|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06361 |
PRK06361 |
histidinol phosphate phosphatase domain-containing protein; |
9-217 |
2.18e-105 |
|
histidinol phosphate phosphatase domain-containing protein;
Pssm-ID: 180543 [Multi-domain] Cd Length: 212 Bit Score: 302.26 E-value: 2.18e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 9 THTILSDGELICSEQIRHAQIHGYTAIAISDHVDESNIDFVLNSLNKFVDNESSYFeGIKILKGVEITHVPPLLIDNLAK 88
Cdd:PRK06361 1 THTIFSDGELIPSELVRRARVLGYRAIAITDHADASNLEEILEKLVRAAEELELYW-DIEVIPGVELTHVPPKLIPKLAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 89 HAKENGADIVLVHGETIVEPVFKKTNYYAVTSKYVDILAHPGLISEEEVALAAKNGVFLELSARKGHSLSNGHVRKLAQK 168
Cdd:PRK06361 80 KARDLGAEIVVVHGETIVEPVEEGTNLAAIECEDVDILAHPGLITEEEAELAAENGVFLEITARKGHSLTNGHVARIARE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1341787971 169 YEAKLLVNSDAHGPDDFLDYDFSLKVALSAGLSIEEAKKIVEKNPLELL 217
Cdd:PRK06361 160 AGAPLVINTDTHAPSDLITYEFARKVALGAGLTEKELEEALENNPKLLL 208
|
|
| HIS2 |
COG1387 |
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ... |
4-204 |
4.71e-51 |
|
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: 164.94 E-value: 4.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 4 LYDFHTHTILSDGELICSEQIRHAQIHGYTAIAISDHVDESNIDFVLNSLN-----KFVDNESSYFEGIKILKGVEITHV 78
Cdd:COG1387 2 RGDLHTHTTYSDGEGTIEEMVEAAIELGLEYIAITDHSPSLFVANGLSEERlleylEEIEELNEKYPDIKILKGIEVDIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 79 PPLLIDNLAKHAKENGADIVLVHG--ETIVEPVFKkTNYYAVTSKYVDILAHPGLI-----------SEEEVALAAKNGV 145
Cdd:COG1387 82 PDGSLDYPDELLAPLDYVIGSVHSilEEDYEEYTE-RLLKAIENPLVDILGHPDGRllggrpgyevdIEEVLEAAAENGV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1341787971 146 FLELSARKGHSLSNGHVRKLAQKYEAKLLVNSDAHGPDDFLDYDFSLKVALSAGLSIEE 204
Cdd:COG1387 161 ALEINTRPLRLDPSDELLKLAKELGVKITIGSDAHSPEDLGDLEYGVALARRAGLTKED 219
|
|
| PHP_HisPPase |
cd07432 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ... |
5-180 |
1.47e-15 |
|
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: 70.35 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 5 YDFHTHTILS-DGELICSEQIRHAQIHGYTAIAISDHVDESNIDFVLnslnkfvdnESSYFEGIKILKGVEIThvpplli 83
Cdd:cd07432 1 ADLHIHSVFSpDSDMTPEEIVERAIELGLDGIAITDHNTIDGAEEAL---------KEAYKDGLLVIPGVEVT------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 84 dnlakhakengadivlvhgetivepvfkktnyyavtskyVDILAHPGLIS-----EEEVALAAKNGVFLELSARKGH-SL 157
Cdd:cd07432 65 ---------------------------------------LVVLAHPDRPSryglsDLILKPLIKNGDAIEVNNSRLRyGL 105
|
170 180
....*....|....*....|...
gi 1341787971 158 SNGHVRKLAQKYEAKLLVNSDAH 180
Cdd:cd07432 106 NNLAAKRYAELGGLPITGGSDAH 128
|
|
| RNase_P_p30 |
pfam01876 |
RNase P subunit p30; This protein is part of the RNase P complex that is involved in tRNA ... |
5-212 |
6.79e-13 |
|
RNase P subunit p30; This protein is part of the RNase P complex that is involved in tRNA maturation.
