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ...
7-287 2.16e-45

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: 153.39  E-value: 2.16e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214   7 LVDYHVHPGYSIDAAPvgIDEYCVRAMQIGLAEICFTphlevDearkHLDWFVRCNGrvMPMEDLqwlDFYFQEINMARE 86
Cdd:COG1387     2 RGDLHTHTTYSDGEGT--IEEMVEAAIELGLEYIAIT-----D----HSPSLFVANG--LSEERL---LEYLEEIEELNE 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214  87 KFsPRLVIKAGIEVGY-EPGREMYIEKILTgfPFDFVLGSIHCLnhvaisskkecavhfagktCAEVAQDYFTSLEAAVK 165
Cdd:COG1387    66 KY-PDIKILKGIEVDIlPDGSLDYPDELLA--PLDYVIGSVHSI-------------------LEEDYEEYTERLLKAIE 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214 166 SRLFDCMAHIDLYRRYGtvyldRNNIEEmhrgYIEKIFKYMARHHIGLEINTSGLRrelgdLHPSKAIVQTALQQGVqIF 245
Cdd:COG1387   124 NPLVDILGHPDGRLLGG-----RPGYEV----DIEEVLEAAAENGVALEINTRPLR-----LDPSDELLKLAKELGV-KI 188
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1224461214 246 TTGSDAHSLSEIGqGLQAAERLLKQFDLQAATF--TGRKPDPQK 287
Cdd:COG1387   189 TIGSDAHSPEDLG-DLEYGVALARRAGLTKEDVfnTLRKEELLK 231
hisJ_fam TIGR01856
histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate ...
9-264 1.31e-39

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: 139.07  E-value: 1.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214   9 DYHVHPGYSIDAAPVgIDEYCVRAMQIGLAEICFTPHLEVDEARKHLDWFvrcnGRVMPMEDLqwlDFYFQEINMAREKF 88
Cdd:TIGR01856   2 DSHSHSPFCAHGTDT-LREVVQEAIQLGFEEICFTEHAPRPFYYPEEDFL----KKEMLFLSL---PEYFQEINQLKQEY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214  89 SPRLVIKAGIEVGYEPGREMYIEKILTGFPFDFVLGSIHCLNHVAISSKKEC---AVHFAGKTCAEVAQDYFTSLEAAVK 165
Cdd:TIGR01856  74 ADKIKILIGLEVDYIPGFEEEIKDFLDSYNLDFVIGSVHHLGGIPIDFDIEEfdeTLFSFQKNLEQAQRDYFESQYDSIQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214 166 S-RLFDCMAHIDLYRRYGTVYLDRNNIEEMhRGYIEKIFKYMARHHIGLEINTSGLRRELGDLHPSKAIVQTALQQGVQi 244
Cdd:TIGR01856 154 NlFKPLVIGHLDLVKKFGPLTDVSSKSDEV-RELLQRILKAVASYGKALEINTSGFRKPLEEAYPSKELLNLAKELGIP- 231
                         250       260
                  ....*....|....*....|
gi 1224461214 245 FTTGSDAHSLSEIGQGLQAA 264
Cdd:TIGR01856 232 LVLGSDAHGPGQVGLSYHKA 251
PHP pfam02811
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ...
9-218 1.54e-19

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


Pssm-ID: 460705 [Multi-domain]  Cd Length: 171  Bit Score: 83.75  E-value: 1.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214   9 DYHVHPGYSIDAAPVGIDEYCVRAMQIGLAEICFTPHlevdearkhldwfvrcngrvMPMEDLqwLDFYfQEINMAREKf 88
Cdd:pfam02811   1 HLHVHSEYSLLDGAARIEELVKRAKELGMPAIAITDH--------------------GNLFGA--VEFY-KAAKKAGIK- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214  89 sprlvIKAGIEVGYEPGREMYIEKILTgFPFDFVLGSIHCL---NHVAISSKKecavHFAGKTCA---EVAQDYFTSLEA 162
Cdd:pfam02811  57 -----PIIGCEVYVAPGSREETEKLLA-KYFDLVLLAVHEVgykNLIKLSSRA----YLEGFKPRidkELLEEYFEGLIA 126
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1224461214 163 AVksrlFDCMAHIDLyrrygtvYLDRNNIEEMHRGYIEKIFKYMARHHIGLEINTS 218
Cdd:pfam02811 127 LS----GCVLGHLDL-------ILLAPGDYEEAEELAEEYLEIFGEDGFYLEINTH 171
 
