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Conserved domains on  [gi|1034656384|ref|XP_016867957|]
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phosphoserine phosphatase isoform X2 [Homo sapiens]

Protein Classification

phosphoserine phosphatase( domain architecture ID 11560826)

phosphoserine phosphatase is a HAD (haloacid dehalogenase) family hydrolase that catalyzes the dephosphorylation of phosphoserine (P-Ser)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 15-171 4.54e-98

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: 281.86  E-value: 4.54e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  15 DAVCFDVDSTVIREEGIDELAKICGVEDAVSEM---------------------------------------------EL 49
Cdd:cd04309     1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELtrramggsipfrdalrkrlaiinptkeqvdefleehpprltpgveEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  50 VSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKI 129
Cdd:cd04309    81 VSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSGGKAKVIEQLKEKHHYKRV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034656384 130 IMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDF 171
Cdd:cd04309   161 IMIGDGATDLEACPPADAFIGFGGNVIREKVKARADWYVTDF 202
 
Name Accession Description Interval E-value
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 15-171 4.54e-98

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: 281.86  E-value: 4.54e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  15 DAVCFDVDSTVIREEGIDELAKICGVEDAVSEM---------------------------------------------EL 49
Cdd:cd04309     1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELtrramggsipfrdalrkrlaiinptkeqvdefleehpprltpgveEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  50 VSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKI 129
Cdd:cd04309    81 VSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSGGKAKVIEQLKEKHHYKRV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034656384 130 IMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDF 171
Cdd:cd04309   161 IMIGDGATDLEACPPADAFIGFGGNVIREKVKARADWYVTDF 202
PLN02954 PLN02954
phosphoserine phosphatase
 10-179 7.44e-72

phosphoserine phosphatase


Pssm-ID: 215514 [Multi-domain]  Cd Length: 224  Bit Score: 216.10  E-value: 7.44e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  10 LFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEM------------------------------------------ 47
Cdd:PLN02954    8 LWRSADAVCFDVDSTVCVDEGIDELAEFCGAGEAVAEWtakamggsvpfeealaarlslfkpslsqveeflekrpprlsp 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  48 ---ELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKF 124
Cdd:PLN02954   88 gipELVKKLRARGTDVYLVSGGFRQMIAPVAAILGIPPENIFANQILFGDSGEYAGFDENEPTSRSGGKAEAVQHIKKKH 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034656384 125 HFKKIIMIGDGATDMEACPP--ADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELE 179
Cdd:PLN02954  168 GYKTMVMIGDGATDLEARKPggADLFIGYGGVQVREAVAAKADWFVTDFQDLIEVLD 224
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 1-175 6.93e-70

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: 211.06  E-value: 6.93e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384   1 MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEM--------------------------------- 47
Cdd:TIGR00338   1 DIAHSELSPLLRSKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEIteramrgeldfkaslrervallkglpvellkev 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  48 -----------ELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPAtnVFANRLKFYfNGEYAGFDETQPTAES-GGKGK 115
Cdd:TIGR00338  81 renlpltegaeELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDA--AFANRLEVE-DGKLTGLVEGPIVDASyKGKTL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034656384 116 VIKLLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNA--KWYITDFVELL 175
Cdd:TIGR00338 158 LILLRKEGISPENTVAVGDGANDLSMIKAAGLGIAFNAKPKLQQKADICinKKDLTDILPLL 219
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 16-171 1.41e-16

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: 74.10  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  16 AVCFDVDSTVIREEGIDELAKICG---------VEDAVSEM--------------------------------------- 47
Cdd:COG0560     5 LAVFDLDGTLIAGESIDELARFLGrrglvdrreVLEEVAAIteramageldfeeslrfrvallaglpeeeleelaerlfe 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  48 ----------ELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPatNVFANRLKFYfNGEYAGfDETQPTAESGGKGKVI 117
Cdd:COG0560    85 evprlypgarELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGID--HVIANELEVE-DGRLTG-EVVGPIVDGEGKAEAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384 118 KLLKEKF--HFKKIIMIGDGATD---MEAcppADAFIGFGGN-VIRQQVKDNAKWYITDF 171
Cdd:COG0560   161 RELAAELgiDLEQSYAYGDSANDlpmLEA---AGLPVAVNPDpALREAADRERGWPVLDL 217
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 47-141 2.84e-08

