|
Name |
Accession |
Description |
Interval |
E-value |
| HIS2 |
COG1387 |
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ... |
1-237 |
2.48e-49 |
|
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: 161.48 E-value: 2.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 1 MIDYHIHSNFSpDSNSSVEDIVKYAREKNLKII-ITDHYEAVEKDHNFKFD-VKSYKEAM----KKYG---LLVGVEFGW 71
Cdd:COG1387 2 RGDLHTHTTYS-DGEGTIEEMVEAAIELGLEYIaITDHSPSLFVANGLSEErLLEYLEEIeelnEKYPdikILKGIEVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 72 DGKSKIDID---LKEFDFVILSYHAYKEyddiqKMYENYLKDLYNIIEVvNDFHVLGHLDFPRRFvkNNEPFSkklyPLI 148
Cdd:COG1387 81 LPDGSLDYPdelLAPLDYVIGSVHSILE-----EDYEEYTERLLKAIEN-PLVDILGHPDGRLLG--GRPGYE----VDI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 149 SEIFKKIIKEGKILEVNTSAiYRYGepnPSYDILKLYRDLGGKyVTIGSDAHRLEDVGrGIYDTLGNLKDLGFEYIMVLN 228
Cdd:COG1387 149 EEVLEAAAENGVALEINTRP-LRLD---PSDELLKLAKELGVK-ITIGSDAHSPEDLG-DLEYGVALARRAGLTKEDVFN 222
|
250
....*....|
gi 490202520 229 D-GKWDMEKI 237
Cdd:COG1387 223 TlRKEELLKL 232
|
|
| PRK05588 |
PRK05588 |
histidinol phosphate phosphatase; |
1-207 |
6.78e-39 |
|
histidinol phosphate phosphatase;
Pssm-ID: 235519 [Multi-domain] Cd Length: 255 Bit Score: 135.16 E-value: 6.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 1 MIDYHIHSNFSPDSNSSVEDIVKYAREKNLKIIITDHYEAVEKDHN-FKFDVKSYKEAMKKY---GLLVGVEFGWdGKSK 76
Cdd:PRK05588 1 MFDTHIHTEFSTDSKMKIEEAIKKAKENNLGIIITEHMDLNLPDKNkFCFDVDSYFNKYSKYrnnKLLLGIELGM-EKDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 77 IDIDLK-----EFDFVILSYHA-------YKE-YDDIQK--MYENYLKDLYNIIEVVNDFHVLGHLDFPRRFVK--NNEP 139
Cdd:PRK05588 80 IEENKElinkyEFDYVIGSIHLvdkldlyLDEfYKDKSKeeAYHIYFENMLKCLEKYDFIDSLGHIDYISRYAKyeDKEI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490202520 140 FSKKLYPLISEIFKKIIKEGKILEVNTSAIYRYGEPNPSYDILKLYRDLGGKYVTIGSDAHRLEDVGR 207
Cdd:PRK05588 160 YYDEFKEIIDEILKVLIEKEKVLEINTRRLDDKRSVENLVKIYKRFYELGGKYITLGSDAHNIEDIGN 227
|
|
| PHP_HisPPase_Hisj_like |
cd12110 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; ... |
2-208 |
2.12e-34 |
|
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: 123.44 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 2 IDYHIHSNFSPDSNSSVEDIVKYAREKNLKII-ITDH----------YEAVEKDHNFKFDVKSYKEAMKKYG----LLVG 66
Cdd:cd12110 1 VDYHTHTPRCDHASGTLEEYVEAAIELGFTEIgFSEHaplpfefddyPESRMAEEELEDYVEEIRRLKEKYAdqieIKLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 67 VEFGW-DGKSKIDIDLKE---FDFVILSYH--------------AYKEYDDIQKMYENYLKDLYNIIEvVNDFHVLGHLD 128
Cdd:cd12110 81 LEVDYfPGYEEELRELLYgypLDYVIGSVHflggwgfdfpedgiAEYFEGDIDELYERYFDLVEKAIE-SGLFDIIGHPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 129 FPRRFvKNNEPFSKKLYPLISEIFKKIIKEGKILEVNTSAIYR-YGEPNPSYDILKLYRDLGGKyVTIGSDAHRLEDVGR 207
Cdd:cd12110 160 LIKKF-GKNDEPDEDYEELIERILRAIAEAGVALEINTAGLRKpVGEPYPSPEFLELAKELGIP-VTLGSDAHSPEDVGQ 237
|
.
