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Conserved domains on  [gi|42571535|ref|NP_973858|]
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3-phosphoserine phosphatase [Arabidopsis thaliana]

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
 72-295 2.25e-166

phosphoserine phosphatase


:

Pssm-ID: 215514 [Multi-domain]  Cd Length: 224  Bit Score: 460.31  E-value: 2.25e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535   72 PSKEILDLWRSVEAVCFDVDSTVCVDEGIDELAEFCGAGKAVAEWTARAMGGSVPFEEALAARLSLFKPSLSKVEEYLDK 151
Cdd:PLN02954   1 PSKDVLELWRSADAVCFDVDSTVCVDEGIDELAEFCGAGEAVAEWTAKAMGGSVPFEEALAARLSLFKPSLSQVEEFLEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535  152 RPPRLSPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIPRENIFANNLLFGNSGEFLGFDENEPTSRSGGKAKAV 231
Cdd:PLN02954  81 RPPRLSPGIPELVKKLRARGTDVYLVSGGFRQMIAPVAAILGIPPENIFANQILFGDSGEYAGFDENEPTSRSGGKAEAV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571535  232 QQIRKGRLYKTMAMIGDGATDLEARKPGGADLFICYAGVQLREAVAANADWLIFKFESLINSLD 295
Cdd:PLN02954 161 QHIKKKHGYKTMVMIGDGATDLEARKPGGADLFIGYGGVQVREAVAAKADWFVTDFQDLIEVLD 224
 
Name Accession Description Interval E-value
PLN02954 PLN02954
phosphoserine phosphatase
 72-295 2.25e-166

phosphoserine phosphatase


Pssm-ID: 215514 [Multi-domain]  Cd Length: 224  Bit Score: 460.31  E-value: 2.25e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535   72 PSKEILDLWRSVEAVCFDVDSTVCVDEGIDELAEFCGAGKAVAEWTARAMGGSVPFEEALAARLSLFKPSLSKVEEYLDK 151
Cdd:PLN02954   1 PSKDVLELWRSADAVCFDVDSTVCVDEGIDELAEFCGAGEAVAEWTAKAMGGSVPFEEALAARLSLFKPSLSQVEEFLEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535  152 RPPRLSPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIPRENIFANNLLFGNSGEFLGFDENEPTSRSGGKAKAV 231
Cdd:PLN02954  81 RPPRLSPGIPELVKKLRARGTDVYLVSGGFRQMIAPVAAILGIPPENIFANQILFGDSGEYAGFDENEPTSRSGGKAEAV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571535  232 QQIRKGRLYKTMAMIGDGATDLEARKPGGADLFICYAGVQLREAVAANADWLIFKFESLINSLD 295
Cdd:PLN02954 161 QHIKKKHGYKTMVMIGDGATDLEARKPGGADLFIGYGGVQVREAVAAKADWFVTDFQDLIEVLD 224
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 84-287 5.60e-122

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: 347.35  E-value: 5.60e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535  84 EAVCFDVDSTVCVDEGIDELAEFCGAGKAVAEWTARAMGGSVPFEEALAARLSLFKPSLSKVEEYLDKRPPRLSPGIEEL 163
Cdd:cd04309   1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFRDALRKRLAIINPTKEQVDEFLEEHPPRLTPGVEEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535 164 VKKLRANNIDVYLISGGFRQMINPVASILGIPRENIFANNLLFGNSGEFLGFDENEPTSRSGGKAKAVQQIRKGRLYKTM 243
Cdd:cd04309  81 VSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSGGKAKVIEQLKEKHHYKRV 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 42571535 244 AMIGDGATDLEARKPggADLFICYAGVQLREAVAANADWLIFKF 287
Cdd:cd04309 161 IMIGDGATDLEACPP--ADAFIGFGGNVIREKVKARADWYVTDF 202
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 81-291 8.60e-45