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: 51.05  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  47 MELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPatnvfanrlkFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHf 126
Cdd:pfam00702 104 AEALKALKERGIKVAILTGDNPEAAEALLRLLGLD----------DYFDVVISGDDVGVGKPKPEIYLAALERLGVKPE- 172

                          90
                  ....*....|....*
gi 1034656384 127 kKIIMIGDGATDMEA 141
Cdd:pfam00702 173 -EVLMVGDGVNDIPA 186
 
Name Accession Description Interval E-value
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 15-171 4.54e-98

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: 281.86  E-value: 4.54e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  15 DAVCFDVDSTVIREEGIDELAKICGVEDAVSEM---------------------------------------------EL 49
Cdd:cd04309     1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELtrramggsipfrdalrkrlaiinptkeqvdefleehpprltpgveEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  50 VSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKI 129
Cdd:cd04309    81 VSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSGGKAKVIEQLKEKHHYKRV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034656384 130 IMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDF 171
Cdd:cd04309   161 IMIGDGATDLEACPPADAFIGFGGNVIREKVKARADWYVTDF 202
PLN02954 PLN02954
phosphoserine phosphatase
 10-179 7.44e-72

phosphoserine phosphatase


Pssm-ID: 215514 [Multi-domain]  Cd Length: 224  Bit Score: 216.10  E-value: 7.44e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  10 LFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEM------------------------------------------ 47
Cdd:PLN02954    8 LWRSADAVCFDVDSTVCVDEGIDELAEFCGAGEAVAEWtakamggsvpfeealaarlslfkpslsqveeflekrpprlsp 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  48 ---ELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKF 124
Cdd:PLN02954   88 gipELVKKLRARGTDVYLVSGGFRQMIAPVAAILGIPPENIFANQILFGDSGEYAGFDENEPTSRSGGKAEAVQHIKKKH 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034656384 125 HFKKIIMIGDGATDMEACPP--ADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELE 179
Cdd:PLN02954  168 GYKTMVMIGDGATDLEARKPggADLFIGYGGVQVREAVAAKADWFVTDFQDLIEVLD 224
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 1-175 6.93e-70

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: 211.06  E-value: 6.93e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384   1 MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEM--------------------------------- 47
Cdd:TIGR00338   1 DIAHSELSPLLRSKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEIteramrgeldfkaslrervallkglpvellkev 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  48 -----------ELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPAtnVFANRLKFYfNGEYAGFDETQPTAES-GGKGK 115
Cdd:TIGR00338  81 renlpltegaeELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDA--AFANRLEVE-DGKLTGLVEGPIVDASyKGKTL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034656384 116 VIKLLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNA--KWYITDFVELL 175
Cdd:TIGR00338 158 LILLRKEGISPENTVAVGDGANDLSMIKAAGLGIAFNAKPKLQQKADICinKKDLTDILPLL 219
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 16-145 1.27e-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: 112.06  E-value: 1.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  16 AVCFDVDSTVIREEG-IDELAKICGVEDAVSEM----------------------------------------------E 48
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSlIDLLAKLLGTNDEVIELtrlapsgrisfedalgrrlallhrsrseevakeflarqvalrpgarE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  49 LVSRLQERNVQVFLISGGFRSIVEHVASKLNIPatNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKE--KFHF 126
Cdd:TIGR01488  81 LISWLKERGIDTVIVSGGFDFFVEPVAEKLGID--DVFANRLEFDDNGLLTGPIEGQVNPEGECKGKVLKELLEesKITL 158