Name Accession Description Interval E-value
PHP_HisPPase_Hisj_like cd12110
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; ...
8-266 3.42e-61

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: 194.32  E-value: 3.42e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214   8 VDYHVHPGYSiDAAPVGIDEYCVRAMQIGLAEICFTPHLEVDEarkhlDWFVRCNGRvMPMEDLqwlDFYFQEINMAREK 87
Cdd:cd12110     1 VDYHTHTPRC-DHASGTLEEYVEAAIELGFTEIGFSEHAPLPF-----EFDDYPESR-MAEEEL---EDYVEEIRRLKEK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214  88 FSPRLVIKAGIEVGYEPGREMYIEKILTGFPFDFVLGSIHCLNHVAISSKKECAVHFAGKTCAEVAQDYFTSLEAAVKSR 167
Cdd:cd12110    71 YADQIEIKLGLEVDYFPGYEEELRELLYGYPLDYVIGSVHFLGGWGFDFPEDGIAEYFEGDIDELYERYFDLVEKAIESG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214 168 LFDCMAHIDLYRRYGTVYLDRNNIEEmhrgYIEKIFKYMARHHIGLEINTSGLRRELGDLHPSKAIVQTALQQGVQIfTT 247
Cdd:cd12110   151 LFDIIGHPDLIKKFGKNDEPDEDYEE----LIERILRAIAEAGVALEINTAGLRKPVGEPYPSPEFLELAKELGIPV-TL 225
                         250
                  ....*....|....*....
gi 1224461214 248 GSDAHSLSEIGQGLQAAER 266
Cdd:cd12110   226 GSDAHSPEDVGQGYDEALA 244
PRK07328 PRK07328
histidinol-phosphatase; Provisional
7-285 4.48e-48

histidinol-phosphatase; Provisional


Pssm-ID: 235992 [Multi-domain]  Cd Length: 269  Bit Score: 161.34  E-value: 4.48e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214   7 LVDYHVHPGYSIDAapVG-IDEYCVRAMQIGLAEICFTPHL---EVDEARKHLDWfvrcngrVMPMEDLQwldFYFQEIN 82
Cdd:PRK07328    3 LVDYHMHTPLCGHA--VGtPEEYVQAARRAGLKEIGFTDHLpmyFLPPEWRDPGL-------AMRLEELP---FYVSEVE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214  83 MAREKFsPRLVIKAGIEVGYEPGREMYIEKILTGFPFDFVLGSIHCLNHVAISSKKECAvHFAGKTCAEVAQDYFTSLEA 162
Cdd:PRK07328   71 RLRARF-PDLYVRLGIEADYHPGTEEFLERLLEAYPFDYVIGSVHYLGAWGFDNPDFVA-EYEERDLDELYRRYFALVEQ 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214 163 AVKSRLFDCMAHIDLYRRYGtvYLDRNNIEEMHrgyiEKIFKYMARHHIGLEINTSGLRRELGDLHPSKAIVQTALQQGV 242
Cdd:PRK07328  149 AARSGLFDIIGHPDLIKKFG--HRPREDLTELY----EEALDVIAAAGLALEVNTAGLRKPVGEIYPSPALLRACRERGI 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1224461214 243 QiFTTGSDAHSLSEIGQGLQAAERLLKQFDL-QAATFTGRKPDP 285
Cdd:PRK07328  223 P-VVLGSDAHRPEEVGFGFAEALALLKEVGYtETVVFRARKRRA 265
HIS2 COG1387
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ...
7-287 2.16e-45

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: 153.39  E-value: 2.16e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214   7 LVDYHVHPGYSIDAAPvgIDEYCVRAMQIGLAEICFTphlevDearkHLDWFVRCNGrvMPMEDLqwlDFYFQEINMARE 86
Cdd:COG1387     2 RGDLHTHTTYSDGEGT--IEEMVEAAIELGLEYIAIT-----D----HSPSLFVANG--LSEERL---LEYLEEIEELNE 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214  87 KFsPRLVIKAGIEVGY-EPGREMYIEKILTgfPFDFVLGSIHCLnhvaisskkecavhfagktCAEVAQDYFTSLEAAVK 165
Cdd:COG1387    66 KY-PDIKILKGIEVDIlPDGSLDYPDELLA--PLDYVIGSVHSI-------------------LEEDYEEYTERLLKAIE 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214 166 SRLFDCMAHIDLYRRYGtvyldRNNIEEmhrgYIEKIFKYMARHHIGLEINTSGLRrelgdLHPSKAIVQTALQQGVqIF 245
Cdd:COG1387   124 NPLVDILGHPDGRLLGG-----RPGYEV----DIEEVLEAAAENGVALEINTRPLR-----LDPSDELLKLAKELGV-KI 188
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1224461214 246 TTGSDAHSLSEIGqGLQAAERLLKQFDLQAATF--TGRKPDPQK 287
Cdd:COG1387   189 TIGSDAHSPEDLG-DLEYGVALARRAGLTKEDVfnTLRKEELLK 231
hisJ_fam TIGR01856
histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate ...
9-264 1.31e-39