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: 151.35  E-value: 8.60e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535    81 RSVEAVCFDVDSTVCVDEGIDELAEFCGAGKAVAEWTARAMGGSVPFEEALAARLSLFKPSLSKVEEYLDKRPPrLSPGI 160
Cdd:TIGR00338  12 RSKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGELDFKASLRERVALLKGLPVELLKEVRENLP-LTEGA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535   161 EELVKKLRANNIDVYLISGGFRQMINPVASILGIPRenIFANNLLFGNsGEFLGFDENEPTSRSgGKAKAVQQIRK--GR 238
Cdd:TIGR00338  91 EELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDA--AFANRLEVED-GKLTGLVEGPIVDAS-YKGKTLLILLRkeGI 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 42571535   239 LYKTMAMIGDGATDLEARKPggADLFICYAGVQLREAVAANA--DWLIFKFESLI 291
Cdd:TIGR00338 167 SPENTVAVGDGANDLSMIKA--AGLGIAFNAKPKLQQKADICinKKDLTDILPLL 219
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 85-284 1.08e-36

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: 130.34  E-value: 1.08e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535  85 AVCFDVDSTVCVDEGIDELAEFCGA---------GKAVAEWTARAMGGSVPFEEALAARLSLFKP-SLSKVEEYLD---K 151
Cdd:COG0560   5 LAVFDLDGTLIAGESIDELARFLGRrglvdrrevLEEVAAITERAMAGELDFEESLRFRVALLAGlPEEELEELAErlfE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535 152 RPPRLSPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIPreNIFANNLLFGNsGEFLGFDENEPTSRsGGKAKAV 231
Cdd:COG0560  85 EVPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGID--HVIANELEVED-GRLTGEVVGPIVDG-EGKAEAL 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535 232 QQIRKGRLY---KTMAmIGDGATD---LEArkpggADLFICY-AGVQLREAVAANADWLI 284
Cdd:COG0560 161 RELAAELGIdleQSYA-YGDSANDlpmLEA-----AGLPVAVnPDPALREAADRERGWPV 214
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 83-260 5.66e-16

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: 74.54  E-value: 5.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535    83 VEAVCFDVDSTVC-----VDEGIDELA-----------EFCGAGKAVAEWTARAMGGSVPFEEALAARLSLFKPSLSKVE 146
Cdd:pfam00702   1 IKAVVFDLDGTLTdgepvVTEAIAELAsehplakaivaAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535   147 EYLDKR---------PPRLSPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIPRENIFAnnllfgNSGEFLGFDE 217
Cdd:pfam00702  81 TVVLVEllgvialadELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVV------ISGDDVGVGK 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 42571535   218 NEPTsrsgGKAKAVQQIrkGRLYKTMAMIGDGATDLEARKPGG 260
Cdd:pfam00702 155 PKPE----IYLAALERL--GVKPEEVLMVGDGVNDIPAAKAAG 191
 
Name Accession Description Interval E-value
PLN02954 PLN02954
phosphoserine phosphatase
 72-295 2.25e-166

phosphoserine phosphatase


Pssm-ID: 215514 [Multi-domain]  Cd Length: 224  Bit Score: 460.31  E-value: 2.25e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535   72 PSKEILDLWRSVEAVCFDVDSTVCVDEGIDELAEFCGAGKAVAEWTARAMGGSVPFEEALAARLSLFKPSLSKVEEYLDK 151
Cdd:PLN02954   1 PSKDVLELWRSADAVCFDVDSTVCVDEGIDELAEFCGAGEAVAEWTAKAMGGSVPFEEALAARLSLFKPSLSQVEEFLEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535  152 RPPRLSPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIPRENIFANNLLFGNSGEFLGFDENEPTSRSGGKAKAV 231
Cdd:PLN02954  81 RPPRLSPGIPELVKKLRARGTDVYLVSGGFRQMIAPVAAILGIPPENIFANQILFGDSGEYAGFDENEPTSRSGGKAEAV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571535  232 QQIRKGRLYKTMAMIGDGATDLEARKPGGADLFICYAGVQLREAVAANADWLIFKFESLINSLD 295
Cdd:PLN02954 161 QHIKKKHGYKTMVMIGDGATDLEARKPGGADLFIGYGGVQVREAVAAKADWFVTDFQDLIEVLD 224
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 84-287 5.60e-122