                         170
                  ....*....|....*....
gi 1034656384 127 KKIIMIGDGATDMEACPPA 145
Cdd:TIGR01488 159 KKIIAVGDSVNDLPMLKLA 177
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 16-171 1.41e-16

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: 74.10  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  16 AVCFDVDSTVIREEGIDELAKICG---------VEDAVSEM--------------------------------------- 47
Cdd:COG0560     5 LAVFDLDGTLIAGESIDELARFLGrrglvdrreVLEEVAAIteramageldfeeslrfrvallaglpeeeleelaerlfe 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  48 ----------ELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPatNVFANRLKFYfNGEYAGfDETQPTAESGGKGKVI 117
Cdd:COG0560    85 evprlypgarELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGID--HVIANELEVE-DGRLTG-EVVGPIVDGEGKAEAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384 118 KLLKEKF--HFKKIIMIGDGATD---MEAcppADAFIGFGGN-VIRQQVKDNAKWYITDF 171
Cdd:COG0560   161 RELAAELgiDLEQSYAYGDSANDlpmLEA---AGLPVAVNPDpALREAADRERGWPVLDL 217
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 17-138 2.93e-14

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: 67.19  E-value: 2.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  17 VCFDVDSTVIREEGIDELAKICGVEDAVSEM--------------------------------------------ELVSR 52
Cdd:cd07500     2 IVFDMDSTLIQQEVIDELAAEAGVGEEVAAIteramrgeldfeeslrervallkglpesvldevyerltltpgaeELIQT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  53 LQERNVQVFLISGGFRSIVEHVASKLNIPAtnVFANRLKF---YFNGEYAGfdetqPTAESGGKGKVIKLLKEKFHFKK- 128
Cdd:cd07500    82 LKAKGYKTAVVSGGFTYFTDRLAEELGLDY--AFANELEIkdgKLTGKVLG-----PIVDAQRKAETLQELAARLGIPLe 154

                         170
                  ....*....|.
gi 1034656384 129 -IIMIGDGATD 138
Cdd:cd07500   155 qTVAVGDGAND 165
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 16-151 5.33e-09

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: 51.24  E-value: 5.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  16 AVCFDVDSTVireegideLAKicgvedavsemELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPatnvfanrlkFYFN 95
Cdd:cd01427     1 AVLFDLDGTL--------LAV-----------ELLKRLRAAGIKLAIVTNRSREALRALLEKLGLG----------DLFD 51

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034656384  96 GEYAGFDETQPTAEsgGKGKVIKLLKEKFHFKKIIMIGDGATDMEACPPA-DAFIGF 151
Cdd:cd01427    52 GIIGSDGGGTPKPK--PKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAgGRTVAV 106
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 47-141 2.84e-08

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: 51.05  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  47 MELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPatnvfanrlkFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHf 126
Cdd:pfam00702 104 AEALKALKERGIKVAILTGDNPEAAEALLRLLGLD----------DYFDVVISGDDVGVGKPKPEIYLAALERLGVKPE- 172

                          90
                  ....*....|....*
gi 1034656384 127 kKIIMIGDGATDMEA 141
Cdd:pfam00702 173 -EVLMVGDGVNDIPA 186
serB PRK11133
phosphoserine phosphatase; Provisional
 19-139 1.90e-06

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 46.87  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  19 FDVDSTVIREEGIDELAKICGVEDAVSEM--------------------------------------------ELVSRLQ 54
Cdd:PRK11133  115 MDMDSTAIQIECIDEIAKLAGTGEEVAEVteramrgeldfeaslrqrvatlkgadanilqqvrenlplmpgltELVLKLQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  55 ERNVQVFLISGGFRSIVEHVASKLNIPAtnVFANRLKFY---FNGEYAGfdetqPTAESGGKGKVIKLLKEKFHF--KKI 129
Cdd:PRK11133  195 ALGWKVAIASGGFTYFADYLRDKLRLDA--AVANELEIMdgkLTGNVLG-----DIVDAQYKADTLTRLAQEYEIplAQT 267