gi 490202520 208 G 208
Cdd:cd12110 238 G 238
|
|
| hisJ_fam |
TIGR01856 |
histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate ... |
2-213 |
1.93e-30 |
|
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: 113.26 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 2 IDYHIHSNFSPDSNSSVEDIVKYAREKNLK-IIITDH----YEAVEKDHNFKFD----VKSYKEAM----KKYG----LL 64
Cdd:TIGR01856 1 RDSHSHSPFCAHGTDTLREVVQEAIQLGFEeICFTEHaprpFYYPEEDFLKKEMlflsLPEYFQEInqlkQEYAdkikIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 65 VGVEFGWDGKSKIDI----DLKEFDFVILSYHA------------YKE-----YDDIQKMYENYLKDLYNIIEVVNDFHV 123
Cdd:TIGR01856 81 IGLEVDYIPGFEEEIkdflDSYNLDFVIGSVHHlggipidfdieeFDEtlfsfQKNLEQAQRDYFESQYDSIQNLFKPLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 124 LGHLDFPRRFVKNNEPFSKK--LYPLISEIFKKIIKEGKILEVNTSAI-YRYGEPNPSYDILKLYRdLGGKYVTIGSDAH 200
Cdd:TIGR01856 161 IGHLDLVKKFGPLTDVSSKSdeVRELLQRILKAVASYGKALEINTSGFrKPLEEAYPSKELLNLAK-ELGIPLVLGSDAH 239
|
250
....*....|...
gi 490202520 201 RLEDVGRGIYDTL 213
Cdd:TIGR01856 240 GPGQVGLSYHKAK 252
|
|
| PHP |
pfam02811 |
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ... |
3-167 |
7.55e-20 |
|
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative phosphoesterase domain.
Pssm-ID: 460705 [Multi-domain] Cd Length: 171 Bit Score: 83.36 E-value: 7.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 3 DYHIHSNFS-PDSNSSVEDIVKYAREKNLKII-ITDHYEAvekdhnfkFDVKSYKEAMKKYGL--LVGVEFGWDGKSKID 78
Cdd:pfam02811 1 HLHVHSEYSlLDGAARIEELVKRAKELGMPAIaITDHGNL--------FGAVEFYKAAKKAGIkpIIGCEVYVAPGSREE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 79 I---DLKEFDFVILSYH-------------AYKEYDDIQKMYENYLKDLYNIIEVVndFHVLGHLDFPRRFVKNNEPFSK 142
Cdd:pfam02811 73 TeklLAKYFDLVLLAVHevgyknliklssrAYLEGFKPRIDKELLEEYFEGLIALS--GCVLGHLDLILLAPGDYEEAEE 150
|
170 180
....*....|....*....|....*
gi 490202520 143 klypLISEIFKKIIKEGKILEVNTS 167
Cdd:pfam02811 151 ----LAEEYLEIFGEDGFYLEINTH 171
|
|
| POLIIIAc |
smart00481 |
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ... |
3-69 |
1.27e-08 |
|
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: 50.34 E-value: 1.27e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490202520 3 DYHIHSNFSP-DSNSSVEDIVKYAREKNLKII-ITDHyeavekdHNFKFDVKSYKeAMKKYGL--LVGVEF 69
Cdd:smart00481 1 DLHVHSDYSLlDGALSPEELVKRAKELGLKAIaITDH-------GNLFGAVEFYK-AAKKAGIkpIIGLEA 63
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HIS2 |
COG1387 |
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ... |
1-237 |
2.48e-49 |
|