Pssm-ID: 396447 [Multi-domain] Cd Length: 214 Bit Score: 64.97 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 5 YDFHTHTiLSDGELICSEQIRHAQIHGYTAIAISDHVDESNIDFVLNSLNKF-VDNESSYFEGIKILKGVEITHVPPLLI 83
Cdd:pfam01876 1 YDLNIPW-PPDGSKLPSRTILTLAELGYTGVAINFTVEAEDGKIPDASEIAErLDELRPELYGLKVYSRVTLVVSDPSKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 84 DNLAKHAkeNGADIVLVHGETIvepvfkKTNYYAVTSKYVDILAH------PGLISEEEVALAAKNGVFLELS------- 150
Cdd:pfam01876 80 QLLSKFR--QKYDLLAVRPGDE------KANRAACENLDVDIISFpytsrlPFGLKHKLARLAVERGVAFEINyspalrd 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 151 ---ARKgHSLSNghVRKLAQKYEAK-LLVNSdahGPDDFLD----YDFSlKVALSAGLSIEEAKKIVEKN 212
Cdd:pfam01876 152 sggSRR-NFISN--ARSLLRLTRGRpVVISS---GARSPLElrapYDVI-NLLKTLGLDEDRAKEAVTTN 214
|
|
| POLIIIAc |
smart00481 |
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ... |
6-79 |
2.82e-05 |
|
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: 40.71 E-value: 2.82e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1341787971 6 DFHTHTILS--DGELICSEQIRHAQIHGYTAIAISDHvdesnidfvlNSLNKFVD-NESSYFEGIKILKGVEITHVP 79
Cdd:smart00481 1 DLHVHSDYSllDGALSPEELVKRAKELGLKAIAITDH----------GNLFGAVEfYKAAKKAGIKPIIGLEANIVD 67
|
|
| CehA_McbA_metalo |
NF038032 |
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ... |
6-77 |
3.52e-03 |
|
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: 37.69 E-value: 3.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1341787971 6 DFHTHTILSDGELICSEQIRHAQIHGYTAIAISDHVDESNidfvlnslNKFVDNESSYFEGIKILKGVEITH 77
Cdd:NF038032 6 DLHIHTNHSDGPTTPEELARAALAEGLDVIALTDHNTISG--------RAYFAELLASERGLLVIPGMEVTT 69
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06361 |
PRK06361 |
histidinol phosphate phosphatase domain-containing protein; |
9-217 |
2.18e-105 |
|
histidinol phosphate phosphatase domain-containing protein;
Pssm-ID: 180543 [Multi-domain] Cd Length: 212 Bit Score: 302.26 E-value: 2.18e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 9 THTILSDGELICSEQIRHAQIHGYTAIAISDHVDESNIDFVLNSLNKFVDNESSYFeGIKILKGVEITHVPPLLIDNLAK 88
Cdd:PRK06361 1 THTIFSDGELIPSELVRRARVLGYRAIAITDHADASNLEEILEKLVRAAEELELYW-DIEVIPGVELTHVPPKLIPKLAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 89 HAKENGADIVLVHGETIVEPVFKKTNYYAVTSKYVDILAHPGLISEEEVALAAKNGVFLELSARKGHSLSNGHVRKLAQK 168
Cdd:PRK06361 80 KARDLGAEIVVVHGETIVEPVEEGTNLAAIECEDVDILAHPGLITEEEAELAAENGVFLEITARKGHSLTNGHVARIARE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1341787971 169 YEAKLLVNSDAHGPDDFLDYDFSLKVALSAGLSIEEAKKIVEKNPLELL 217
