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Conserved domains on  [gi|19920360|ref|NP_608336|]
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uncharacterized protein Dmel_CG12237 [Drosophila melanogaster]

Protein Classification

HAD family hydrolase( domain architecture ID 10536425)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Put_Phosphatase pfam06888
Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. ...
 30-264 2.43e-126

Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. Some family members represent the products of the PSI14 phosphatase family in Lycopersicon esculentum (Tomato).


:

Pssm-ID: 284339  Cd Length: 234  Bit Score: 360.15  E-value: 2.43e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360    30 AAFDFDHTIVSQNTDTVVRDLLPTEVTSAKVNELVENDCWTEYMAEVFRLLHEQQVSEARIRDTIRGIPEVPGFVRLIKH 109
Cdd:pfam06888   3 VVFDFDKTIIDVDSDNWVVDELPTTQLFEQLRPTMPKGFWNELMDRVMKELHDQGVSIADIKAVLRSIPLVPGMVRLIKF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360   110 LAK-RLHYDLIIISDSNSVFIDEWLRAHNLADCFVAIFTNPAEFDASGRLMVRAHHQQSdCKLSASNLCKGRVLEHFVIE 188
Cdd:pfam06888  83 LAKnGLGCDLIIISDANSFFIETILRAAGLHDLFSEIFTNPASVDARGRLTVLPYHDHS-CNLCPSNMCKGKVLDEIVAS 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19920360   189 QdLRRSIRYDHVFYVGDGNNDICPVLRQRACDFACARKGFAMEKHLLRNrsKLKLRAQLLIWKSGFDLMDQMLALP 264
Cdd:pfam06888 162 Q-AREGVRYERVIYVGDGANDFCPSLRLRECDVAMPRKGFPLWKLISEN--PLLLKASVVEWSSGAELEEILLQLI 234
 
Name Accession Description Interval E-value
Put_Phosphatase pfam06888
Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. ...
 30-264 2.43e-126

Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. Some family members represent the products of the PSI14 phosphatase family in Lycopersicon esculentum (Tomato).


Pssm-ID: 284339  Cd Length: 234  Bit Score: 360.15  E-value: 2.43e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360    30 AAFDFDHTIVSQNTDTVVRDLLPTEVTSAKVNELVENDCWTEYMAEVFRLLHEQQVSEARIRDTIRGIPEVPGFVRLIKH 109
Cdd:pfam06888   3 VVFDFDKTIIDVDSDNWVVDELPTTQLFEQLRPTMPKGFWNELMDRVMKELHDQGVSIADIKAVLRSIPLVPGMVRLIKF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360   110 LAK-RLHYDLIIISDSNSVFIDEWLRAHNLADCFVAIFTNPAEFDASGRLMVRAHHQQSdCKLSASNLCKGRVLEHFVIE 188
Cdd:pfam06888  83 LAKnGLGCDLIIISDANSFFIETILRAAGLHDLFSEIFTNPASVDARGRLTVLPYHDHS-CNLCPSNMCKGKVLDEIVAS 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19920360   189 QdLRRSIRYDHVFYVGDGNNDICPVLRQRACDFACARKGFAMEKHLLRNrsKLKLRAQLLIWKSGFDLMDQMLALP 264
Cdd:pfam06888 162 Q-AREGVRYERVIYVGDGANDFCPSLRLRECDVAMPRKGFPLWKLISEN--PLLLKASVVEWSSGAELEEILLQLI 234
HAD_Pase cd16418
phosphatases, similar to human PHOSPHO1 and PHOSPHO2 phosphatases; belongs to the haloacid ...
 103-222 8.46e-64