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: 139.07  E-value: 1.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214   9 DYHVHPGYSIDAAPVgIDEYCVRAMQIGLAEICFTPHLEVDEARKHLDWFvrcnGRVMPMEDLqwlDFYFQEINMAREKF 88
Cdd:TIGR01856   2 DSHSHSPFCAHGTDT-LREVVQEAIQLGFEEICFTEHAPRPFYYPEEDFL----KKEMLFLSL---PEYFQEINQLKQEY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214  89 SPRLVIKAGIEVGYEPGREMYIEKILTGFPFDFVLGSIHCLNHVAISSKKEC---AVHFAGKTCAEVAQDYFTSLEAAVK 165
Cdd:TIGR01856  74 ADKIKILIGLEVDYIPGFEEEIKDFLDSYNLDFVIGSVHHLGGIPIDFDIEEfdeTLFSFQKNLEQAQRDYFESQYDSIQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214 166 S-RLFDCMAHIDLYRRYGTVYLDRNNIEEMhRGYIEKIFKYMARHHIGLEINTSGLRRELGDLHPSKAIVQTALQQGVQi 244
Cdd:TIGR01856 154 NlFKPLVIGHLDLVKKFGPLTDVSSKSDEV-RELLQRILKAVASYGKALEINTSGFRKPLEEAYPSKELLNLAKELGIP- 231
                         250       260
                  ....*....|....*....|
gi 1224461214 245 FTTGSDAHSLSEIGQGLQAA 264
Cdd:TIGR01856 232 LVLGSDAHGPGQVGLSYHKA 251
PRK06740 PRK06740
histidinol phosphate phosphatase domain-containing protein;
25-282 7.36e-29

histidinol phosphate phosphatase domain-containing protein;


Pssm-ID: 180677 [Multi-domain]  Cd Length: 331  Bit Score: 112.54  E-value: 7.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214  25 IDEYCVRAMQIGLAEICFTPHL-EVDEARKHLDWFVRCNGRVMPMEDLQWLDFYFQE--------INMAREKFSPRLV-I 94
Cdd:PRK06740   63 IDLYLEEALRKGIKEVGIVDHLyRFYEAREYYEKYVDISDSRLGRLQKEWLDQVRVAslddftkaIEEAKERWSKRGVtL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214  95 KAGIEVGYEPGREMYIEKILTGFPFDFVLGSIHCLNHVAISSkKECAVHFAGKTCAEVAQDYFTSLEAAVKSRLFDCMAH 174
Cdd:PRK06740  143 KLGIEADYFIGGEQELQSLLALGDFDYVIGSVHFLNGWGFDN-PDTKEYFEEHDLYALYDTFFKTVECAIRSELFDIIAH 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214 175 IDLYRRYGTvyldRNNiEEMHRGYIEKIFKYMARHHIGLEINTS-GLRRELGDLHPSKAIVQTALQQGVqIFTTGSDAHS 253
Cdd:PRK06740  222 LDNIKVFNY----RLD-ENEQLSYYKEIARALVETNTATEINAGlYYRYPVREMCPSPLFLQVLAKHEV-PITLSSDAHY 295
                         250       260       270
                  ....*....|....*....|....*....|
gi 1224461214 254 LSEIGQGLQAAERLLKQFDLQA-ATFTGRK 282
Cdd:PRK06740  296 PNDLGKYVEENVKTLRNHGVTSlATFTKRV 325
PRK08123 PRK08123
histidinol-phosphatase HisJ;
8-260 5.23e-21

histidinol-phosphatase HisJ;