Cdd:PRK06361 160 AGAPLVINTDTHAPSDLITYEFARKVALGAGLTEKELEEALENNPKLLL 208
|
|
| HIS2 |
COG1387 |
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ... |
4-204 |
4.71e-51 |
|
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: 164.94 E-value: 4.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 4 LYDFHTHTILSDGELICSEQIRHAQIHGYTAIAISDHVDESNIDFVLNSLN-----KFVDNESSYFEGIKILKGVEITHV 78
Cdd:COG1387 2 RGDLHTHTTYSDGEGTIEEMVEAAIELGLEYIAITDHSPSLFVANGLSEERlleylEEIEELNEKYPDIKILKGIEVDIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 79 PPLLIDNLAKHAKENGADIVLVHG--ETIVEPVFKkTNYYAVTSKYVDILAHPGLI-----------SEEEVALAAKNGV 145
Cdd:COG1387 82 PDGSLDYPDELLAPLDYVIGSVHSilEEDYEEYTE-RLLKAIENPLVDILGHPDGRllggrpgyevdIEEVLEAAAENGV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1341787971 146 FLELSARKGHSLSNGHVRKLAQKYEAKLLVNSDAHGPDDFLDYDFSLKVALSAGLSIEE 204
Cdd:COG1387 161 ALEINTRPLRLDPSDELLKLAKELGVKITIGSDAHSPEDLGDLEYGVALARRAGLTKED 219
|
|
| PHP_HisPPase |
cd07432 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ... |
5-180 |
1.47e-15 |
|
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: 70.35 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 5 YDFHTHTILS-DGELICSEQIRHAQIHGYTAIAISDHVDESNIDFVLnslnkfvdnESSYFEGIKILKGVEIThvpplli 83
Cdd:cd07432 1 ADLHIHSVFSpDSDMTPEEIVERAIELGLDGIAITDHNTIDGAEEAL---------KEAYKDGLLVIPGVEVT------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 84 dnlakhakengadivlvhgetivepvfkktnyyavtskyVDILAHPGLIS-----EEEVALAAKNGVFLELSARKGH-SL 157
Cdd:cd07432 65 ---------------------------------------LVVLAHPDRPSryglsDLILKPLIKNGDAIEVNNSRLRyGL 105
|
170 180
....*....|....*....|...
gi 1341787971 158 SNGHVRKLAQKYEAKLLVNSDAH 180
Cdd:cd07432 106 NNLAAKRYAELGGLPITGGSDAH 128
|
|
| PHP_PolX |
cd07436 |
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal ... |
6-209 |
1.34e-14 |
|
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: 70.14 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 6 DFHTHTILSDGELICSEQIRHAQIHGYTAIAISDHvdeSNIDFVLNSL--------NKFVD--NESsyFEGIKILKGVEI 75
Cdd:cd07436 8 DLHVHTTWSDGRNSIEEMAEAARALGYEYIAITDH---SKSLRVANGLseerlreqIEEIDalNEK--LPGIRILKGIEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 76 thvpplliDNLakhakENGA-----------DIVL--VHG------ETIVEPVFKktnyyAVTSKYVDILAHP-G-LISE 134
Cdd:cd07436 83 --------DIL-----PDGSldypdevlaelDVVVasVHSgfnqseEEMTERLLK-----AIENPHVDILGHPtGrLLGR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 135 --------EEV-ALAAKNGVFLELSARKGHS-LSNGHVRKlAQKYEAKLLVNSDAHGPDDFLDYDFSLKVALSAGLsieE 204