phosphatases, similar to human PHOSPHO1 and PHOSPHO2 phosphatases; belongs to the haloacid dehalogenase-like superfamily; This family includes phosphatases with different substrate specificities. Human PHOSPHO1 is a phosphoethanolamine/phosphocholine phosphatase associated with high levels of expression at mineralizing regions of bone and cartilage and is thought to be involved in the generation of inorganic phosphate for bone mineralization. Human PHOSPHO2 is a putative phosphatase which shows high specific activity toward pyridoxal-5-phosphate; PHODPHO2 is not specific to bone but is expressed in a wide range of soft tissues. These 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 (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) 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: 319855  Cd Length: 130  Bit Score: 197.17  E-value: 8.46e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360 103 FVRLIKHLAKRLHYDLIIISDSNSVFIDEWLRAHNLADCFVAIFTNPAEFDASGRLMVRAHHQQSDCKLSASNLCKGRVL 182
Cdd:cd16418  12 MVDLIKFLAKNDGFELIIISDANSFFIEEWLEAAGFHDLFSKIFTNPASFDANGNLTVRPYFHSHSCLLCPSNMCKGKVL 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19920360 183 EHFVIEQDlRRSIRYDHVFYVGDGNNDICPVLRQRACDFA 222
Cdd:cd16418  92 EEYVASRA-QDSVHYERVIYVGDGANDFCPVLRLRKGDVA 130
DKMTPPase-SF TIGR01489
2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This phosphatase is a member of the IB ...
 32-214 2.88e-35

2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This phosphatase is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. With the exception of OMNI|NTL01BS01361 from B. subtilis and GP|15024582 from Clostridium acetabutylicum, the members of this group are all eukaryotic, spanning metazoa, plants and fungi. The B. subtilus gene (YkrX, renamed MtnX) is part of an operon for the conversion of methylthioribose (MTR) to methionine. It works with the enolase MtnW, a RuBisCO homolog. The combination of MtnW and MtnX achieves the same overall reaction as the enolase-phosphatase MtnC. The function of MtnX was shown by Ashida, et al. (2003) to be 2,3-diketo-5-methylthio-1-phosphopentane phosphatase, rather than 2,3-diketo-5-methylthio-1-phosphopentane phosphatase as proposed earlier. See the Genome Property for methionine salvage for more details. In eukaryotes, methionine salvage from methylthioadenosine also occurs. It seems reasonable that members of this family in eukaryotes fulfill a similar role as in Bacillus. A more specific, equivalog-level model is TIGR03333. Note that SP|P53981 from S. cerevisiae, a member of this family, is annotated as a "probable membrane protein" due to a predicted transmembrane helix. The region in question contains the second of the three conserved HAD superfamily catalytic motifs and thus, considering the fold of the HAD catalytic domain, is unlikely to be a transmembrane region in fact. [Central intermediary metabolism, Other]


Pssm-ID: 213629 [Multi-domain]  Cd Length: 188  Bit Score: 126.01  E-value: 2.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360    32 FDFDHTIVSQNTDTVVRDLLPTEVTSAKVNELVENDCWTEYMAEVFRLLHEQQVSEARIRDTIRGIPEVPGFVRLIKhLA 111
Cdd:TIGR01489   6 SDFDGTITLNDSDDWITDKFGPPEANRLLDGVLSKTLSIKFMDRRMKGLLPSGLKEDEILEVLKSAPIDPGFKEFIA-FI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360   112 KRLHYDLIIISDSNSVFIDEWLRAHNLADCFVAIFTNPAEFDASGRLMVRAHHQQSdCKLSASNLCKGRVLEHFvieqdl 191
Cdd:TIGR01489  85 KEHGIDFIVISDGNDFFIDPVLEGIGEKDVFIEIYSNPASFDNDGRHIVWPHHCHG-CCSCPCGCCKGKVIHKL------ 157

                         170       180
                  ....*....|....*....|...
gi 19920360   192 rRSIRYDHVFYVGDGNNDICPVL 214
Cdd:TIGR01489 158 -SEPKYQHIIYIGDGVTDVCPAK 179
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 30-224 8.56e-07

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: 49.06  E-value: 8.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360  30 AAFDFDHTIVSQNTDT------VVRDLLPTEVTSAKVNELVE---NDCWT--EYMAEVFRLL--HEQQVSEARIRDTIRG 96
Cdd:COG0560   6 AVFDLDGTLIAGESIDelarflGRRGLVDRREVLEEVAAITEramAGELDfeESLRFRVALLagLPEEELEELAERLFEE 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360  97 IPEV-PGFVRLIKHLaKRLHYDLIIISDSNSVFIDEWLRAHNLaDCFVAiftNPAEFD-------ASGRLMVRAHhqqsd 168
Cdd:COG0560  86 VPRLyPGARELIAEH-RAAGHKVAIVSGGFTFFVEPIAERLGI-DHVIA---NELEVEdgrltgeVVGPIVDGEG----- 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19920360 169 cklsasnlcKGRVLEHFVIEQDlrrsIRYDHVFYVGDGNNDIcPVLrqRACDFACA 224
Cdd:COG0560 156 ---------KAEALRELAAELG----IDLEQSYAYGDSANDL-PML--EAAGLPVA 195
 
Name Accession Description Interval E-value
Put_Phosphatase pfam06888
Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. ...
 30-264 2.43e-126

Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. Some family members represent the products of the PSI14 phosphatase family in Lycopersicon esculentum (Tomato).


