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Conserved domains on  [gi|215704249|dbj|BAG93089|]
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unnamed protein product [Oryza sativa Japonica Group]

Protein Classification

PLN02954 family protein( domain architecture ID 10010943)

PLN02954 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02954 PLN02954
phosphoserine phosphatase
 73-296 2.47e-164

phosphoserine phosphatase


:

Pssm-ID: 215514 [Multi-domain]  Cd Length: 224  Bit Score: 455.31  E-value: 2.47e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  73 PSKGVLETWCNADAVCFDVDSTVCLDEGIDELADFCGAGKAVAEWTAKAMTGTVPFEEALAARLSLIKPYLSQVDDCLVK 152
Cdd:PLN02954   1 PSKDVLELWRSADAVCFDVDSTVCVDEGIDELAEFCGAGEAVAEWTAKAMGGSVPFEEALAARLSLFKPSLSQVEEFLEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249 153 RPPRISPGIADLIKKLKANNTDVFLVSGGFRQMIKPVASELGIPPENIIANQLLFGTSGEYAGFDPTEPTSRSGGKALAV 232
Cdd:PLN02954  81 RPPRLSPGIPELVKKLRARGTDVYLVSGGFRQMIAPVAAILGIPPENIFANQILFGDSGEYAGFDENEPTSRSGGKAEAV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215704249 233 QQIRQNHGYKTLVMIGDGATDLEARQPGGADLFICYAGVQMREAVAAKADWVVIDFQELISELP 296
Cdd:PLN02954 161 QHIKKKHGYKTMVMIGDGATDLEARKPGGADLFIGYGGVQVREAVAAKADWFVTDFQDLIEVLD 224
 
Name Accession Description Interval E-value
PLN02954 PLN02954
phosphoserine phosphatase
 73-296 2.47e-164

phosphoserine phosphatase


Pssm-ID: 215514 [Multi-domain]  Cd Length: 224  Bit Score: 455.31  E-value: 2.47e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  73 PSKGVLETWCNADAVCFDVDSTVCLDEGIDELADFCGAGKAVAEWTAKAMTGTVPFEEALAARLSLIKPYLSQVDDCLVK 152
Cdd:PLN02954   1 PSKDVLELWRSADAVCFDVDSTVCVDEGIDELAEFCGAGEAVAEWTAKAMGGSVPFEEALAARLSLFKPSLSQVEEFLEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249 153 RPPRISPGIADLIKKLKANNTDVFLVSGGFRQMIKPVASELGIPPENIIANQLLFGTSGEYAGFDPTEPTSRSGGKALAV 232
Cdd:PLN02954  81 RPPRLSPGIPELVKKLRARGTDVYLVSGGFRQMIAPVAAILGIPPENIFANQILFGDSGEYAGFDENEPTSRSGGKAEAV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215704249 233 QQIRQNHGYKTLVMIGDGATDLEARQPGGADLFICYAGVQMREAVAAKADWVVIDFQELISELP 296
Cdd:PLN02954 161 QHIKKKHGYKTMVMIGDGATDLEARKPGGADLFIGYGGVQVREAVAAKADWFVTDFQDLIEVLD 224
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 85-288 3.18e-114

phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319801 [Multi-domain]  Cd Length: 202  Bit Score: 327.70  E-value: 3.18e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  85 DAVCFDVDSTVCLDEGIDELADFCGAGKAVAEWTAKAMTGTVPFEEALAARLSLIKPYLSQVDDCLVKRPPRISPGIADL 164
Cdd:cd04309    1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFRDALRKRLAIINPTKEQVDEFLEEHPPRLTPGVEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249 165 IKKLKANNTDVFLVSGGFRQMIKPVASELGIPPENIIANQLLFGTSGEYAGFDPTEPTSRSGGKALAVQQIRQNHGYKTL 244
Cdd:cd04309   81 VSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSGGKAKVIEQLKEKHHYKRV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 215704249 245 VMIGDGATDLEARQPggADLFICYAGVQMREAVAAKADWVVIDF 288
Cdd:cd04309  161 IMIGDGATDLEACPP--ADAFIGFGGNVIREKVKARADWYVTDF 202
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 84-296 2.23e-43