Cdd:cd07436 145 regyevdmERViEAAAETGTALEINANPDRLdLDDRHARR-AKEAGVKIAINTDAHSTDGLDNMRYGVGTARRGWL---E 220
|
....*
gi 1341787971 205 AKKIV 209
Cdd:cd07436 221 KEDVL 225
|
|
| PHP_HisPPase_Ycdx_like |
cd07437 |
Polymerase and Histidinol Phosphatase domain of Ycdx like; PHP Ycdx-like is a stand alone PHP ... |
6-199 |
1.98e-13 |
|
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: 66.70 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 6 DFHTHTILSD------GELICSeqirhAQIHGYTAIAISDH----VDESNIDFVLNSlnKFVDNEssyFEGIKILKGVEI 75
Cdd:cd07437 4 DLHTHTIASGhaystiEEMARA-----AAEKGLKLLGITDHgpamPGAPHPWYFGNL--KVIPRE---IYGVRILRGVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 76 THV--------PPLLIDNLakhakengaDIVL--VHgetivEPVFKK------TNYY--AVTSKYVDILAHPG----LIS 133
Cdd:cd07437 74 NIIdydgnldlPERVLKRL---------DYVIasLH-----EPCFAPgtkeenTRAYinAMENPYVDIIGHPGnpryPID 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1341787971 134 EEEVALAAK-NGVFLEL------SARKGhslSNGHVRKLAQ---KYEAKLLVNSDAHGPDDFLDYDFSLKVALSAG 199
Cdd:cd07437 140 YEAVVKAAKeYNVLLEInnsslsPSRKG---SRENCREIAElckKYGVPVIVGSDAHIAYDIGNFDEALELLEEIG 212
|
|
| RPP1 |
COG1603 |
RNase P/RNase MRP subunit p30 [Translation, ribosomal structure and biogenesis]; |
3-213 |
3.61e-13 |
|
RNase P/RNase MRP subunit p30 [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441211 [Multi-domain] Cd Length: 231 Bit Score: 66.07 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 3 KLYDFHTHtILSDGELICSEQIRHAQIHGYTAIAISDHvDESNIDFVLNSLNKFvdnessyfEGIKILKGVEITHVPP-L 81
Cdd:COG1603 2 KMYDLAVH-AYPDGDSTVARLALTAKRLGYDGIVVRNH-SDARADYDAEAIREE--------YGIDVVRGVEIRADNPsK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 82 LIDNLAKHAKENgaDIVLVHGETIvepvfkKTNYYAVTSKYVDILAHP-----GLISEEEVALAAKNGVFLELS------ 150
Cdd:COG1603 72 LSGAVGNYRPKV--DVVAVHGGDE------KINRAAVENPRVDVLAHPmtardGGFNHVLAKAAAENGVAVEFDlgpllr 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1341787971 151 ARKG---HSLSN-GHVRKLAQKYEAKLLVNSDAHgpdDFLDydfsLK-----VALSA--GLSIEEAKKIVEKNP 213
Cdd:COG1603 144 ARGGrrvRALQRlRKLLELVRKYDFPLVVSSGAR---SHLD----LRaprelIALGElfGFEEEEAEEGLSEWP 210
|
|
| RNase_P_p30 |
pfam01876 |
RNase P subunit p30; This protein is part of the RNase P complex that is involved in tRNA ... |
5-212 |
6.79e-13 |
|
RNase P subunit p30; This protein is part of the RNase P complex that is involved in tRNA maturation.
