|
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
|
|
|