                         170
                  ....*....|
gi 1034656384 130 IMIGDGATDM 139
Cdd:PRK11133  268 VAIGDGANDL 277
P-type_ATPase_Cu-like cd02094
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ...
 32-138 3.49e-06

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: 46.32  E-value: 3.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  32 DELAKICGVEDAVSE--MELVSRLQERNVQVFLISGGFRSIVEHVASKLNIpaTNVFANRLkfyfngeyagfdetqPtae 109
Cdd:cd02094   457 GELAGLIAVADPLKPdaAEAIEALKKMGIKVVMLTGDNRRTARAIAKELGI--DEVIAEVL---------------P--- 516

                          90       100
                  ....*....|....*....|....*....
gi 1034656384 110 sGGKGKVIKLLKEKFHfkKIIMIGDGATD 138
Cdd:cd02094   517 -EDKAEKVKKLQAQGK--KVAMVGDGIND 542
HAD_Pase cd07524
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like ...
 48-146 1.55e-05

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: 43.47  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  48 ELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKfyFNGEYAGFDETQPTAESGG----KGKVIKLLKEK 123
Cdd:cd07524    79 EFVAFCQEHGIPFIIVSGGMDFFIEPLLEGLVIEKIAIYCNGSD--FSGEQIHIDWPHECDCTNGcgccKSSIIRKYSKP 156

                          90       100
                  ....*....|....*....|...
gi 1034656384 124 FHFkkIIMIGDGATDMEACPPAD 146
Cdd:cd07524   157 RPF--IIVIGDSVTDLEAAKEAD 177
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
48-135 4.92e-05

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 42.82  E-value: 4.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  48 ELVSRLQERNVQVFLISGGFRSIVEHVASKLNIpaTNVFANRLkfyfngeyagfdetqPtaesGGKGKVIKLLKEKFHfk 127
Cdd:COG2217   548 EAIAALKALGIRVVMLTGDNERTAEAVARELGI--DEVRAEVL---------------P----EDKAAAVRELQAQGK-- 604


                  ....*...
gi 1034656384 128 KIIMIGDG 135
Cdd:COG2217   605 KVAMVGDG 612
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
48-180 5.19e-05

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 42.22  E-value: 5.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  48 ELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPAtnvfanrlkfYFNGEYAGFDetqpTAESGGKGKVIKLLKEKFHFK 127
Cdd:COG0546    91 ELLEALKARGIKLAVVTNKPREFAERLLEALGLDD----------YFDAIVGGDD----VPPAKPKPEPLLEALERLGLD 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034656384 128 K--IIMIGDGATDMEACPPADA-FIG--FGGNVIRQQVKDNAKWYITDFVELLGELEE 180
Cdd:COG0546   157 PeeVLMVGDSPHDIEAARAAGVpFIGvtWGYGSAEELEAAGADYVIDSLAELLALLAE 214
P-type_ATPase_Cu-like cd07552
P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+) ...
 48-174 1.22e-04

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: 41.52  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  48 ELVSRLQERNVQVFLISGGFRSIVEHVASKLNIpaTNVFANRLKfyfngeyagfDEtqptaesggKGKVIKLLKEKfhFK 127
Cdd:cd07552   462 EAIRALKAQGITPVMLTGDNEEVAQAVAEELGI--DEYFAEVLP----------ED---------KAKKVKELQAE--GK 518

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034656384 128 KIIMIGDGATDMEACPPADA--FIGFGGNV---------IRQQVKDnakwyITDFVEL 174
Cdd:cd07552   519 KVAMVGDGVNDAPALAQADVgiAIGAGTDVaiesadvvlVKSDPRD-----IVDFLEL 571
P-type_ATPase_HM cd02079
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ...
 32-153 1.74e-04