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: 161.48 E-value: 2.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 1 MIDYHIHSNFSpDSNSSVEDIVKYAREKNLKII-ITDHYEAVEKDHNFKFD-VKSYKEAM----KKYG---LLVGVEFGW 71
Cdd:COG1387 2 RGDLHTHTTYS-DGEGTIEEMVEAAIELGLEYIaITDHSPSLFVANGLSEErLLEYLEEIeelnEKYPdikILKGIEVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 72 DGKSKIDID---LKEFDFVILSYHAYKEyddiqKMYENYLKDLYNIIEVvNDFHVLGHLDFPRRFvkNNEPFSkklyPLI 148
Cdd:COG1387 81 LPDGSLDYPdelLAPLDYVIGSVHSILE-----EDYEEYTERLLKAIEN-PLVDILGHPDGRLLG--GRPGYE----VDI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 149 SEIFKKIIKEGKILEVNTSAiYRYGepnPSYDILKLYRDLGGKyVTIGSDAHRLEDVGrGIYDTLGNLKDLGFEYIMVLN 228
Cdd:COG1387 149 EEVLEAAAENGVALEINTRP-LRLD---PSDELLKLAKELGVK-ITIGSDAHSPEDLG-DLEYGVALARRAGLTKEDVFN 222
|
250
....*....|
gi 490202520 229 D-GKWDMEKI 237
Cdd:COG1387 223 TlRKEELLKL 232
|
|
| PRK05588 |
PRK05588 |
histidinol phosphate phosphatase; |
1-207 |
6.78e-39 |
|
histidinol phosphate phosphatase;
Pssm-ID: 235519 [Multi-domain] Cd Length: 255 Bit Score: 135.16 E-value: 6.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 1 MIDYHIHSNFSPDSNSSVEDIVKYAREKNLKIIITDHYEAVEKDHN-FKFDVKSYKEAMKKY---GLLVGVEFGWdGKSK 76
Cdd:PRK05588 1 MFDTHIHTEFSTDSKMKIEEAIKKAKENNLGIIITEHMDLNLPDKNkFCFDVDSYFNKYSKYrnnKLLLGIELGM-EKDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 77 IDIDLK-----EFDFVILSYHA-------YKE-YDDIQK--MYENYLKDLYNIIEVVNDFHVLGHLDFPRRFVK--NNEP 139
Cdd:PRK05588 80 IEENKElinkyEFDYVIGSIHLvdkldlyLDEfYKDKSKeeAYHIYFENMLKCLEKYDFIDSLGHIDYISRYAKyeDKEI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490202520 140 FSKKLYPLISEIFKKIIKEGKILEVNTSAIYRYGEPNPSYDILKLYRDLGGKYVTIGSDAHRLEDVGR 207
Cdd:PRK05588 160 YYDEFKEIIDEILKVLIEKEKVLEINTRRLDDKRSVENLVKIYKRFYELGGKYITLGSDAHNIEDIGN 227
|
|
| PHP_HisPPase_Hisj_like |
cd12110 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; ... |
2-208 |
2.12e-34 |
|
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: 123.44 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 2 IDYHIHSNFSPDSNSSVEDIVKYAREKNLKII-ITDH----------YEAVEKDHNFKFDVKSYKEAMKKYG----LLVG 66
Cdd:cd12110 1 VDYHTHTPRCDHASGTLEEYVEAAIELGFTEIgFSEHaplpfefddyPESRMAEEELEDYVEEIRRLKEKYAdqieIKLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 67 VEFGW-DGKSKIDIDLKE---FDFVILSYH--------------AYKEYDDIQKMYENYLKDLYNIIEvVNDFHVLGHLD 128
Cdd:cd12110 81 LEVDYfPGYEEELRELLYgypLDYVIGSVHflggwgfdfpedgiAEYFEGDIDELYERYFDLVEKAIE-SGLFDIIGHPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 129 FPRRFvKNNEPFSKKLYPLISEIFKKIIKEGKILEVNTSAIYR-YGEPNPSYDILKLYRDLGGKyVTIGSDAHRLEDVGR 207
Cdd:cd12110 160 LIKKF-GKNDEPDEDYEELIERILRAIAEAGVALEINTAGLRKpVGEPYPSPEFLELAKELGIP-VTLGSDAHSPEDVGQ 237
|
.