Pssm-ID: 396447 [Multi-domain] Cd Length: 214 Bit Score: 64.97 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 5 YDFHTHTiLSDGELICSEQIRHAQIHGYTAIAISDHVDESNIDFVLNSLNKF-VDNESSYFEGIKILKGVEITHVPPLLI 83
Cdd:pfam01876 1 YDLNIPW-PPDGSKLPSRTILTLAELGYTGVAINFTVEAEDGKIPDASEIAErLDELRPELYGLKVYSRVTLVVSDPSKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 84 DNLAKHAkeNGADIVLVHGETIvepvfkKTNYYAVTSKYVDILAH------PGLISEEEVALAAKNGVFLELS------- 150
Cdd:pfam01876 80 QLLSKFR--QKYDLLAVRPGDE------KANRAACENLDVDIISFpytsrlPFGLKHKLARLAVERGVAFEINyspalrd 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 151 ---ARKgHSLSNghVRKLAQKYEAK-LLVNSdahGPDDFLD----YDFSlKVALSAGLSIEEAKKIVEKN 212
Cdd:pfam01876 152 sggSRR-NFISN--ARSLLRLTRGRpVVISS---GARSPLElrapYDVI-NLLKTLGLDEDRAKEAVTTN 214
|
|
| PRK09248 |
PRK09248 |
putative hydrolase; Validated |
1-217 |
2.01e-12 |
|
putative hydrolase; Validated
Pssm-ID: 236429 [Multi-domain] Cd Length: 246 Bit Score: 64.09 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 1 MNKLYDFHTHTILSD---GELIcsEQIRHAQIHGYTAIAISDH----VDESNIDFVLNS--LNKFVDnessyfeGIKILK 71
Cdd:PRK09248 1 MKYPVDTHTHTIASGhaySTLH--ENAAEAKQKGLKLFAITDHgpdmPGAPHYWHFGNLrvLPRKVD-------GVGILR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 72 GVEIT--------HVPPLLIDNLakhakengaDIVL--VHgetivEPVF----KKTNYYAV----TSKYVDILAHPG--- 130
Cdd:PRK09248 72 GIEANiknydgeiDLPGDMLKKL---------DIVIagFH-----EPVFapgdKETNTQALinaiKNGRVDIIGHPGnpk 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 131 -LISEEEVALAAK-NGVFLEL------SARKGHSLSNGHVRKLAQKYEAKLLVNSDAHGPDDFLDYDFSLKVALSAGLSI 202
Cdd:PRK09248 138 yPIDIEAVVKAAKeHNVALEInnssfgHSRKGSEDNCRAIAALCKKAGVWVALGSDAHIAFDIGNFEEALKILDEVGFPE 217
|
250
....*....|....*
gi 1341787971 203 EeakKIVEKNPLELL 217
Cdd:PRK09248 218 E---RILNVSPRRLL 229
|
|
| YciV |
COG0613 |
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ... |
5-186 |
3.29e-11 |
|
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and metabolism];
Pssm-ID: 440378 [Multi-domain] Cd Length: 188 Bit Score: 59.92 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 5 YDFHTHTILSDGELICSEQIRHAQIHGYTAIAISDHvdesnidFVLNSLNKFVDNESSYfeGIKILKGVEI-THVPPLLI 83
Cdd:COG0613 4 IDLHVHTTASDGSLSPEELVARAKAAGLDVLAITDH-------DTVAGYEEAAEAAKEL--GLLVIPGVEIsTRWEGREV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 84 DNLAKHAKENGADIVlvhgETIVEPVFKKTNYYAVTSKYVD---------ILAHPGLISEEEV------ALAAKNGVFLE 148
Cdd:COG0613 75 HILGYGIDPEDPALE----ALLGIPVEKAEREWLSLEEAIDlireaggvaVLAHPFRYKRGRWlddlleELADAGLDGIE 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 1341787971 149 LSARKGHSLSNGHVRKLAQKYEAKLLVNSDAHGPDDFL 186
Cdd:COG0613 151 VYNGRHSPEDNERAAELAEEYGLLATGGSDAHGPEKPL 188
|
|
| PRK00912 |
PRK00912 |
ribonuclease P protein component 3; Provisional |
3-217 |
3.10e-10 |
|
ribonuclease P protein component 3; Provisional
Pssm-ID: 234862 [Multi-domain] Cd Length: 237 Bit Score: 58.10 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 3 KLYDFHTHTiLSDGELICSEQIRHAQIHGYTAIAISdhvdesnidfvlNSLNKFVDNESSYF--EGIKILKGVEITHVPP 80