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: 347.35  E-value: 5.60e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535  84 EAVCFDVDSTVCVDEGIDELAEFCGAGKAVAEWTARAMGGSVPFEEALAARLSLFKPSLSKVEEYLDKRPPRLSPGIEEL 163
Cdd:cd04309   1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFRDALRKRLAIINPTKEQVDEFLEEHPPRLTPGVEEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535 164 VKKLRANNIDVYLISGGFRQMINPVASILGIPRENIFANNLLFGNSGEFLGFDENEPTSRSGGKAKAVQQIRKGRLYKTM 243
Cdd:cd04309  81 VSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSGGKAKVIEQLKEKHHYKRV 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 42571535 244 AMIGDGATDLEARKPggADLFICYAGVQLREAVAANADWLIFKF 287
Cdd:cd04309 161 IMIGDGATDLEACPP--ADAFIGFGGNVIREKVKARADWYVTDF 202
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 81-291 8.60e-45

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: 151.35  E-value: 8.60e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535    81 RSVEAVCFDVDSTVCVDEGIDELAEFCGAGKAVAEWTARAMGGSVPFEEALAARLSLFKPSLSKVEEYLDKRPPrLSPGI 160
Cdd:TIGR00338  12 RSKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGELDFKASLRERVALLKGLPVELLKEVRENLP-LTEGA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535   161 EELVKKLRANNIDVYLISGGFRQMINPVASILGIPRenIFANNLLFGNsGEFLGFDENEPTSRSgGKAKAVQQIRK--GR 238
Cdd:TIGR00338  91 EELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDA--AFANRLEVED-GKLTGLVEGPIVDAS-YKGKTLLILLRkeGI 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 42571535   239 LYKTMAMIGDGATDLEARKPggADLFICYAGVQLREAVAANA--DWLIFKFESLI 291
Cdd:TIGR00338 167 SPENTVAVGDGANDLSMIKA--AGLGIAFNAKPKLQQKADICinKKDLTDILPLL 219
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 85-284 1.08e-36

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: 130.34  E-value: 1.08e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535  85 AVCFDVDSTVCVDEGIDELAEFCGA---------GKAVAEWTARAMGGSVPFEEALAARLSLFKP-SLSKVEEYLD---K 151
Cdd:COG0560   5 LAVFDLDGTLIAGESIDELARFLGRrglvdrrevLEEVAAITERAMAGELDFEESLRFRVALLAGlPEEELEELAErlfE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535 152 RPPRLSPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIPreNIFANNLLFGNsGEFLGFDENEPTSRsGGKAKAV 231
Cdd:COG0560  85 EVPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGID--HVIANELEVED-GRLTGEVVGPIVDG-EGKAEAL 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535 232 QQIRKGRLY---KTMAmIGDGATD---LEArkpggADLFICY-AGVQLREAVAANADWLI 284
Cdd:COG0560 161 RELAAELGIdleQSYA-YGDSANDlpmLEA-----AGLPVAVnPDPALREAADRERGWPV 214
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 85-258 1.81e-31

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: 115.53  E-value: 1.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535    85 AVCFDVDSTVCVDEG-IDELAEFCGAGKAVAEWTARAMGGSVPFEEALAARLSLFKPSLSK--VEEYLDKRPPrLSPGIE 161
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSlIDLLAKLLGTNDEVIELTRLAPSGRISFEDALGRRLALLHRSRSEevAKEFLARQVA-LRPGAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535   162 ELVKKLRANNIDVYLISGGFRQMINPVASILGIprENIFANNLLFGNSGEFLGFDENEPTSRSGGKAKAVQQI--RKGRL 239
Cdd:TIGR01488  80 ELISWLKERGIDTVIVSGGFDFFVEPVAEKLGI--DDVFANRLEFDDNGLLTGPIEGQVNPEGECKGKVLKELleESKIT 157