gi 490202520 208 G 208
Cdd:cd12110 238 G 238
|
|
| hisJ_fam |
TIGR01856 |
histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate ... |
2-213 |
1.93e-30 |
|
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: 113.26 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 2 IDYHIHSNFSPDSNSSVEDIVKYAREKNLK-IIITDH----YEAVEKDHNFKFD----VKSYKEAM----KKYG----LL 64
Cdd:TIGR01856 1 RDSHSHSPFCAHGTDTLREVVQEAIQLGFEeICFTEHaprpFYYPEEDFLKKEMlflsLPEYFQEInqlkQEYAdkikIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 65 VGVEFGWDGKSKIDI----DLKEFDFVILSYHA------------YKE-----YDDIQKMYENYLKDLYNIIEVVNDFHV 123
Cdd:TIGR01856 81 IGLEVDYIPGFEEEIkdflDSYNLDFVIGSVHHlggipidfdieeFDEtlfsfQKNLEQAQRDYFESQYDSIQNLFKPLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 124 LGHLDFPRRFVKNNEPFSKK--LYPLISEIFKKIIKEGKILEVNTSAI-YRYGEPNPSYDILKLYRdLGGKYVTIGSDAH 200
Cdd:TIGR01856 161 IGHLDLVKKFGPLTDVSSKSdeVRELLQRILKAVASYGKALEINTSGFrKPLEEAYPSKELLNLAK-ELGIPLVLGSDAH 239
|
250
....*....|...
gi 490202520 201 RLEDVGRGIYDTL 213
Cdd:TIGR01856 240 GPGQVGLSYHKAK 252
|
|
| PHP_HisPPase |
cd07432 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ... |
2-201 |
2.04e-25 |
|
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: 96.54 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 2 IDYHIHSNFSPDSNSSVEDIVKYAREKNLKII-ITDHYEAVEkdhnfkfdVKSYKEAMKKYGLLV--GVEFGwdgkskid 78
Cdd:cd07432 1 ADLHIHSVFSPDSDMTPEEIVERAIELGLDGIaITDHNTIDG--------AEEALKEAYKDGLLVipGVEVT-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 79 idlkefdfvilsyhaykeyddiqkmyenylkdlyniievvndFHVLGHLDFPRRFVKNNepfskklyplisEIFKKIIKE 158
Cdd:cd07432 65 ------------------------------------------LVVLAHPDRPSRYGLSD------------LILKPLIKN 90
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490202520 159 GKILEVNTSAiYRYGEPNPsydILKLYRDLGGKYVTIGSDAHR 201
Cdd:cd07432 91 GDAIEVNNSR-LRYGLNNL---AAKRYAELGGLPITGGSDAHT 129
|
|
| PRK07329 |
PRK07329 |
hypothetical protein; Provisional |
1-227 |
5.04e-25 |
|
hypothetical protein; Provisional
Pssm-ID: 180933 [Multi-domain] Cd Length: 246 Bit Score: 98.96 E-value: 5.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 1 MIDYHIHSNFSPDSNSSVEDIVKYAREKnlkIIITDHYEAVEKDHNFKFDVKSY-------KEAMKKYG--LLVGVEFGW 71
Cdd:PRK07329 1 IRDQHLHTHFSFDSDAKFEDYLTHFDGE---IVTTEHLDLSNPYDTGQDDVPDYakysaeiAELNEKYGnrIKKGIEIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 72 DGKSKIDI----DLKEFDFVILSYHAYKEYD---------DIQKMYENYLKDLYNIIEVVNDFHVLGHLDFP-RRF---V 134
Cdd:PRK07329 78 FAPREDDIldflANKDFDLKLLSVHHNGVYDylddevadmDKKELLQEYFEKMEEAIGRVHDADVLAHFDYGlRLFdltV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 135 KNNEPFSkklyPLISEIFKKIIKEGKILEVNTSAIYRYGEPNPSYDILKLYRDLGGKYVTIGSDAHRLEDVGRGIYDTLG 214
Cdd:PRK07329 158 EELKAFE----PQLTRIFAKMIDNDLAFELNTKSMYLYGNEGLYRYAIELYKQLGGKLFSIGSDAHKLEHYRYNFDDAQK 233
|
250
....*....|...