Cdd:PRK00912 2 KFYDLNVHA-VPDGYDTVLRLISEASHLGYSGIALS------------NHSDKYPESKPELEdlLGFEIFRGVEIVASNP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 81 LLIDNLAKHAKeNGADIVLVHGETivepvfKKTNYYAVTSKYVDILAHPGLISEEE------VALAAKNGVFLELS---- 150
Cdd:PRK00912 69 SKLRGLVGKFR-KKVDVLAVHGGD------EKVNRAACENPRVDILSHPYTKRKDSginhvlAKEAARNNVAIEFNlrdi 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1341787971 151 -----ARKGHSLSN-GHVRKLAQKYEAKLLVNSDAHGPDDFLDYDFSLKVALSAGLSIEEAKKIVEKNPLELL 217
Cdd:PRK00912 142 lksrgGRRARTLSNfRDNLALARKYDFPLVLTSGAMSCYDLRSPREMIALAELFGMEEDEALKALSYYPESII 214
|
|
| PRK08392 |
PRK08392 |
hypothetical protein; Provisional |
6-204 |
5.41e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 169423 [Multi-domain] Cd Length: 215 Bit Score: 57.10 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 6 DFHTHTILSDGELICSEQIRHAQIHGYTAIAISDHVDEsnidFVLNSLNKFVDNESSYFEG--IKILKGVE--ITHVPPL 81
Cdd:PRK08392 2 DLHTHTVYSDGIGSVRDNIAEAERKGLRLVGISDHIHY----FTPSKFNAYINEIRQWGEEseIVVLAGIEanITPNGVD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 82 LIDNLAKHakengADIVL--VHGETIVEPVFKKTNYY--AVTSKYVDILAHPGLI-------SEEE----VALAAKNGVF 146
Cdd:PRK08392 78 ITDDFAKK-----LDYVIasVHEWFGRPEHHEYIELVklALMDENVDIIGHFGNSfpyigypSEEElkeiLDLAEAYGKA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1341787971 147 LELSARkgHSLSNGHVRKLAQKYEAKLLVNSDAHGPDDFLDYDFSLKVALSAGLSIEE 204
Cdd:PRK08392 153 FEISSR--YRVPDLEFIRECIKRGIKLTFASDAHRPEDVGNVSWSLKVFKKAGGKKED 208
|
|
| PRK08609 |
PRK08609 |
DNA polymerase/3'-5' exonuclease PolX; |
6-188 |
3.52e-09 |
|
DNA polymerase/3'-5' exonuclease PolX;
Pssm-ID: 236311 [Multi-domain] Cd Length: 570 Bit Score: 55.73 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 6 DFHTHTILSDGELICSEQIRHAQIHGYTAIAISDHvdeSNIDFVLNSL--------NKFVDNESSYFEGIKILKGVEITH 77
Cdd:PRK08609 337 DLHMHTTWSDGAFSIEEMVEACIAKGYEYMAITDH---SQYLKVANGLteerlleqAEEIKALNEKYPEIDILSGIEMDI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 78 VPPLLIDNLAKHAKENGADIVLVHG------ETIVEPVfkKTnyyAVTSKYVDILAHPG--LIS---------EEEVALA 140
Cdd:PRK08609 414 LPDGSLDYDDEVLAELDYVIAAIHSsfsqseEEIMKRL--EN---ACRNPYVRLIAHPTgrLIGrrdgydvniDQLIELA 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1341787971 141 AKNGVFLELSARKGH-SLSNGHVRKlAQKYEAKLLVNSDAHGPD--DFLDY 188
Cdd:PRK08609 489 KETNTALELNANPNRlDLSAEHLKK-AQEAGVKLAINTDAHHTEmlDDMKY 538
|
|
| PHP_HisPPase_Hisj_like |
cd12110 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; ... |
5-190 |
1.53e-07 |
|
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: 50.25 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 5 YDFHTHTILSD---GELIcsEQIRHAQIHGYTAIAISDH--------------VDESNIDFVLNSLNKFVDNessYFEGI 67
Cdd:cd12110 1 VDYHTHTPRCDhasGTLE--EYVEAAIELGFTEIGFSEHaplpfefddypesrMAEEELEDYVEEIRRLKEK---YADQI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 68 KILKGVEITHVPP---LLIDNLAKH---------------AKENGADIVLVHGETIVEPVFKKtnYY-----AVTSKYVD 124
Cdd:cd12110 76 EIKLGLEVDYFPGyeeELRELLYGYpldyvigsvhflggwGFDFPEDGIAEYFEGDIDELYER--YFdlvekAIESGLFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 125 ILAHPGLI----------------SEEEVALAAKNGVFLELSA---RKGHSLS--NGHVRKLAQKYEAKLLVNSDAHGPD 183
Cdd:cd12110 154 IIGHPDLIkkfgkndepdedyeelIERILRAIAEAGVALEINTaglRKPVGEPypSPEFLELAKELGIPVTLGSDAHSPE 233
|
....*..