                         170
                  ....*....|....*....
gi 42571535   240 YKTMAMIGDGATDLEARKP 258
Cdd:TIGR01488 158 LKKIIAVGDSVNDLPMLKL 176
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 86-253 5.74e-30

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: 111.49  E-value: 5.74e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535  86 VCFDVDSTVCVDEGIDELAEFCGAGKAVAEWTARAMGGSVPFEEALAARLSLFKP-SLSKVEEYLDKRPprLSPGIEELV 164
Cdd:cd07500   2 IVFDMDSTLIQQEVIDELAAEAGVGEEVAAITERAMRGELDFEESLRERVALLKGlPESVLDEVYERLT--LTPGAEELI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535 165 KKLRANNIDVYLISGGFRQMINPVASILGIprENIFANNLLFGN---SGEFLGfdenEPTSRSgGKAKAVQQIRKG---R 238
Cdd:cd07500  80 QTLKAKGYKTAVVSGGFTYFTDRLAEELGL--DYAFANELEIKDgklTGKVLG----PIVDAQ-RKAETLQELAARlgiP 152

                       170
                ....*....|....*
gi 42571535 239 LYKTMAMiGDGATDL 253
Cdd:cd07500 153 LEQTVAV-GDGANDL 166
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 83-260 5.66e-16

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: 74.54  E-value: 5.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535    83 VEAVCFDVDSTVC-----VDEGIDELA-----------EFCGAGKAVAEWTARAMGGSVPFEEALAARLSLFKPSLSKVE 146
Cdd:pfam00702   1 IKAVVFDLDGTLTdgepvVTEAIAELAsehplakaivaAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535   147 EYLDKR---------PPRLSPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIPRENIFAnnllfgNSGEFLGFDE 217
Cdd:pfam00702  81 TVVLVEllgvialadELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVV------ISGDDVGVGK 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 42571535   218 NEPTsrsgGKAKAVQQIrkGRLYKTMAMIGDGATDLEARKPGG 260
Cdd:pfam00702 155 PKPE----IYLAALERL--GVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_Pase cd07524
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like ...
 89-268 6.30e-15

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: 71.98  E-value: 6.30e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535  89 DVDSTVCVDEGIDELAEFCGAGKAVAE-WTARAMGGSVPFEEALAARLSLFkPSLSKVE--EYLDKRPpRLSPGIEELVK 165
Cdd:cd07524   5 DFDGTITENDNIIYLMDEFAPPLEEWEaLKEGVLSQTLSFREGVGQMFELL-PSSLKDEiiEFLEKTA-KIRPGFKEFVA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535 166 KLRANNIDVYLISGGFRQMINPVASILGIPRENIFANNLLFgnSGEFLGFD-ENEPTSRSG-GKAKAVqQIRK-GRLYKT 242
Cdd:cd07524  83 FCQEHGIPFIIVSGGMDFFIEPLLEGLVIEKIAIYCNGSDF--SGEQIHIDwPHECDCTNGcGCCKSS-IIRKySKPRPF 159

                       170       180
                ....*....|....*....|....*.
gi 42571535 243 MAMIGDGATDLEARKPggADLfiCYA 268
Cdd:cd07524 160 IIVIGDSVTDLEAAKE--ADL--VFA 181
serB PRK11133
phosphoserine phosphatase; Provisional
 63-253 2.12e-14

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 72.29  E-value: 2.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535   63 TLGHEGN--IVPSKEILDLwRSVEAVCFDVDSTVCVDEGIDELAEFCGAGKAVAEWTARAMGGSVPFEEALAARLSLFKP 140
Cdd:PRK11133  89 RLAHELGldVAPLGKIPHL-RTPGLLVMDMDSTAIQIECIDEIAKLAGTGEEVAEVTERAMRGELDFEASLRQRVATLKG 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535  141 S----LSKVEEYLdkrPprLSPGIEELVKKLRANNIDVYLISGGF-------RQMINPVAsilgiprenIFANNLLFGN- 208
Cdd:PRK11133 168 AdaniLQQVRENL---P--LMPGLTELVLKLQALGWKVAIASGGFtyfadylRDKLRLDA---------AVANELEIMDg 233