gi 490202520 215 NLKDLGFEYIMVL 227
Cdd:PRK07329 234 LLKEHGIKEIALI 246
|
|
| PRK07328 |
PRK07328 |
histidinol-phosphatase; Provisional |
1-231 |
6.19e-20 |
|
histidinol-phosphatase; Provisional
Pssm-ID: 235992 [Multi-domain] Cd Length: 269 Bit Score: 85.84 E-value: 6.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 1 MIDYHIHSNFSPDSNSSVEDIVKYAREKNLK-IIITDH----------YEA-----VEKDHNFKFDVKSYKEAMKKYGLL 64
Cdd:PRK07328 3 LVDYHMHTPLCGHAVGTPEEYVQAARRAGLKeIGFTDHlpmyflppewRDPglamrLEELPFYVSEVERLRARFPDLYVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 65 VGVEF----GWDGKSKIDIDLKEFDFVILSYHaY------------KEYD--DIQKMYENYlkdlYNIIEVVND---FHV 123
Cdd:PRK07328 83 LGIEAdyhpGTEEFLERLLEAYPFDYVIGSVH-YlgawgfdnpdfvAEYEerDLDELYRRY----FALVEQAARsglFDI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 124 LGHLDFPRRFvkNNEPfSKKLYPLISEIFKKIIKEGKILEVNTsAIYRY--GEPNPSYDILKLYRDLGGKyVTIGSDAHR 201
Cdd:PRK07328 158 IGHPDLIKKF--GHRP-REDLTELYEEALDVIAAAGLALEVNT-AGLRKpvGEIYPSPALLRACRERGIP-VVLGSDAHR 232
|
250 260 270
....*....|....*....|....*....|
gi 490202520 202 LEDVGRGIYDTLGNLKDLGFEYIMVLNDGK 231
Cdd:PRK07328 233 PEEVGFGFAEALALLKEVGYTETVVFRARK 262
|
|
| PHP |
pfam02811 |
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ... |
3-167 |
7.55e-20 |
|
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative phosphoesterase domain.
Pssm-ID: 460705 [Multi-domain] Cd Length: 171 Bit Score: 83.36 E-value: 7.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 3 DYHIHSNFS-PDSNSSVEDIVKYAREKNLKII-ITDHYEAvekdhnfkFDVKSYKEAMKKYGL--LVGVEFGWDGKSKID 78
Cdd:pfam02811 1 HLHVHSEYSlLDGAARIEELVKRAKELGMPAIaITDHGNL--------FGAVEFYKAAKKAGIkpIIGCEVYVAPGSREE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 79 I---DLKEFDFVILSYH-------------AYKEYDDIQKMYENYLKDLYNIIEVVndFHVLGHLDFPRRFVKNNEPFSK 142
Cdd:pfam02811 73 TeklLAKYFDLVLLAVHevgyknliklssrAYLEGFKPRIDKELLEEYFEGLIALS--GCVLGHLDLILLAPGDYEEAEE 150
|
170 180
....*....|....*....|....*
gi 490202520 143 klypLISEIFKKIIKEGKILEVNTS 167
Cdd:pfam02811 151 ----LAEEYLEIFGEDGFYLEINTH 171
|
|
| YciV |
COG0613 |
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ... |
1-204 |
1.20e-14 |
|
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and metabolism];
Pssm-ID: 440378 [Multi-domain] Cd Length: 188 Bit Score: 69.55 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 1 MIDYHIHSNFSpDSNSSVEDIVKYAREKNLKII-ITDHyeavekdhnfkFDVKSYKEAM---KKYGLLV--GVEF--GWD 72
Cdd:COG0613 3 KIDLHVHTTAS-DGSLSPEELVARAKAAGLDVLaITDH-----------DTVAGYEEAAeaaKELGLLVipGVEIstRWE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 73 GKSK------IDIDLKEFDFVILSYHAYKEYDDIqkmyenylkDLYNIIEVVND---FHVLGHldfprrfvknnePFSKK 143
Cdd:COG0613 71 GREVhilgygIDPEDPALEALLGIPVEKAEREWL---------SLEEAIDLIREaggVAVLAH------------PFRYK 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490202520 144 LYPLISEIFKKIIKEG-KILEVntsaIYRYGEPNPSYDILKLYRDLgGKYVTIGSDAHRLED 204
Cdd:COG0613 130 RGRWLDDLLEELADAGlDGIEV----YNGRHSPEDNERAAELAEEY-GLLATGGSDAHGPEK 186
|
|
| PRK09248 |
PRK09248 |
putative hydrolase; Validated |
2-207 |
2.31e-13 |
|
putative hydrolase; Validated