gi 1341787971 184 DfLDYDF 190
Cdd:cd12110 234 D-VGQGY 239
|
|
| PHP_HisPPase_Chlorobi_like |
cd12112 |
Polymerase and Histidinol Phosphatase domain of Chlorobi like; The PHP (also called histidinol ... |
6-76 |
1.27e-06 |
|
Polymerase and Histidinol Phosphatase domain of Chlorobi 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. Chlorobi PHP is uncharacterized protein. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to produce 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: 213996 [Multi-domain] Cd Length: 235 Bit Score: 47.71 E-value: 1.27e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1341787971 6 DFHTHTILSDGELICSEQIRHAQIHGYTAIAISDHVD-ESNIDFVLNS-LNKFVD--NESSYFEGIKILKGVEIT 76
Cdd:cd12112 16 DFHTHTVFSDGHVWPEIRVREAWREGLDAIAITEHIEyRPHKEDIPHPdRNRSYKiaKEAAESKGLLIIPGAEIT 90
|
|
| PHP_HisPPase_AMP |
cd07438 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) ... |
5-181 |
3.48e-06 |
|
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) AMP bound; The PHP domain of this HisPPase family has an unknown function. It has a second domain inserted in the middle that binds adenosine 5-monophosphate (AMP). The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to give histidinol. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to the other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.
Pssm-ID: 213993 [Multi-domain] Cd Length: 155 Bit Score: 45.46 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 5 YDFHTHTILSDGELICSEQIRHAQIHGYTAIAISDH--VDesNIDFVLNSLNKFvdnessyfeGIKILKGVEIThvppll 82
Cdd:cd07438 1 IDLHTHSTASDGTLSPEELVELAKEAGLKVLAITDHdtVA--GLEEALAAAKEL---------GIELIPGVEIS------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 83 idnlakhAKENGADI-VLVHGETIVEpVFKKTNYYAVtskyvdiLAHPGLI------SEEEVALAAKNGVF-LELSARKG 154
Cdd:cd07438 64 -------TEYEGREVhILGSPEEAIE-LIHAAGGVAV-------LAHPGLYklsrkkLEELIEELKEAGLDgIEVYHPYH 128
|
170 180
....*....|....*....|....*....