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 42571535  209 --SGEFLGfdenePTSRSGGKAKAVQQIRKG---RLYKTMAmIGDGATDL 253
Cdd:PRK11133 234 klTGNVLG-----DIVDAQYKADTLTRLAQEyeiPLAQTVA-IGDGANDL 277
HAD pfam12710
haloacid dehalogenase-like hydrolase;
86-255 2.25e-14

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 69.87  E-value: 2.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535    86 VCFDVDSTVCVDEGIDELAEFCGAGKAVAEWTA---------RAMGGSVPFEEALAARLSLFKPSLSKVEEYL-----DK 151
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRAllvllllalLRLLGRLSRAGARELLRALLAGLPEEDAAELerfvaEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535   152 RPPRLSPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIprENIFANNLLFGNS---GEFLGFDENeptSRSGGKA 228
Cdd:pfam12710  81 ALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGF--DEVLATELEVDDGrftGELRLIGPP---CAGEGKV 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 42571535   229 KAVQQIRKGRLYKTMAM----IGDGATDLEA 255
Cdd:pfam12710 156 RRLRAWLAARGLGLDLAdsvaYGDSPSDLPM 186
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
85-295 9.54e-08

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 51.47  E-value: 9.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535  85 AVCFD-----VDSTVCVDEGIDELAEFCG------------AGKAVAEWTARAMGGSVP--FEEALAARLSLFKpslskv 145
Cdd:COG0546   3 LVLFDldgtlVDSAPDIAAALNEALAELGlppldleelralIGLGLRELLRRLLGEDPDeeLEELLARFRELYE------ 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535 146 EEYLDKrpPRLSPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIprENIFAnnllfgnsgEFLGFDEnepTSRSG 225
Cdd:COG0546  77 EELLDE--TRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGL--DDYFD---------AIVGGDD---VPPAK 140

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571535 226 GKAKAVQQI--RKGRLYKTMAMIGDGATDLE-ARKPGGADLFICYaGVQLREAV-AANADWLIFKFESLINSLD 295
Cdd:COG0546 141 PKPEPLLEAleRLGLDPEEVLMVGDSPHDIEaARAAGVPFIGVTW-GYGSAEELeAAGADYVIDSLAELLALLA 213
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 145-254 1.76e-07

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: 50.42  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535   145 VEEYLDKR-PPRLSPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIprENIFANNLLFGNSGEFLGFDENEPTsR 223
Cdd:TIGR01490  76 VEEFVNQKiESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGI--DNAIGTRLEESEDGIYTGNIDGNNC-K 152

                          90       100       110
                  ....*....|....*....|....*....|...
gi 42571535   224 SGGKAKAVQQI--RKGRLYKTMAMIGDGATDLE 254
Cdd:TIGR01490 153 GEGKVHALAELlaEEQIDLKDSYAYGDSISDLP 185
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 160-262 3.22e-07

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: 47.78  E-value: 3.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535 160 IEELVKKLRANNIDVYLISGGFRQMINPVASILGIprenifannllfGNSGEFLGFDENEPTSRSGGKAKAVQQIRKGRL 239
Cdd:cd01427  12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGL------------GDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVD 79

                        90       100
                ....*....|....*....|...
gi 42571535 240 YKTMAMIGDGATDLEARKPGGAD 262
Cdd:cd01427  80 PEEVLFVGDSENDIEAARAAGGR 102
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 83-194 1.48e-06

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: 48.10  E-value: 1.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535  83 VEAVCFDVDSTVC-----VDEGIDELAEFCGAGKAVAEWTA-----------RAMGGSVPFEEALAARLSLFKPSLSK-- 144
Cdd:COG1011   1 IKAVLFDLDGTLLdfdpvIAEALRALAERLGLLDEAEELAEayraieyalwrRYERGEITFAELLRRLLEELGLDLAEel 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571535 145 VEEYLD--KRPPRLSPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGI 194
Cdd:COG1011  81 AEAFLAalPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGL 132
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 108-254 4.05e-05