Pssm-ID: 236429 [Multi-domain] Cd Length: 246 Bit Score: 67.17 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 2 IDYHIHSNFSPDSNSSVEDIVKYAREKNLKII-ITDHYEAVeKD--HNFKF-DVKSYKEAMKKYGLLVGVEFG-WDGKSK 76
Cdd:PRK09248 5 VDTHTHTIASGHAYSTLHENAAEAKQKGLKLFaITDHGPDM-PGapHYWHFgNLRVLPRKVDGVGILRGIEANiKNYDGE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 77 IDID---LKEFDFVILSYHA--YkEYDDIqkmyENYLKDLYNIIEvvNDF-HVLGHLDFPRrfvknnepfskklYPL-IS 149
Cdd:PRK09248 84 IDLPgdmLKKLDIVIAGFHEpvF-APGDK----ETNTQALINAIK--NGRvDIIGHPGNPK-------------YPIdIE 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490202520 150 EIFKKIIKEGKILEVNTSAIY--RYG-EPNpSYDILKLYRDLGGkYVTIGSDAHRLEDVGR 207
Cdd:PRK09248 144 AVVKAAKEHNVALEINNSSFGhsRKGsEDN-CRAIAALCKKAGV-WVALGSDAHIAFDIGN 202
|
|
| PRK08123 |
PRK08123 |
histidinol-phosphatase HisJ; |
3-213 |
2.03e-12 |
|
histidinol-phosphatase HisJ;
Pssm-ID: 236155 [Multi-domain] Cd Length: 270 Bit Score: 64.93 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 3 DYHIHSNFSP-DSNSSVEDIVKYAREKNLK-IIITDHY--------EAVEKDHNFKF-DVKSYKEAM----KKYgllvgv 67
Cdd:PRK08123 5 DGHTHTPFCPhGSKDDLEAYIERAIELGFTeITFTEHAplppgfidPTPRQDSAMAIeQLERYLKELnelkKKY------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 68 efgwdgKSKIDI--------------DLKEF--------DFVILSYH--------------------AYKEYDDIQKMYE 105
Cdd:PRK08123 79 ------AGQIDIriglevdyiegyeeETRAFlneygpllDDSILSVHflkgdgeyycidyspetfaeFVDLLGSIEAVYE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 106 NYLKDLYNIIEVVNDFHV---LGHLDFPRRFVKN-NEPFSKKLYPLISEIFKKIIKEGKILEVNTSAIYR--YGEPNPSY 179
Cdd:PRK08123 153 AYYETVLQSIEADLGPYKpkrIGHITLVRKFQKLfPPDFDEKNKELIEDILALIKKRGYELDFNTAGLRKpyCGEPYPPG 232
|
250 260 270
....*....|....*....|....*....|....
gi 490202520 180 DILKLYRDLGGKYVtIGSDAHRLEDVGRGiYDTL 213
Cdd:PRK08123 233 EIITLAKKLGIPLV-YGSDAHSAADVGRG-YDTI 264
|
|
| PHP_HisPPase_Ycdx_like |
cd07437 |
Polymerase and Histidinol Phosphatase domain of Ycdx like; PHP Ycdx-like is a stand alone PHP ... |
2-207 |
3.13e-12 |
|
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: 64.00 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 2 IDYHIHSNFSPDSNSSVEDIVKYAREKNLKII-ITDHYEAVEkD--HNFKFdvKSYKEAMKK-YG--LLVGVEFGW-DGK 74
Cdd:cd07437 3 ADLHTHTIASGHAYSTIEEMARAAAEKGLKLLgITDHGPAMP-GapHPWYF--GNLKVIPREiYGvrILRGVEANIiDYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 75 SKIDID---LKEFDFVILSYHAyKEYDDIQKmyENYLKDLYNIIEvvNDF-HVLGHLDFPRrfvknnepfskklYPL-IS 149
Cdd:cd07437 80 GNLDLPervLKRLDYVIASLHE-PCFAPGTK--EENTRAYINAME--NPYvDIIGHPGNPR-------------YPIdYE 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490202520 150 EIFKKIIKEGKILEVNTS--AIYRYG-EPNpSYDILKLYRDLGGKyVTIGSDAHRLEDVGR 207
Cdd:cd07437 142 AVVKAAKEYNVLLEINNSslSPSRKGsREN-CREIAELCKKYGVP-VIVGSDAHIAYDIGN 200
|
|
| PHP_HisPPase_AMP |
cd07438 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) ... |
2-75 |
3.02e-09 |
|
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: 54.32 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 2 IDYHIHSNFSpDSNSSVEDIVKYAREKNLKII-ITDHyeavekdhnfkfD-VKSYKEAM---KKYGLLV--GVEFG--WD 72
Cdd:cd07438 1 IDLHTHSTAS-DGTLSPEELVELAKEAGLKVLaITDH------------DtVAGLEEALaaaKELGIELipGVEISteYE 67
|
...