Pssm-ID: 284339  Cd Length: 234  Bit Score: 360.15  E-value: 2.43e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360    30 AAFDFDHTIVSQNTDTVVRDLLPTEVTSAKVNELVENDCWTEYMAEVFRLLHEQQVSEARIRDTIRGIPEVPGFVRLIKH 109
Cdd:pfam06888   3 VVFDFDKTIIDVDSDNWVVDELPTTQLFEQLRPTMPKGFWNELMDRVMKELHDQGVSIADIKAVLRSIPLVPGMVRLIKF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360   110 LAK-RLHYDLIIISDSNSVFIDEWLRAHNLADCFVAIFTNPAEFDASGRLMVRAHHQQSdCKLSASNLCKGRVLEHFVIE 188
Cdd:pfam06888  83 LAKnGLGCDLIIISDANSFFIETILRAAGLHDLFSEIFTNPASVDARGRLTVLPYHDHS-CNLCPSNMCKGKVLDEIVAS 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19920360   189 QdLRRSIRYDHVFYVGDGNNDICPVLRQRACDFACARKGFAMEKHLLRNrsKLKLRAQLLIWKSGFDLMDQMLALP 264
Cdd:pfam06888 162 Q-AREGVRYERVIYVGDGANDFCPSLRLRECDVAMPRKGFPLWKLISEN--PLLLKASVVEWSSGAELEEILLQLI 234
HAD_Pase cd16418
phosphatases, similar to human PHOSPHO1 and PHOSPHO2 phosphatases; belongs to the haloacid ...
 103-222 8.46e-64

phosphatases, similar to human PHOSPHO1 and PHOSPHO2 phosphatases; belongs to the haloacid dehalogenase-like superfamily; This family includes phosphatases with different substrate specificities. Human PHOSPHO1 is a phosphoethanolamine/phosphocholine phosphatase associated with high levels of expression at mineralizing regions of bone and cartilage and is thought to be involved in the generation of inorganic phosphate for bone mineralization. Human PHOSPHO2 is a putative phosphatase which shows high specific activity toward pyridoxal-5-phosphate; PHODPHO2 is not specific to bone but is expressed in a wide range of soft tissues. These 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 (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) 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: 319855  Cd Length: 130  Bit Score: 197.17  E-value: 8.46e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360 103 FVRLIKHLAKRLHYDLIIISDSNSVFIDEWLRAHNLADCFVAIFTNPAEFDASGRLMVRAHHQQSDCKLSASNLCKGRVL 182
Cdd:cd16418  12 MVDLIKFLAKNDGFELIIISDANSFFIEEWLEAAGFHDLFSKIFTNPASFDANGNLTVRPYFHSHSCLLCPSNMCKGKVL 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19920360 183 EHFVIEQDlRRSIRYDHVFYVGDGNNDICPVLRQRACDFA 222
Cdd:cd16418  92 EEYVASRA-QDSVHYERVIYVGDGANDFCPVLRLRKGDVA 130
DKMTPPase-SF TIGR01489
2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This phosphatase is a member of the IB ...
 32-214 2.88e-35