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 147.50  E-value: 2.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249   84 ADAVCFDVDSTVCLDEGIDELADFCGAGKAVAEWTAKAMTGTVPFEEALAARLSLIKPylSQVDDCL-VKRPPRISPGIA 162
Cdd:TIGR00338  14 KKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGELDFKASLRERVALLKG--LPVELLKeVRENLPLTEGAE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  163 DLIKKLKANNTDVFLVSGGFRQMIKPVASELGIPPenIIANQLLFgTSGEYAGFDPTEPT-SRSGGKALAVQQIRQNHGY 241
Cdd:TIGR00338  92 ELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDA--AFANRLEV-EDGKLTGLVEGPIVdASYKGKTLLILLRKEGISP 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 215704249  242 KTLVMIGDGATDLEARQPggADLFICYAGvqmREAVAAKADwVVIDFQELISELP 296
Cdd:TIGR00338 169 ENTVAVGDGANDLSMIKA--AGLGIAFNA---KPKLQQKAD-ICINKKDLTDILP 217
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 86-289 1.77e-39

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 137.66  E-value: 1.77e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  86 AVCFDVDSTVCLDEGIDELADFCGA---------GKAVAEWTAKAMTGTVPFEEALAARLSLIKPY----LSQVDDCLVK 152
Cdd:COG0560    5 LAVFDLDGTLIAGESIDELARFLGRrglvdrrevLEEVAAITERAMAGELDFEESLRFRVALLAGLpeeeLEELAERLFE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249 153 RPPRISPGIADLIKKLKANNTDVFLVSGGFRQMIKPVASELGIPpeNIIANQLLFgTSGEYAGfDPTEPTSRSGGKALAV 232
Cdd:COG0560   85 EVPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGID--HVIANELEV-EDGRLTG-EVVGPIVDGEGKAEAL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215704249 233 QQIRQNHGY--KTLVMIGDGATD---LEArqpggADLFICY-AGVQMREAVAAKADWVVIDFQ 289
Cdd:COG0560  161 RELAAELGIdlEQSYAYGDSANDlpmLEA-----AGLPVAVnPDPALREAADRERGWPVLDLL 218
HAD pfam12710
haloacid dehalogenase-like hydrolase;
87-256 1.26e-14

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 70.64  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249   87 VCFDVDSTVCLDEGIDELADFCGAGKAVAEWTA---------KAMTGTVPFEEALAARLSLIKPYLSQVDD-----CLVK 152
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRAllvllllalLRLLGRLSRAGARELLRALLAGLPEEDAAelerfVAEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  153 RPPRISPGIADLIKKLKANNTDVFLVSGGFRQMIKPVASELGIppENIIANQLLFGTSGEYAGFDPTEPTSRSGGKALAV 232
Cdd:pfam12710  81 ALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGF--DEVLATELEVDDGRFTGELRLIGPPCAGEGKVRRL 158

                         170       180
                  ....*....|....*....|....*...
gi 215704249  233 QQIRQNHGYK----TLVMIGDGATDLEA 256
Cdd:pfam12710 159 RAWLAARGLGldlaDSVAYGDSPSDLPM 186
 