gi 1341787971 155 HSLSNGHVRKLAQKYeaKLLVN--SDAHG 181
Cdd:cd07438 129 SPEDRERLLELAKEY--GLLVTggSDFHG 155
|
|
| PolX |
COG1796 |
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair]; |
6-188 |
4.67e-06 |
|
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
Pssm-ID: 441401 [Multi-domain] Cd Length: 567 Bit Score: 46.72 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 6 DFHTHTILSDGELICSEQIRHAQIHGYTAIAISDHVDESnidFVLNSLN--------KFVDNESSYFEGIKILKGVEITH 77
Cdd:COG1796 339 DLHHHTTWSDGGASIEEMAAAAAARGYYYIAITDHSSSL---VVAGGLDeerllqqeEEIDALNERLDGIILLLGGEEDI 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 78 VPPLLIDNLAKHAKENGADIVLVHGETIVEPVFKKTNYYAV-TSKYVDILAHPG-----------LISEEEVALAAKNGV 145
Cdd:COG1796 416 LDDGGLDDDDDLLLEDDDVVAAVHHSFLLQDEEMTRRRLAAaNEPVVVIIHHPTgrlllrrrpyyVDDEAIIAAAAAAGA 495
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1341787971 146 FLELSARKGHSLSNGHVRKLAQKYEAKLLVNSDAHGPDDFLDY 188
Cdd:COG1796 496 LEEENNAPRRLLLLDDLARAAAEGGVVIIIIDDAHHTDLLLDL 538
|
|
| POLIIIAc |
smart00481 |
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ... |
6-79 |
2.82e-05 |
|
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: 40.71 E-value: 2.82e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1341787971 6 DFHTHTILS--DGELICSEQIRHAQIHGYTAIAISDHvdesnidfvlNSLNKFVD-NESSYFEGIKILKGVEITHVP 79
Cdd:smart00481 1 DLHVHSDYSllDGALSPEELVKRAKELGLKAIAITDH----------GNLFGAVEfYKAAKKAGIKPIIGLEANIVD 67
|
|
| PHP_HisPPase_Thermotoga_like |
cd12111 |
Polymerase and Histidinol Phosphatase domain of Thermotoga like; The PHP (also called ... |
4-101 |
1.05e-04 |
|
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: 42.02 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 4 LYDFHTHTILSDGELICSEQIRHAQIHGYTAIAISDHV-DESNIDFVLNSLNKFVDNESSYFEGIKILK----------- 71
Cdd:cd12111 3 LCDFHIHTTYSDGALSLSEVVDLYGQHGFDVIAITDHVvDRASLIGKFPQGTHPGVTEANFEDYMEALKveakrawekye 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1341787971 72 -----GVEIT------HV----------PPLLIDNLAKHAKENGADIVLVH 101
Cdd:cd12111 83 mivipGVELTnntdsyHIlgidvkeyidPCLSVEEIIAEIHKQGGIAVAAH 133
|
|
| PHP |
cd07309 |
Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2 ... |
6-76 |
2.95e-03 |
|
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: 35.87 E-value: 2.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1341787971 6 DFHTHTILSDGELI-CSEQIRHAQIHGYTAIAISDHVDESNiDFVLNSLNKFVDNESSYFEGIKILKGVEIT 76
Cdd:cd07309 2 DLHTHTVFSDGDHAkLTELVDKAKELGPDALAITDHGNLRG-LAEFNTAGK*NHIKAAEAAGIKIIIGSEVN 72
|
|
| CehA_McbA_metalo |
NF038032 |
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ... |
6-77 |
3.52e-03 |
|
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: 37.69 E-value: 3.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1341787971 6 DFHTHTILSDGELICSEQIRHAQIHGYTAIAISDHVDESNidfvlnslNKFVDNESSYFEGIKILKGVEITH 77
Cdd:NF038032 6 DLHIHTNHSDGPTTPEELARAALAEGLDVIALTDHNTISG--------RAYFAELLASERGLLVIPGMEVTT 69
|
|
| PHP |
pfam02811 |
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ... |
6-99 |
4.62e-03 |
|
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative phosphoesterase domain.
Pssm-ID: 460705 [Multi-domain] Cd Length: 171 Bit Score: 36.37 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341787971 6 DFHTHTILS--DGELICSEQIRHAQIHGYTAIAISDHVDesnidfvLNSLNKFVDNESSYfeGIKILKGVEITHVPPLLI 83
Cdd:pfam02811 1 HLHVHSEYSllDGAARIEELVKRAKELGMPAIAITDHGN-------LFGAVEFYKAAKKA--GIKPIIGCEVYVAPGSRE 71
|
90
....*....|....*.
gi 1341787971 84 DnlAKHAKENGADIVL 99
Cdd:pfam02811 72 E--TEKLLAKYFDLVL 85
|
|
| |