2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This phosphatase is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. With the exception of OMNI|NTL01BS01361 from B. subtilis and GP|15024582 from Clostridium acetabutylicum, the members of this group are all eukaryotic, spanning metazoa, plants and fungi. The B. subtilus gene (YkrX, renamed MtnX) is part of an operon for the conversion of methylthioribose (MTR) to methionine. It works with the enolase MtnW, a RuBisCO homolog. The combination of MtnW and MtnX achieves the same overall reaction as the enolase-phosphatase MtnC. The function of MtnX was shown by Ashida, et al. (2003) to be 2,3-diketo-5-methylthio-1-phosphopentane phosphatase, rather than 2,3-diketo-5-methylthio-1-phosphopentane phosphatase as proposed earlier. See the Genome Property for methionine salvage for more details. In eukaryotes, methionine salvage from methylthioadenosine also occurs. It seems reasonable that members of this family in eukaryotes fulfill a similar role as in Bacillus. A more specific, equivalog-level model is TIGR03333. Note that SP|P53981 from S. cerevisiae, a member of this family, is annotated as a "probable membrane protein" due to a predicted transmembrane helix. The region in question contains the second of the three conserved HAD superfamily catalytic motifs and thus, considering the fold of the HAD catalytic domain, is unlikely to be a transmembrane region in fact. [Central intermediary metabolism, Other]


Pssm-ID: 213629 [Multi-domain]  Cd Length: 188  Bit Score: 126.01  E-value: 2.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360    32 FDFDHTIVSQNTDTVVRDLLPTEVTSAKVNELVENDCWTEYMAEVFRLLHEQQVSEARIRDTIRGIPEVPGFVRLIKhLA 111
Cdd:TIGR01489   6 SDFDGTITLNDSDDWITDKFGPPEANRLLDGVLSKTLSIKFMDRRMKGLLPSGLKEDEILEVLKSAPIDPGFKEFIA-FI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360   112 KRLHYDLIIISDSNSVFIDEWLRAHNLADCFVAIFTNPAEFDASGRLMVRAHHQQSdCKLSASNLCKGRVLEHFvieqdl 191
Cdd:TIGR01489  85 KEHGIDFIVISDGNDFFIDPVLEGIGEKDVFIEIYSNPASFDNDGRHIVWPHHCHG-CCSCPCGCCKGKVIHKL------ 157

                         170       180
                  ....*....|....*....|...
gi 19920360   192 rRSIRYDHVFYVGDGNNDICPVL 214
Cdd:TIGR01489 158 -SEPKYQHIIYIGDGVTDVCPAK 179
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 30-215 1.14e-19

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: 84.33  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360    30 AAFDFDHTIVSQNTDT-VVRDLLPTEVTSAKVNELVeNDCWTEYMAEVFRLLHEQQ--VSEARIRDTIRGIPEV-PGFVR 105
Cdd:TIGR01488   2 AIFDFDGTLTRQDSLIdLLAKLLGTNDEVIELTRLA-PSGRISFEDALGRRLALLHrsRSEEVAKEFLARQVALrPGARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360   106 LIKHLAKRLHyDLIIISDSNSVFIDEWLRAHNLADcfvaIFTNPAEFDASGRLMVRAHhqqsdCKLSASNLCKGRVLEHF 185
Cdd:TIGR01488  81 LISWLKERGI-DTVIVSGGFDFFVEPVAEKLGIDD----VFANRLEFDDNGLLTGPIE-----GQVNPEGECKGKVLKEL 150

                         170       180       190
                  ....*....|....*....|....*....|
gi 19920360   186 VIEqdlrRSIRYDHVFYVGDGNNDICPVLR 215
Cdd:TIGR01488 151 LEE----SKITLKKIIAVGDSVNDLPMLKL 176
HAD pfam12710
haloacid dehalogenase-like hydrolase;
30-215 1.11e-07

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 50.99  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360    30 AAFDFDHTIVSQNTDTVVRDLLpTEVTSAKVNELVENDCWTEYMAEVFRLLHEQqvSEARIRDTIRGIPEV--------- 100
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRAL-LRRGGPDLWRALLVLLLLALLRLLGRLSRAG--ARELLRALLAGLPEEdaaelerfv 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360   101 ---------PGFVRLIKHLAKRlHYDLIIISDSNSVFIDEWLRAHNLADCFvaiftnpaefdaSGRLMVRAHHQQSDCKL 171
Cdd:pfam12710  78 aevalprlhPGALELLAAHRAA-GDRVVVVTGGLRPLVEPVLAELGFDEVL------------ATELEVDDGRFTGELRL 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 19920360   172 SASNlCKG-----RVLEHFVIEqdlRRSIRYDHVFYVGDGNNDIcPVLR 215
Cdd:pfam12710 145 IGPP-CAGegkvrRLRAWLAAR---GLGLDLADSVAYGDSPSDL-PMLR 188
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 30-224 8.56e-07

