NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2047148379|ref|XP_041736467|]
View 

probable phosphatase phospho1 [Coregonus clupeaformis]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

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

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 37-272 1.18e-103

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member pfam06888:

Pssm-ID: 473868  Cd Length: 234  Bit Score: 301.21  E-value: 1.18e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379  37 FLIFFDFDETIVDESSDDVVVQAAPGQNLPTWLKDTYRPGHYNEYMQRVLAYMAEKGVNESAIRSVIEKIPASPGMLALF 116
Cdd:pfam06888   1 ILVVFDFDKTIIDVDSDNWVVDELPTTQLFEQLRPTMPKGFWNELMDRVMKELHDQGVSIADIKAVLRSIPLVPGMVRLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379 117 QFLRHcPPQDFEVVLVSDANTFFIESWLRRVGARQLFVKIFTNPATFDKDGRLVLRPFHSHSCLRCPENMCKQVILRDYV 196
Cdd:pfam06888  81 KFLAK-NGLGCDLIIISDANSFFIETILRAAGLHDLFSEIFTNPASVDARGRLTVLPYHDHSCNLCPSNMCKGKVLDEIV 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2047148379 197 MRRTQErGRPFQRVFYVGDGANDFCPSLILGPRDTAFARRDYPMHRLITEiheaRPGEFKAVTVPWASGDDVVERL 272
Cdd:pfam06888 160 ASQARE-GVRYERVIYVGDGANDFCPSLRLRECDVAMPRKGFPLWKLISE----NPLLLKASVVEWSSGAELEEIL 230
 
Name Accession Description Interval E-value
Put_Phosphatase pfam06888
Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. ...
 37-272 1.18e-103

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: 301.21  E-value: 1.18e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379  37 FLIFFDFDETIVDESSDDVVVQAAPGQNLPTWLKDTYRPGHYNEYMQRVLAYMAEKGVNESAIRSVIEKIPASPGMLALF 116
Cdd:pfam06888   1 ILVVFDFDKTIIDVDSDNWVVDELPTTQLFEQLRPTMPKGFWNELMDRVMKELHDQGVSIADIKAVLRSIPLVPGMVRLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379 117 QFLRHcPPQDFEVVLVSDANTFFIESWLRRVGARQLFVKIFTNPATFDKDGRLVLRPFHSHSCLRCPENMCKQVILRDYV 196
Cdd:pfam06888  81 KFLAK-NGLGCDLIIISDANSFFIETILRAAGLHDLFSEIFTNPASVDARGRLTVLPYHDHSCNLCPSNMCKGKVLDEIV 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2047148379 197 MRRTQErGRPFQRVFYVGDGANDFCPSLILGPRDTAFARRDYPMHRLITEiheaRPGEFKAVTVPWASGDDVVERL 272
Cdd:pfam06888 160 ASQARE-GVRYERVIYVGDGANDFCPSLRLRECDVAMPRKGFPLWKLISE----NPLLLKASVVEWSSGAELEEIL 230
HAD_Pase cd16418
phosphatases, similar to human PHOSPHO1 and PHOSPHO2 phosphatases; belongs to the haloacid ...
 112-232 1.80e-51

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: 164.81  E-value: 1.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379 112 MLALFQFLRHCPpqDFEVVLVSDANTFFIESWLRRVGARQLFVKIFTNPATFDKDGRLVLRP-FHSHSCLRCPENMCKQV 190
Cdd:cd16418    12 MVDLIKFLAKND--GFELIIISDANSFFIEEWLEAAGFHDLFSKIFTNPASFDANGNLTVRPyFHSHSCLLCPSNMCKGK 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2047148379 191 ILRDYVMRRTQErGRPFQRVFYVGDGANDFCPSLILGPRDTA 232
Cdd:cd16418    90 VLEEYVASRAQD-SVHYERVIYVGDGANDFCPVLRLRKGDVA 130
DKMTPPase-SF TIGR01489
2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This phosphatase is a member of the IB ...
 37-235 6.21e-47

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: 155.28  E-value: 6.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379  37 FLIFFDFDETIVDESSDDVVVQAAPGQNLPTWLKDTYRPGHYNEYMQRVLAYMAEKGVNESAIRSVIEKIPASPGMLALF 116
Cdd:TIGR01489   2 VVVVSDFDGTITLNDSDDWITDKFGPPEANRLLDGVLSKTLSIKFMDRRMKGLLPSGLKEDEILEVLKSAPIDPGFKEFI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379 117 QFLRHcppQDFEVVLVSDANTFFIESWLRRVGARQLFVKIFTNPATFDKDGRLVLRPFHSHSCLRCPENMCKqvilrDYV 196
Cdd:TIGR01489  82 AFIKE---HGIDFIVISDGNDFFIDPVLEGIGEKDVFIEIYSNPASFDNDGRHIVWPHHCHGCCSCPCGCCK-----GKV 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2047148379 197 MRRTQERGRPfqRVFYVGDGANDFCPSLILgprDTAFAR 235
Cdd:TIGR01489 154 IHKLSEPKYQ--HIIYIGDGVTDVCPAKLS---DVVFAK 187
MtnX COG4359
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase (methionine salvage) [Amino acid ...
 36-237 1.27e-20

2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase (methionine salvage) [Amino acid transport and metabolism];