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: 43.45  E-value: 4.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535 108 GAGKAVAEWtaRAMGGSVPFEEALAARLslfkpslskVEEYLdkrPPRLSPGIEELVKKLRANNIDVYLISGGFRQMINP 187
Cdd:cd02612  51 GAGMEALLG--FATAGLAGELAALVEEF---------VEEYI---LRVLYPEARELIAWHKAAGHDVVLISASPEELVAP 116

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571535 188 VASILGIprENIFANNLLFGN---SGEFLGfdenePTSRSGGKAKAVQQIRKGRL--YKTMAMIGDGATDLE 254
Cdd:cd02612 117 IARKLGI--DNVLGTQLETEDgryTGRIIG-----PPCYGEGKVKRLREWLAEEGidLKDSYAYSDSINDLP 181
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
83-194 4.99e-05

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 43.27  E-value: 4.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535  83 VEAVCFDVDSTVcVD---------------EGI----DELAEFCG-AGKAVAEWTARAMGGSVPFEEALAARLSLFkpsl 142
Cdd:COG0637   2 IKAVIFDMDGTL-VDseplharawreafaeLGIdlteEEYRRLMGrSREDILRYLLEEYGLDLPEEELAARKEELY---- 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571535 143 skvEEYLDKRPPRLSPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGI 194
Cdd:COG0637  77 ---RELLAEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGL 125
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 85-255 1.54e-04

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: 41.61  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535    85 AVCFDVDSTVCVDEGIDElaefcgagKAVAEWTARAMGGSVPFEEALAAR-----------LSLFKPSLSKVEEYLDKRP 153
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIR--------RAFPQTFEEFGLDPASFKALKQAGglaeeewyriaTSALEELQGRFWSEYDAEE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535   154 PRLsPGIEELVKKLRANNIDVYLISGGFRQMInpvasilgiprenifanNLLFGNSGEFLGFDENEPTSRSGGK------ 227
Cdd:TIGR01549  73 AYI-RGAADLLARLKSAGIKLGIISNGSLRAQ-----------------KLLLRLFGLGDYFELILVSDEPGSKpepeif 134

                         170       180
                  ....*....|....*....|....*...
gi 42571535   228 AKAVQQIrkgRLYKTMAMIGDGATDLEA 255
Cdd:TIGR01549 135 LAALESL---GVPPEVLHVGDNLNDIEG 159
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
 153-257 1.16e-03

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: 40.38  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535   153 PPRlsPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIPrenifannllfgnsgeflGFDENEPTsrsgGKAKAVQ 232
Cdd:TIGR01494 387 PLR--PDAKETIEALRKAGIKVVMLTGDNVLTAKAIAKELGID------------------VFARVKPE----EKAAIVE 442

                          90       100
                  ....*....|....*....|....*
gi 42571535   233 QIRKgrLYKTMAMIGDGATDLEARK 257
Cdd:TIGR01494 443 ALQE--KGRTVAMTGDGVNDAPALK 465
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
153-249 1.68e-03

Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 39.74  E-value: 1.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535 153 PPRlsPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIprENIFAnNLLfgnsgeflgfdenePtsrsGGKAKAVQ 232
Cdd:COG2217 541 TLR--PEAAEAIAALKALGIRVVMLTGDNERTAEAVARELGI--DEVRA-EVL--------------P----EDKAAAVR 597

                        90
                ....*....|....*..
gi 42571535 233 QIRKGrlYKTMAMIGDG 249
Cdd:COG2217 598 ELQAQ--GKKVAMVGDG 612
P-type_ATPase_Cu-like cd02094
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ...
 158-252 1.95e-03