Pssm-ID: 236155 [Multi-domain]  Cd Length: 270  Bit Score: 89.97  E-value: 5.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214   8 VDYHVHPGYSidaaPVG----IDEYCVRAMQIGLAEICFTPH------LEVDEARkhldwfvrcNGRVMPMEDlqwLDFY 77
Cdd:PRK08123    4 RDGHTHTPFC----PHGskddLEAYIERAIELGFTEITFTEHaplppgFIDPTPR---------QDSAMAIEQ---LERY 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214  78 FQEINMAREKFSPRLVIKAGIEVGYEPGREMYIEKILTGF-PF--DFVLgSIHCLNH----VAISSKKEC---AVHFAGK 147
Cdd:PRK08123   68 LKELNELKKKYAGQIDIRIGLEVDYIEGYEEETRAFLNEYgPLldDSIL-SVHFLKGdgeyYCIDYSPETfaeFVDLLGS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214 148 TcAEVAQDYFTSLEAAVKSRLFDC----MAHIDLYRRYGTVY---LDRNNIEEmhrgyIEKIFKYMARHHIGLEINTSGL 220
Cdd:PRK08123  147 I-EAVYEAYYETVLQSIEADLGPYkpkrIGHITLVRKFQKLFppdFDEKNKEL-----IEDILALIKKRGYELDFNTAGL 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1224461214 221 RREL-GDLHPSKAIVQTALQQGVQiFTTGSDAHSLSEIGQG 260
Cdd:PRK08123  221 RKPYcGEPYPPGEIITLAKKLGIP-LVYGSDAHSAADVGRG 260
PRK05588 PRK05588
histidinol phosphate phosphatase;
9-287 5.48e-21

histidinol phosphate phosphatase;


Pssm-ID: 235519 [Multi-domain]  Cd Length: 255  Bit Score: 89.71  E-value: 5.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214   9 DYHVHPGYSIDAApVGIDEYCVRAMQIGLAEIcFTPHLEVDearkhldwfvrcngrvMPMEDLQWLDF--YFQEINMARe 86
Cdd:PRK05588    3 DTHIHTEFSTDSK-MKIEEAIKKAKENNLGII-ITEHMDLN----------------LPDKNKFCFDVdsYFNKYSKYR- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214  87 kfSPRLVIkaGIEVGYEPGREMYIEKILTGFPFDFVLGSIHCLNHVAISSKKecavHFAGKTCAEVAQDYF-TSLEAAVK 165
Cdd:PRK05588   64 --NNKLLL--GIELGMEKDLIEENKELINKYEFDYVIGSIHLVDKLDLYLDE----FYKDKSKEEAYHIYFeNMLKCLEK 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214 166 SRLFDCMAHIDLYRRYGTvYLDRNNIEEMHRGYIEKIFKYMARHHIGLEINTsglrRELGDLHPSKAIVQTA---LQQGV 242
Cdd:PRK05588  136 YDFIDSLGHIDYISRYAK-YEDKEIYYDEFKEIIDEILKVLIEKEKVLEINT----RRLDDKRSVENLVKIYkrfYELGG 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1224461214 243 QIFTTGSDAHSLSEIGQGLQAAERLLKQFDLQAATFTGRKPDPQK 287
Cdd:PRK05588  211 KYITLGSDAHNIEDIGNNFKFALEIAEYCNLKPVYFKNRKPEYDK 255
PHP pfam02811
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ...
9-218 1.54e-19

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


Pssm-ID: 460705 [Multi-domain]  Cd Length: 171  Bit Score: 83.75  E-value: 1.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214   9 DYHVHPGYSIDAAPVGIDEYCVRAMQIGLAEICFTPHlevdearkhldwfvrcngrvMPMEDLqwLDFYfQEINMAREKf 88
Cdd:pfam02811   1 HLHVHSEYSLLDGAARIEELVKRAKELGMPAIAITDH--------------------GNLFGA--VEFY-KAAKKAGIK- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214  89 sprlvIKAGIEVGYEPGREMYIEKILTgFPFDFVLGSIHCL---NHVAISSKKecavHFAGKTCA---EVAQDYFTSLEA 162
Cdd:pfam02811  57 -----PIIGCEVYVAPGSREETEKLLA-KYFDLVLLAVHEVgykNLIKLSSRA----YLEGFKPRidkELLEEYFEGLIA 126
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1224461214 163 AVksrlFDCMAHIDLyrrygtvYLDRNNIEEMHRGYIEKIFKYMARHHIGLEINTS 218
Cdd:pfam02811 127 LS----GCVLGHLDL-------ILLAPGDYEEAEELAEEYLEIFGEDGFYLEINTH 171
PRK07329 PRK07329
hypothetical protein; Provisional
9-272 3.83e-16