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: 49.06  E-value: 8.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360  30 AAFDFDHTIVSQNTDT------VVRDLLPTEVTSAKVNELVE---NDCWT--EYMAEVFRLL--HEQQVSEARIRDTIRG 96
Cdd:COG0560   6 AVFDLDGTLIAGESIDelarflGRRGLVDRREVLEEVAAITEramAGELDfeESLRFRVALLagLPEEELEELAERLFEE 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360  97 IPEV-PGFVRLIKHLaKRLHYDLIIISDSNSVFIDEWLRAHNLaDCFVAiftNPAEFD-------ASGRLMVRAHhqqsd 168
Cdd:COG0560  86 VPRLyPGARELIAEH-RAAGHKVAIVSGGFTFFVEPIAERLGI-DHVIA---NELEVEdgrltgeVVGPIVDGEG----- 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19920360 169 cklsasnlcKGRVLEHFVIEQDlrrsIRYDHVFYVGDGNNDIcPVLrqRACDFACA 224
Cdd:COG0560 156 ---------KAEALRELAAELG----IDLEQSYAYGDSANDL-PML--EAAGLPVA 195
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 32-147 6.10e-05

uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized Bacillus subtilis YhcW; This subfamily includes the uncharacterized Bacillus subtilis YhcW. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. 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: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 42.63  E-value: 6.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360  32 FDFDHTIVsqntDTvvrdllptevtsakvnELVENDCWTEYMAEVFRLLHEQQVSEARirdtirGIPEVPGFVRLIkHLA 111
Cdd:cd16423   4 FDFDGVIV----DT----------------EPLWYEAWQELLNERRNELIKRQFSEKT------DLPPIEGVKELL-EFL 56

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19920360 112 KRLHYDLIIISDSNSVFIDEWLRAHNLADCFVAIFT 147
Cdd:cd16423  57 KEKGIKLAVASSSPRRWIEPHLERLGLLDYFEVIVT 92
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 32-147 1.20e-03

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


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 39.63  E-value: 1.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360  32 FDFDHTIVsqNTDTVVRDLLptEVTSAKVNELVEND------------CWTEY------MAEVFRLL---HEQQVSEARI 90
Cdd:COG1011   6 FDLDGTLL--DFDPVIAEAL--RALAERLGLLDEAEelaeayraieyaLWRRYergeitFAELLRRLleeLGLDLAEELA 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19920360  91 RDTIRGIPEV----PGFVRLIKHLAKRlHYDLIIISDSNSVFIDEWLRAHNLADCFVAIFT 147
Cdd:COG1011  82 EAFLAALPELvepyPDALELLEALKAR-GYRLALLTNGSAELQEAKLRRLGLDDLFDAVVS 141
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 104-224 1.69e-03

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: 37.38  E-value: 1.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360 104 VRLIKHLaKRLHYDLIIISDSNSVFIDEWLRAHNLADCFVAIFTnpaefdasgrlmvrahhqqSDCKLSASNLCKGrvle 183
Cdd:cd01427  13 VELLKRL-RAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIG-------------------SDGGGTPKPKPKP---- 68

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 19920360 184 hfVIEQDLRRSIRYDHVFYVGDGNNDICpvLRQRACDFACA 224
Cdd:cd01427  69 --LLLLLLKLGVDPEEVLFVGDSENDIE--AARAAGGRTVA 105
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
32-147 2.32e-03

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 38.37  E-value: 2.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920360  32 FDFDHTIVsqntDT----------VVRDLLPTEVTSAKVNELVeNDCWTEYMAEVFRLLHEQQVSEAR-------IRDTI 94
Cdd:COG0546   6 FDLDGTLV----DSapdiaaalneALAELGLPPLDLEELRALI-GLGLRELLRRLLGEDPDEELEELLarfrelyEEELL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 19920360  95 RGIPEVPGFVRLIKHLAKRlHYDLIIISDSNSVFIDEWLRAHNLADCFVAIFT 147
Cdd:COG0546  81 DETRLFPGVRELLEALKAR-GIKLAVVTNKPREFAERLLEALGLDDYFDAIVG 132
 
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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