Name Accession Description Interval E-value
PLN02954 PLN02954
phosphoserine phosphatase
 73-296 2.47e-164

phosphoserine phosphatase


Pssm-ID: 215514 [Multi-domain]  Cd Length: 224  Bit Score: 455.31  E-value: 2.47e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  73 PSKGVLETWCNADAVCFDVDSTVCLDEGIDELADFCGAGKAVAEWTAKAMTGTVPFEEALAARLSLIKPYLSQVDDCLVK 152
Cdd:PLN02954   1 PSKDVLELWRSADAVCFDVDSTVCVDEGIDELAEFCGAGEAVAEWTAKAMGGSVPFEEALAARLSLFKPSLSQVEEFLEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249 153 RPPRISPGIADLIKKLKANNTDVFLVSGGFRQMIKPVASELGIPPENIIANQLLFGTSGEYAGFDPTEPTSRSGGKALAV 232
Cdd:PLN02954  81 RPPRLSPGIPELVKKLRARGTDVYLVSGGFRQMIAPVAAILGIPPENIFANQILFGDSGEYAGFDENEPTSRSGGKAEAV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215704249 233 QQIRQNHGYKTLVMIGDGATDLEARQPGGADLFICYAGVQMREAVAAKADWVVIDFQELISELP 296
Cdd:PLN02954 161 QHIKKKHGYKTMVMIGDGATDLEARKPGGADLFIGYGGVQVREAVAAKADWFVTDFQDLIEVLD 224
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 85-288 3.18e-114

phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319801 [Multi-domain]  Cd Length: 202  Bit Score: 327.70  E-value: 3.18e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  85 DAVCFDVDSTVCLDEGIDELADFCGAGKAVAEWTAKAMTGTVPFEEALAARLSLIKPYLSQVDDCLVKRPPRISPGIADL 164
Cdd:cd04309    1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFRDALRKRLAIINPTKEQVDEFLEEHPPRLTPGVEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249 165 IKKLKANNTDVFLVSGGFRQMIKPVASELGIPPENIIANQLLFGTSGEYAGFDPTEPTSRSGGKALAVQQIRQNHGYKTL 244
Cdd:cd04309   81 VSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSGGKAKVIEQLKEKHHYKRV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 215704249 245 VMIGDGATDLEARQPggADLFICYAGVQMREAVAAKADWVVIDF 288
Cdd:cd04309  161 IMIGDGATDLEACPP--ADAFIGFGGNVIREKVKARADWYVTDF 202
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 84-296 2.23e-43

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 147.50  E-value: 2.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249   84 ADAVCFDVDSTVCLDEGIDELADFCGAGKAVAEWTAKAMTGTVPFEEALAARLSLIKPylSQVDDCL-VKRPPRISPGIA 162
Cdd:TIGR00338  14 KKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGELDFKASLRERVALLKG--LPVELLKeVRENLPLTEGAE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  163 DLIKKLKANNTDVFLVSGGFRQMIKPVASELGIPPenIIANQLLFgTSGEYAGFDPTEPT-SRSGGKALAVQQIRQNHGY 241
Cdd:TIGR00338  92 ELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDA--AFANRLEV-EDGKLTGLVEGPIVdASYKGKTLLILLRKEGISP 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 215704249  242 KTLVMIGDGATDLEARQPggADLFICYAGvqmREAVAAKADwVVIDFQELISELP 296
Cdd:TIGR00338 169 ENTVAVGDGANDLSMIKA--AGLGIAFNA---KPKLQQKAD-ICINKKDLTDILP 217
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 86-289 1.77e-39

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 137.66  E-value: 1.77e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  86 AVCFDVDSTVCLDEGIDELADFCGA---------GKAVAEWTAKAMTGTVPFEEALAARLSLIKPY----LSQVDDCLVK 152
Cdd:COG0560    5 LAVFDLDGTLIAGESIDELARFLGRrglvdrrevLEEVAAITERAMAGELDFEESLRFRVALLAGLpeeeLEELAERLFE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249 153 RPPRISPGIADLIKKLKANNTDVFLVSGGFRQMIKPVASELGIPpeNIIANQLLFgTSGEYAGfDPTEPTSRSGGKALAV 232
Cdd:COG0560   85 EVPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGID--HVIANELEV-EDGRLTG-EVVGPIVDGEGKAEAL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215704249 233 QQIRQNHGY--KTLVMIGDGATD---LEArqpggADLFICY-AGVQMREAVAAKADWVVIDFQ 289
Cdd:COG0560  161 RELAAELGIdlEQSYAYGDSANDlpmLEA-----AGLPVAVnPDPALREAADRERGWPVLDLL 218
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 87-254 1.27e-28