gi 490202520 73 GKS 75
Cdd:cd07438 68 GRE 70
|
|
| PHP_PolX |
cd07436 |
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal ... |
3-204 |
5.14e-09 |
|
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: 54.73 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 3 DYHIHSNFSpDSNSSVEDIVKYAREKNLK-IIITDHY-----------EAVEKDHNfkfDVKSYKEAMKKYGLLVGVEfg 70
Cdd:cd07436 8 DLHVHTTWS-DGRNSIEEMAEAARALGYEyIAITDHSkslrvanglseERLREQIE---EIDALNEKLPGIRILKGIE-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 71 wdgkskIDID-----------LKEFDFVILSYHaYKEYDDIQKMYENYLKDLYNiiEVVndfHVLGHldfPR-RFVKNNE 138
Cdd:cd07436 82 ------VDILpdgsldypdevLAELDVVVASVH-SGFNQSEEEMTERLLKAIEN--PHV---DILGH---PTgRLLGRRE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 139 PfskklYPL-ISEIFKKIIKEGKILEVNTSaiyrygePN---PSYDILKLYRDLGGKYVtIGSDAHRLED 204
Cdd:cd07436 147 G-----YEVdMERVIEAAAETGTALEINAN-------PDrldLDDRHARRAKEAGVKIA-INTDAHSTDG 203
|
|
| POLIIIAc |
smart00481 |
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ... |
3-69 |
1.27e-08 |
|
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: 50.34 E-value: 1.27e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490202520 3 DYHIHSNFSP-DSNSSVEDIVKYAREKNLKII-ITDHyeavekdHNFKFDVKSYKeAMKKYGL--LVGVEF 69
Cdd:smart00481 1 DLHVHSDYSLlDGALSPEELVKRAKELGLKAIaITDH-------GNLFGAVEFYK-AAKKAGIkpIIGLEA 63
|
|
| PRK06740 |
PRK06740 |
histidinol phosphate phosphatase domain-containing protein; |
40-237 |
1.48e-08 |
|
histidinol phosphate phosphatase domain-containing protein;
Pssm-ID: 180677 [Multi-domain] Cd Length: 331 Bit Score: 53.99 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 40 AVEKDHNFKFDVKSYKEAMKKYG--LLVGVE----FGWDGKSKIDIDLKEFDFVILSYH-------------AYKEYDDI 100
Cdd:PRK06740 117 RVASLDDFTKAIEEAKERWSKRGvtLKLGIEadyfIGGEQELQSLLALGDFDYVIGSVHflngwgfdnpdtkEYFEEHDL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 101 QKMYENYLKDLYNIIEVvNDFHVLGHLDFPRRFvkNNEPFSKKLYPLISEIFKKIIKEGKILEVNTSAIYRY--GEPNPS 178
Cdd:PRK06740 197 YALYDTFFKTVECAIRS-ELFDIIAHLDNIKVF--NYRLDENEQLSYYKEIARALVETNTATEINAGLYYRYpvREMCPS 273
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490202520 179 YDILKLYRDLGGKYvTIGSDAHRLEDVGRGIYDTLGNLKDLGFEYIMVLNDGKWDMEKI 237
Cdd:PRK06740 274 PLFLQVLAKHEVPI-TLSSDAHYPNDLGKYVEENVKTLRNHGVTSLATFTKRVRTMRLL 331
|
|
| PHP |
cd07309 |
Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2 ... |
2-69 |
5.88e-05 |
|
Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. PHP in polymerases has trinuclear zinc/magnesium dependent proofreading activity. It has also been shown that the PHP domain functions in DNA repair. The PHP structures have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.