P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A and ATP7B; The mammalian copper-transporting P-type ATPases, ATP7A and ATP7B are key molecules required for the regulation and maintenance of copper homeostasis. Menkes and Wilson diseases are caused by mutation in ATP7A and ATP7B respectively. This subfamily includes other copper-transporting ATPases such as: Bacillus subtilis CopA , Archeaoglobus fulgidus CopA, and Saccharomyces cerevisiae Ccc2p. 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: 319783 [Multi-domain]  Cd Length: 647  Bit Score: 39.77  E-value: 1.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535 158 PGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIprENIFANNLlfgnsgeflgfdenePtsrsGGKAKAVQQIRKG 237
Cdd:cd02094 471 PDAAEAIEALKKMGIKVVMLTGDNRRTARAIAKELGI--DEVIAEVL---------------P----EDKAEKVKKLQAQ 529

                        90
                ....*....|....*
gi 42571535 238 rlYKTMAMIGDGATD 252
Cdd:cd02094 530 --GKKVAMVGDGIND 542
P-type_ATPase_Cu-like cd07552
P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+) ...
 155-252 3.00e-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: 39.21  E-value: 3.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535 155 RLSPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIPRenIFANNLlfgnsgeflgfdenePTSrsggKAKAVQQI 234
Cdd:cd07552 455 EIKPESKEAIRALKAQGITPVMLTGDNEEVAQAVAEELGIDE--YFAEVL---------------PED----KAKKVKEL 513

                        90
                ....*....|....*...
gi 42571535 235 RKGrlYKTMAMIGDGATD 252
Cdd:cd07552 514 QAE--GKKVAMVGDGVND 529
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 85-178 3.67e-03

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. 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: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 37.71  E-value: 3.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535  85 AVCFDVDStVCVDEGIDE-LAEFCGAGKAVAEWTARAMGGSVPFEEALAARLSL--FKPSLSK----------VEEYLDK 151
Cdd:cd02603   3 AVLFDFGG-VLIDPDPAAaVARFEALTGEPSEFVLDTEGLAGAFLELERGRITEeeFWEELREelgrplsaelFEELVLA 81

                        90       100
                ....*....|....*....|....*..
gi 42571535 152 RPpRLSPGIEELVKKLRANNIDVYLIS 178
Cdd:cd02603  82 AV-DPNPEMLDLLEALRAKGYKVYLLS 107
P-type_ATPase cd07539
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
 153-257 8.65e-03

uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase transporters of unknown function. The P-type ATPases, are 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. They 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. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd2+, and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.


Pssm-ID: 319840 [Multi-domain]  Cd Length: 634  Bit Score: 37.40  E-value: 8.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535 153 PPRlsPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIPREnifannLLFGNSGEFLGFDENEPTSRSGG------ 226
Cdd:cd07539 430 TAR--PGAAALIAALHDAGIDVVMITGDHPITARAIAKELGLPRD------AEVVTGAELDALDEEALTGLVADidvfar 501

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 42571535 227 -----KAKAVQQIRK-GRLyktMAMIGDGATDLEARK 257
Cdd:cd07539 502 vspeqKLQIVQALQAaGRV---VAMTGDGANDAAAIR 535
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
 129-265 9.26e-03

ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, are 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. They 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. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.


Pssm-ID: 319764 [Multi-domain]  Cd Length: 319  Bit Score: 37.05  E-value: 9.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535 129 EALAARLSLFKPSLSKVEEYLD-------KRPPRlsPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIPRENIFA 201
Cdd:cd01431  86 LALAYREFDPETSKEAVELNLVflgliglQDPPR--PEVKEAIAKCRTAGIKVVMITGDNPLTAIAIAREIGIDTKASGV 163

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571535 202 NNLLFGNSGEFLGFDENEPT----SRSG--GKAKAVQQIRKgrLYKTMAMIGDGATDLEARKPggADLFI 265
Cdd:cd01431 164 ILGEEADEMSEEELLDLIAKvavfARVTpeQKLRIVKALQA--RGEVVAMTGDGVNDAPALKQ--ADVGI 229
 
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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