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 108.02  E-value: 1.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  87 VCFDVDSTVCLDEGIDELADFCGAGKAVAEWTAKAMTGTVPFEEALAARLSLIK--PYlSQVDDCLVKRPprISPGIADL 164
Cdd:cd07500    2 IVFDMDSTLIQQEVIDELAAEAGVGEEVAAITERAMRGELDFEESLRERVALLKglPE-SVLDEVYERLT--LTPGAEEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249 165 IKKLKANNTDVFLVSGGFRQMIKPVASELGIppENIIANQLLFgTSGEYAGfDPTEPTSRSGGKALAVQQIRQNHGYKTL 244
Cdd:cd07500   79 IQTLKAKGYKTAVVSGGFTYFTDRLAEELGL--DYAFANELEI-KDGKLTG-KVLGPIVDAQRKAETLQELAARLGIPLE 154

                        170
                 ....*....|..
gi 215704249 245 --VMIGDGATDL 254
Cdd:cd07500  155 qtVAVGDGANDL 166
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 86-259 2.54e-28

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 107.05  E-value: 2.54e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249   86 AVCFDVDSTVCLDEG-IDELADFCGAGKAVAEWTAKAMTGTVPFEEALAARLSLIKPYLS-QVDDCLVKRPPRISPGIAD 163
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSlIDLLAKLLGTNDEVIELTRLAPSGRISFEDALGRRLALLHRSRSeEVAKEFLARQVALRPGARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  164 LIKKLKANNTDVFLVSGGFRQMIKPVASELGIppENIIANQLLFGTSGEYAGFDPTEPTSRSGGKALAVQQIRQNHGY-- 241
Cdd:TIGR01488  81 LISWLKERGIDTVIVSGGFDFFVEPVAEKLGI--DDVFANRLEFDDNGLLTGPIEGQVNPEGECKGKVLKELLEESKItl 158

                         170
                  ....*....|....*...
gi 215704249  242 KTLVMIGDGATDLEARQP 259
Cdd:TIGR01488 159 KKIIAVGDSVNDLPMLKL 176
HAD_Pase cd07524
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like ...
 90-269 8.57e-16

phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like superfamily; Bacillus subtilis recycles two toxic byproducts of polyamine metabolism, methylthioadenosine and methylthioribose, into methionine by a salvage pathway. The sixth reaction in this pathway is catalyzed by B. subtilis MtnX: the dephosphorylation of 2- hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HKMTP- 1-P) into 1,2-dihydroxy-3-keto-5-methylthiopentene. The hydrolysis of HK-MTP-1-P is a two-step mechanism involving the formation of a transiently phosphorylated aspartyl intermediate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319826 [Multi-domain]  Cd Length: 211  Bit Score: 74.29  E-value: 8.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  90 DVDSTVCLDEGIDELADFCGAGKAVAE-WTAKAMTGTVPFEEALAARLSLIKPylSQVDDCL--VKRPPRISPGIADLIK 166
Cdd:cd07524    5 DFDGTITENDNIIYLMDEFAPPLEEWEaLKEGVLSQTLSFREGVGQMFELLPS--SLKDEIIefLEKTAKIRPGFKEFVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249 167 KLKANNTDVFLVSGGFRQMIKPVASELGIPPENIIANQLLFgtSGEYAGFD-PTEPTSRSG---GKALAVQQIRQNHGYk 242
Cdd:cd07524   83 FCQEHGIPFIIVSGGMDFFIEPLLEGLVIEKIAIYCNGSDF--SGEQIHIDwPHECDCTNGcgcCKSSIIRKYSKPRPF- 159