Pssm-ID: 213985 [Multi-domain] Cd Length: 88 Bit Score: 40.49 E-value: 5.88e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490202520 2 IDYHIHSNFSPDSNSSVEDIVKYAREKNLKII-ITDHYEAV-EKDHNFKFDVKSYKEAmKKYGLLV--GVEF 69
Cdd:cd07309 1 VDLHTHTVFSDGDHAKLTELVDKAKELGPDALaITDHGNLRgLAEFNTAGK*NHIKAA-EAAGIKIiiGSEV 71
|
|
| PHP_PolIIIA |
cd07431 |
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III; ... |
5-89 |
1.43e-04 |
|
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III; PolIIIAs that contain an N-terminal PHP domain have been classified into four basic groups based on genome composition, phylogenetic, and domain structural analysis: polC, dnaE1, dnaE2, and dnaE3. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. DNA polymerase III holoenzyme is one of the five eubacterial DNA polymerases that is responsible for the replication of the DNA duplex. The alpha subunit of DNA polymerase III core enzyme catalyzes the reaction for polymerizing both DNA strands. The PolIIIA PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination, and like other PHP structures, exhibits a distorted (beta/alpha) 7 barrel and coordinates up to 3 metals. Initially, it was proposed that PHP region might be involved in pyrophosphate hydrolysis, but such activity has not been found. It has been shown that the PHP domain of PolIIIA has a trinuclear metal complex and is capable of proofreading activity.
Pssm-ID: 213986 [Multi-domain] Cd Length: 179 Bit Score: 41.42 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 5 HIHSNFSP-DSNSSVEDIVKYAREKNLK-IIITDH---YEAVEkdhnFkfdvksYKEAmKKYGL--LVGVEFGwdgkskI 77
Cdd:cd07431 4 HVHSSYSLlDSAIRPEDLVARAKELGYSaLALTDRnvlYGAVR----F------YKAC-KKAGIkpIIGLELT------V 66
|
90
....*....|..
gi 490202520 78 DIDLKEFDFVIL 89
Cdd:cd07431 67 EGDGEPYPLLLL 78
|
|
| DnaE |
COG0587 |
DNA polymerase III, alpha subunit [Replication, recombination and repair]; |
5-69 |
1.82e-04 |
|
DNA polymerase III, alpha subunit [Replication, recombination and repair];
Pssm-ID: 440352 [Multi-domain] Cd Length: 1050 Bit Score: 42.36 E-value: 1.82e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490202520 5 HIHSNFSP-DSNSSVEDIVKYAREKNLK-IIITDH---YEAVEkdhnFkfdvksYKEAmKKYGL--LVGVEF 69
Cdd:COG0587 9 HVHSEYSLlDGASRPEELVARAAELGMPaLAITDHgnlFGAVR----F------YKAA-KKAGIkpIIGCEL 69
|
|
| PRK08392 |
PRK08392 |
hypothetical protein; Provisional |
2-207 |
2.27e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 169423 [Multi-domain] Cd Length: 215 Bit Score: 40.92 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 2 IDYHIHSNFSpDSNSSVEDIVKYAREKNLKII-ITDH--YEAVEKDHNFKFDVKSYKEAmKKYGLLVGVEFGW--DGKSK 76
Cdd:PRK08392 1 MDLHTHTVYS-DGIGSVRDNIAEAERKGLRLVgISDHihYFTPSKFNAYINEIRQWGEE-SEIVVLAGIEANItpNGVDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490202520 77 IDIDLKEFDFVILSYHAYKEYDDIQkMYENYLKdLYNIIEVVNdfhVLGHLDfprrfvkNNEPFSKklYPLISEIfKKII 156
Cdd:PRK08392 79 TDDFAKKLDYVIASVHEWFGRPEHH-EYIELVK-LALMDENVD---IIGHFG-------NSFPYIG--YPSEEEL-KEIL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490202520 157 ----KEGKILEVntSAIYRYgepnPSYDILKLYRDLGGKyVTIGSDAHRLEDVGR 207
Cdd:PRK08392 144 dlaeAYGKAFEI--SSRYRV----PDLEFIRECIKRGIK-LTFASDAHRPEDVGN 191
|
|
| PRK06749 |
PRK06749 |
replicative DNA helicase; Provisional |
27-89 |
2.23e-03 |
|
replicative DNA helicase; Provisional
Pssm-ID: 168658 [Multi-domain] Cd Length: 428 Bit Score: 38.78 E-value: 2.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490202520 27 EKNLKII---ITDHYEAVEKDHNFKFDVKS-----YKEAMKKYGLLVGVEFGWDGKSKIDIDLKEFDFVIL 89
Cdd:PRK06749 121 EKSEKIIgetITALCELEEKDCVCEFDLKDalvdlYEELHQDAKEITGIETGYTSLNKMTCGLQEGDFVVL 191
|
|
| |