P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. These ATPases include mammalian copper-transporting ATPases, ATP7A and ATP7B, Bacillus subtilis CadA which transports cadmium, zinc and cobalt out of the cell, Bacillus subtilis ZosA/PfeT which transports copper, and perhaps also zinc and ferrous iron, Archaeoglobus fulgidus CopA and CopB, Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase, and Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+). The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This family 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: 319774 [Multi-domain]  Cd Length: 617  Bit Score: 41.05  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  32 DELAKICGVEDAVSE--MELVSRLQERNVQVFLISGGFRSIVEHVASKLNIpaTNVFAnrlkfyfngeyagfdETQPtAE 109
Cdd:cd02079   437 GKLVGLFALEDQLRPeaKEVIAELKSGGIKVVMLTGDNEAAAQAVAKELGI--DEVHA---------------GLLP-ED 498

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034656384 110 sggKGKVIKLLKEKFHfkKIIMIGDGATDMEACPPADAFIGFGG 153
Cdd:cd02079   499 ---KLAIVKALQAEGG--PVAMVGDGINDAPALAQADVGIAMGS 537
P-type_ATPase_HM cd07550
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
 32-153 9.14e-04

P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. 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: 319848 [Multi-domain]  Cd Length: 592  Bit Score: 39.18  E-value: 9.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  32 DELAKICGVEDAVSE--MELVSRLQERNV-QVFLISGGFRSIVEHVASKLNIpaTNVFANRLkfyfngeyagfdetqPTa 108
Cdd:cd07550   410 GRLIGVIGLSDPLRPeaAEVIARLRALGGkRIIMLTGDHEQRARALAEQLGI--DRYHAEAL---------------PE- 471

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034656384 109 esgGKGKVIKLLKEKFHfkKIIMIGDGATDMEACPPADAFIGFGG 153
Cdd:cd07550   472 ---DKAEIVEKLQAEGR--TVAFVGDGINDSPALSYADVGISMRG 511
UMPH-1 pfam05822
Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5 ...
 26-138 1.19e-03

Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5'-nucleotidase proteins. P5'N-1, also known as uridine monophosphate hydrolase-1 (UMPH-1), is a member of a large functional group of enzymes, characterized by the ability to dephosphorylate nucleic acids. P5'N-1 catalyzes the dephosphorylation of pyrimidine nucleoside monophosphates to the corresponding nucleosides. Deficiencies in this proteins function can lead to several different disorders in humans.


Pssm-ID: 310424 [Multi-domain]  Cd Length: 246  Bit Score: 38.11  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  26 IREEGIDELAKIC--GVEDAVSEMelVSRLQERNVQVFLISGGFRSIVEHVASKLNI--PATNVFANRLKFYFNGEYAGF 101
Cdd:pfam05822  75 LQKEAIAEVVAESdiMLRDGTHEF--FDDLQQLNVPVLIFSAGLGDVLEEVLRQANVmhPNVKVVSNFMDFDDDGVLNGF 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034656384 102 deTQPTAESGGK-------GKVIKLLKEKFHfkkIIMIGDGATD 138
Cdd:pfam05822 153 --KGPLIHTFNKnetvldgTEYFDQLHTRDN---IILLGDSLGD 191
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
 39-162 1.46e-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: 38.45  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656384  39 GVEDAVSE--MELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPatnVFAnrlkfyfngeyagfdETQPTaesgGKGKV 116
Cdd:TIGR01494 383 TFEDPLRPdaKETIEALRKAGIKVVMLTGDNVLTAKAIAKELGID---VFA---------------RVKPE----EKAAI 440

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1034656384 117 IKLLKEKFHfkKIIMIGDGATDMEACPPADAFIGFGGNVIRQQVKD 162
Cdd:TIGR01494 441 VEALQEKGR--TVAMTGDGVNDAPALKKADVGIAMGSGDVAKAAAD 484
 
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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