                        170       180
                 ....*....|....*....|....*...
gi 215704249 243 tLVMIGDGATDLE-ARQpggADLfiCYA 269
Cdd:cd07524  160 -IIVIGDSVTDLEaAKE---ADL--VFA 181
HAD pfam12710
haloacid dehalogenase-like hydrolase;
87-256 1.26e-14

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 70.64  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249   87 VCFDVDSTVCLDEGIDELADFCGAGKAVAEWTA---------KAMTGTVPFEEALAARLSLIKPYLSQVDD-----CLVK 152
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRAllvllllalLRLLGRLSRAGARELLRALLAGLPEEDAAelerfVAEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  153 RPPRISPGIADLIKKLKANNTDVFLVSGGFRQMIKPVASELGIppENIIANQLLFGTSGEYAGFDPTEPTSRSGGKALAV 232
Cdd:pfam12710  81 ALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGF--DEVLATELEVDDGRFTGELRLIGPPCAGEGKVRRL 158

                         170       180
                  ....*....|....*....|....*...
gi 215704249  233 QQIRQNHGYK----TLVMIGDGATDLEA 256
Cdd:pfam12710 159 RAWLAARGLGldlaDSVAYGDSPSDLPM 186
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 85-256 9.48e-13

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 65.69  E-value: 9.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249   85 DAVCFDVDSTVC-----LDEGIDELA-----------DFCGAGKAVAEWTAKAMTGTVPFEEALAARLSLIKPYLSQVDD 148
Cdd:pfam00702   2 KAVVFDLDGTLTdgepvVTEAIAELAsehplakaivaAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGLT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  149 CLVKR---------PPRISPGIADLIKKLKANNTDVFLVSGGFRQMIKPVASELGIPPENIIanqLLFGTSGEYAGFDPT 219
Cdd:pfam00702  82 VVLVEllgvialadELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDV---VISGDDVGVGKPKPE 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 215704249  220 eptsrsgGKALAVQQIRQNHgyKTLVMIGDGATDLEA 256
Cdd:pfam00702 159 -------IYLAALERLGVKP--EEVLMVGDGVNDIPA 186
serB PRK11133
phosphoserine phosphatase; Provisional
 89-254 1.21e-11

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 64.20  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  89 FDVDSTVCLDEGIDELADFCGAGKAVAEWTAKAMTGTVPFEEALAARLSLIK----PYLSQVDDCLvkrPprISPGIADL 164
Cdd:PRK11133 115 MDMDSTAIQIECIDEIAKLAGTGEEVAEVTERAMRGELDFEASLRQRVATLKgadaNILQQVRENL---P--LMPGLTEL 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249 165 IKKLKANNTDVFLVSGGF-------RQMIKPVAselgippenIIANQL------LfgtSGEYAGfdptePTSRSGGKALA 231
Cdd:PRK11133 190 VLKLQALGWKVAIASGGFtyfadylRDKLRLDA---------AVANELeimdgkL---TGNVLG-----DIVDAQYKADT 252

                        170       180
                 ....*....|....*....|....*
gi 215704249 232 VQQIRQNHGYKT--LVMIGDGATDL 254
Cdd:PRK11133 253 LTRLAQEYEIPLaqTVAIGDGANDL 277
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
85-295 1.63e-08

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 53.78  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  85 DAVCFD-----VDSTVCLDEGIDELADFCGaGKAVAEWTAKAMTGtVPFEEALAARLSLIKP---------YLSQVDDCL 150
Cdd:COG0546    2 KLVLFDldgtlVDSAPDIAAALNEALAELG-LPPLDLEELRALIG-LGLRELLRRLLGEDPDeeleellarFRELYEEEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249 151 VKRPpRISPGIADLIKKLKANNTDVFLVSGGFRQMIKPVASELGIPPeniianqlLFGTsgeYAGFDPTEPtsrSGGKAL 230
Cdd:COG0546   80 LDET-RLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDD--------YFDA---IVGGDDVPP---AKPKPE 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215704249 231 AVQQIRQNHGYK--TLVMIGDGATDLE-ARQPGGADLFICYaGVQMREAV-AAKADWVVIDFQELISEL 295
Cdd:COG0546  145 PLLEALERLGLDpeEVLMVGDSPHDIEaARAAGVPFIGVTW-GYGSAEELeAAGADYVIDSLAELLALL 212
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 155-255 1.91e-08