hypothetical protein; Provisional


Pssm-ID: 180933 [Multi-domain]  Cd Length: 246  Bit Score: 76.23  E-value: 3.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214   9 DYHVHPGYSIDAapvgiDEYCVRAMQIGLAEICFTPHLEVDearkhldwfvrcNGRVMPMEDLQWLDFYFQEINMAREKF 88
Cdd:PRK07329    3 DQHLHTHFSFDS-----DAKFEDYLTHFDGEIVTTEHLDLS------------NPYDTGQDDVPDYAKYSAEIAELNEKY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214  89 SPRlvIKAGIEVGYEPGREMYIEKILTGFPFDFVLGSIHclnHVAISSKKECAVhfAGKTCAEVAQDYFTSLEAAVKSRL 168
Cdd:PRK07329   66 GNR--IKKGIEIGYFAPREDDILDFLANKDFDLKLLSVH---HNGVYDYLDDEV--ADMDKKELLQEYFEKMEEAIGRVH 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214 169 -FDCMAHIDlyrrYGtvyLDRNNI--EEM--HRGYIEKIFKYMARHHIGLEINTSGLRReLGDLHPSKAIVQTALQQGVQ 243
Cdd:PRK07329  139 dADVLAHFD----YG---LRLFDLtvEELkaFEPQLTRIFAKMIDNDLAFELNTKSMYL-YGNEGLYRYAIELYKQLGGK 210
                         250       260
                  ....*....|....*....|....*....
gi 1224461214 244 IFTTGSDAHSLSEIGQGLQAAERLLKQFD 272
Cdd:PRK07329  211 LFSIGSDAHKLEHYRYNFDDAQKLLKEHG 239
PHP_HisPPase cd07432
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ...
8-253 1.99e-09

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: 54.55  E-value: 1.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214   8 VDYHVHPGYSIDAApVGIDEYCVRAMQIGLAEICFTPHLEVDEARKHLdwfvrcngrvmpmedlqwldfyfqeinmaREK 87
Cdd:cd07432     1 ADLHIHSVFSPDSD-MTPEEIVERAIELGLDGIAITDHNTIDGAEEAL-----------------------------KEA 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214  88 FSPRLVIKAGIEVGyepgremyiekiltgfpfdfvlgsihclnhvaisskkecavhfagktcaevaqdyftsleaavksr 167
Cdd:cd07432    51 YKDGLLVIPGVEVT------------------------------------------------------------------ 64
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214 168 lFDCMAHIDLYRRYGTVYLdrnnieemhrgyiekIFKYMARHHIGLEINTSGLRRELGDLHpskaiVQTALQQGVQIFTT 247
Cdd:cd07432    65 -LVVLAHPDRPSRYGLSDL---------------ILKPLIKNGDAIEVNNSRLRYGLNNLA-----AKRYAELGGLPITG 123

                  ....*.
gi 1224461214 248 GSDAHS 253
Cdd:cd07432   124 GSDAHT 129
PHP_HisPPase_Ycdx_like cd07437
Polymerase and Histidinol Phosphatase domain of Ycdx like; PHP Ycdx-like is a stand alone PHP ...
120-272 8.81e-05

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: 42.81  E-value: 8.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224461214 120 DFVLGSIHclnhvaisskKECavhFAGKTCAEVAQDYFtsleAAVKSRLFDCMAHIDLYRrygtvY-LDrnnieemhrgy 198
Cdd:cd07437    93 DYVIASLH----------EPC---FAPGTKEENTRAYI----NAMENPYVDIIGHPGNPR-----YpID----------- 139
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224461214 199 IEKIFKYMARHHIGLEINTSGLRRELGDLHPS-KAIVQTALQQGVQIfTTGSDAHSLSEIGQgLQAAERLLKQFD 272
Cdd:cd07437   140 YEAVVKAAKEYNVLLEINNSSLSPSRKGSRENcREIAELCKKYGVPV-IVGSDAHIAYDIGN-FDEALELLEEIG 212
PRK09248 PRK09248
putative hydrolase; Validated
199-272 1.53e-04

putative hydrolase; Validated


Pssm-ID: 236429 [Multi-domain]  Cd Length: 246  Bit Score: 42.13  E-value: 1.53e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1224461214 199 IEKIFKYMARHHIGLEINTS--GLRRElGDLHPSKAIVQTALQQGVQIfTTGSDAHSLSEIGqGLQAAERLLKQFD 272
Cdd:PRK09248  142 IEAVVKAAKEHNVALEINNSsfGHSRK-GSEDNCRAIAALCKKAGVWV-ALGSDAHIAFDIG-NFEEALKILDEVG 214
 
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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