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273654 [Multi-domain]  Cd Length: 202  Bit Score: 53.50  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  155 PRISPGIADLIKKLKANNTDVFLVSGGFRQMIKPVASELGIppENIIANQLLFGTSGEYAGfDPTEPTSRSGGKALAVQQ 234
Cdd:TIGR01490  86 SILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGI--DNAIGTRLEESEDGIYTG-NIDGNNCKGEGKVHALAE 162

                          90       100
                  ....*....|....*....|...
gi 215704249  235 I--RQNHGYKTLVMIGDGATDLE 255
Cdd:TIGR01490 163 LlaEEQIDLKDSYAYGDSISDLP 185
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 152-255 1.72e-07

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 50.38  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249 152 KRPPRISPGIADLIKKLKANNTDVFLVSGGFRQMIKPVASELGIppENIIANQLLF---GTSGEYAGfdptePTSRSGGK 228
Cdd:cd02612   80 YILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGI--DNVLGTQLETedgRYTGRIIG-----PPCYGEGK 152

                         90       100
                 ....*....|....*....|....*....
gi 215704249 229 ALAVQQIRQNHG--YKTLVMIGDGATDLE 255
Cdd:cd02612  153 VKRLREWLAEEGidLKDSYAYSDSINDLP 181
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 161-263 3.73e-06

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 44.69  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249 161 IADLIKKLKANNTDVFLVSGGFRQMIKPVASELGIP--PENIIANqllfgtsgeyagfdPTEPTSRSGGKALAVQQIRQN 238
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGdlFDGIIGS--------------DGGGTPKPKPKPLLLLLLKLG 77

                         90       100
                 ....*....|....*....|....*
gi 215704249 239 HGYKTLVMIGDGATDLEARQPGGAD 263
Cdd:cd01427   78 VDPEEVLFVGDSENDIEAARAAGGR 102
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 86-256 5.24e-05

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 42.77  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249   86 AVCFDVDSTVCLDEGIDEladfcgagKAVAEWTAKAMTGTVPFEEALAAR---LSLIKPYLSQVDDCLVKRPPRI----- 157
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIR--------RAFPQTFEEFGLDPASFKALKQAGglaEEEWYRIATSALEELQGRFWSEydaee 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  158 --SPGIADLIKKLKANNTDVFLVSGGFRQMIKpvaselgippeniianqLLFGTSGEYAGFDPTEPTSRSGGK------A 229
Cdd:TIGR01549  73 ayIRGAADLLARLKSAGIKLGIISNGSLRAQK-----------------LLLRLFGLGDYFELILVSDEPGSKpepeifL 135

                         170       180
                  ....*....|....*....|....*..
gi 215704249  230 LAVQQIRQnhgYKTLVMIGDGATDLEA 256
Cdd:TIGR01549 136 AALESLGV---PPEVLHVGDNLNDIEG 159
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
 154-289 1.86e-04

ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large family of trans-membrane transporters acting on charged substances. The distinguishing feature of the family is the formation of a phosphorylated intermediate (aspartyl-phosphate) during the course of the reaction. Another common name for these enzymes is the E1-E2 ATPases based on the two isolable conformations: E1 (unphosphorylated) and E2 (phosphorylated). Generally, P-type ATPases consist of only a single subunit encompassing the ATPase and ion translocation pathway, however, in the case of the potassium (TIGR01497) and sodium/potassium (TIGR01106) varieties, these functions are split between two subunits. Additional small regulatory or stabilizing subunits may also exist in some forms. P-type ATPases are nearly ubiquitous in life and are found in numerous copies in higher organisms (at least 45 in Arabidopsis thaliana, for instance). Phylogenetic analyses have revealed that the P-type ATPase subfamily is divided up into groups based on substrate specificities and this is represented in the various subfamily and equivalog models that have been made: IA (K+) TIGR01497, IB (heavy metals) TIGR01525, IIA1 (SERCA-type Ca++) TIGR01116, IIA2 (PMR1-type Ca++) TIGR01522, IIB (PMCA-type Ca++) TIGR01517, IIC (Na+/K+, H+/K+ antiporters) TIGR01106, IID (fungal-type Na+ and K+) TIGR01523, IIIA (H+) TIGR01647, IIIB (Mg++) TIGR01524, IV (phospholipid, flippase) TIGR01652 and V (unknown specificity) TIGR01657. The crystal structure of one calcium-pumping ATPase and an analysis of the fold of the catalytic domain of the P-type ATPases have been published. These reveal that the catalytic core of these enzymes is a haloacid dehalogenase(HAD)-type aspartate-nucleophile hydrolase. The location of the ATP-binding loop in between the first and second HAD conserved catalytic motifs defines these enzymes as members of subfamily I of the HAD superfamily (see also TIGR01493, TIGR01509, TIGR01549, TIGR01544 and TIGR01545). Based on these classifications, the P-type ATPase _superfamily_ corresponds to the IC subfamily of the HAD superfamily.


Pssm-ID: 273656 [Multi-domain]  Cd Length: 545  Bit Score: 42.69  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  154 PPRisPGIADLIKKLKANNTDVFLVSGGFRQMIKPVASELGIppeniianqllfgtsGEYAGFDPTEptsrsggKALAVQ 233
Cdd:TIGR01494 387 PLR--PDAKETIEALRKAGIKVVMLTGDNVLTAKAIAKELGI---------------DVFARVKPEE-------KAAIVE 442

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 215704249  234 QIRQNhgYKTLVMIGDGATDLEA-RQpggADLficyaGVQMREAVAAK--ADWVVIDFQ 289
Cdd:TIGR01494 443 ALQEK--GRTVAMTGDGVNDAPAlKK---ADV-----GIAMGSGDVAKaaADIVLLDDD 491
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 85-195 1.36e-03

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 39.24  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249  85 DAVCFDVDSTVC-----LDEGIDELADFCG----AGKAVAEWTAKAM-------TGTVPFEEALAARL---------SLI 139
Cdd:COG1011    2 KAVLFDLDGTLLdfdpvIAEALRALAERLGlldeAEELAEAYRAIEYalwrryeRGEITFAELLRRLLeelgldlaeELA 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 215704249 140 KPYLSQVDDCLvkrppRISPGIADLIKKLKANNTDVFLVSGGFRQMIKPVASELGI 195
Cdd:COG1011   82 EAFLAALPELV-----EPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGL 132
P-type_ATPase_Cu-like cd07552
P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+) ...
 156-253 6.22e-03

P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+)-ATPase; Archaeoglobus fulgidus CopB transports Cu(2+) from the cytoplasm to the exterior of the cell using ATP as energy source, it transports preferentially Cu(2+) over Cu(+), it is activated by Cu(2+) with high affinity and partially by Cu(+) and Ag(+). This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319850 [Multi-domain]  Cd Length: 632  Bit Score: 38.05  E-value: 6.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215704249 156 RISPGIADLIKKLKANNTDVFLVSGGFRQMIKPVASELGIPpeniianqllfgtsgEY-AGFDPTEptsrsggKALAVQQ 234
Cdd:cd07552  455 EIKPESKEAIRALKAQGITPVMLTGDNEEVAQAVAEELGID---------------EYfAEVLPED-------KAKKVKE 512

                         90
                 ....*....|....*....
gi 215704249 235 IrQNHGYKTlVMIGDGATD 253
Cdd:cd07552  513 L-QAEGKKV-AMVGDGVND 529
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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