Pssm-ID: 443493 [Multi-domain]  Cd Length: 209  Bit Score: 87.18  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379  36 RFLIFFDFDETIvdeSSDDVVVQ-----AAPGqnlptW--LKDTYRPGHYN--EYMQRVLAYMaekGVNESAIRSVIEKI 106
Cdd:COG4359     1 KPVIFCDFDGTI---TEKDVIDAilerfAPPG-----WeeIEDDWLAGEISsrECLGRQFALL---PASKEELDALLENI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379 107 PASPGMLAlfqFLRHCPPQDFEVVLVSDANTFFIESWLRRVGARqlFVKIFTNPATFDkDGRLVLRPFHSHSclRCPEN- 185
Cdd:COG4359    70 EIDPGFKE---FVQFCRERGIPLYIVSDGLDFYIEPILERYGLS--DVPIYANRLVFD-GGGIRIEFPYADP--DCSNGc 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2047148379 186 -MCKQVILRDYvmrrtqerGRPFQRVFYVGDGANDFCPSLILgprDTAFARRD 237
Cdd:COG4359   142 gTCKCAVIRKL--------KSDGYKVIYIGDGRSDFCAAKLA---DLVFAKGK 183
 
Name Accession Description Interval E-value
Put_Phosphatase pfam06888
Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. ...
 37-272 1.18e-103

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: 301.21  E-value: 1.18e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379  37 FLIFFDFDETIVDESSDDVVVQAAPGQNLPTWLKDTYRPGHYNEYMQRVLAYMAEKGVNESAIRSVIEKIPASPGMLALF 116
Cdd:pfam06888   1 ILVVFDFDKTIIDVDSDNWVVDELPTTQLFEQLRPTMPKGFWNELMDRVMKELHDQGVSIADIKAVLRSIPLVPGMVRLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379 117 QFLRHcPPQDFEVVLVSDANTFFIESWLRRVGARQLFVKIFTNPATFDKDGRLVLRPFHSHSCLRCPENMCKQVILRDYV 196
Cdd:pfam06888  81 KFLAK-NGLGCDLIIISDANSFFIETILRAAGLHDLFSEIFTNPASVDARGRLTVLPYHDHSCNLCPSNMCKGKVLDEIV 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2047148379 197 MRRTQErGRPFQRVFYVGDGANDFCPSLILGPRDTAFARRDYPMHRLITEiheaRPGEFKAVTVPWASGDDVVERL 272
Cdd:pfam06888 160 ASQARE-GVRYERVIYVGDGANDFCPSLRLRECDVAMPRKGFPLWKLISE----NPLLLKASVVEWSSGAELEEIL 230
HAD_Pase cd16418
phosphatases, similar to human PHOSPHO1 and PHOSPHO2 phosphatases; belongs to the haloacid ...
 112-232 1.80e-51

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: 164.81  E-value: 1.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379 112 MLALFQFLRHCPpqDFEVVLVSDANTFFIESWLRRVGARQLFVKIFTNPATFDKDGRLVLRP-FHSHSCLRCPENMCKQV 190
Cdd:cd16418    12 MVDLIKFLAKND--GFELIIISDANSFFIEEWLEAAGFHDLFSKIFTNPASFDANGNLTVRPyFHSHSCLLCPSNMCKGK 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2047148379 191 ILRDYVMRRTQErGRPFQRVFYVGDGANDFCPSLILGPRDTA 232
Cdd:cd16418    90 VLEEYVASRAQD-SVHYERVIYVGDGANDFCPVLRLRKGDVA 130
DKMTPPase-SF TIGR01489
2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This phosphatase is a member of the IB ...
 37-235 6.21e-47

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: 155.28  E-value: 6.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379  37 FLIFFDFDETIVDESSDDVVVQAAPGQNLPTWLKDTYRPGHYNEYMQRVLAYMAEKGVNESAIRSVIEKIPASPGMLALF 116
Cdd:TIGR01489   2 VVVVSDFDGTITLNDSDDWITDKFGPPEANRLLDGVLSKTLSIKFMDRRMKGLLPSGLKEDEILEVLKSAPIDPGFKEFI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379 117 QFLRHcppQDFEVVLVSDANTFFIESWLRRVGARQLFVKIFTNPATFDKDGRLVLRPFHSHSCLRCPENMCKqvilrDYV 196
Cdd:TIGR01489  82 AFIKE---HGIDFIVISDGNDFFIDPVLEGIGEKDVFIEIYSNPASFDNDGRHIVWPHHCHGCCSCPCGCCK-----GKV 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2047148379 197 MRRTQERGRPfqRVFYVGDGANDFCPSLILgprDTAFAR 235
Cdd:TIGR01489 154 IHKLSEPKYQ--HIIYIGDGVTDVCPAKLS---DVVFAK 187
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 38-226 3.27e-27

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: 103.97  E-value: 3.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379  38 LIFFDFDETIVD-ESSDDVVVQAAPGQNLPTWLKDTYRPGhYNEYMQRV-LAYMAEKGVN-ESAIRSVIEKIPA-SPGML 113
Cdd:TIGR01488   1 LAIFDFDGTLTRqDSLIDLLAKLLGTNDEVIELTRLAPSG-RISFEDALgRRLALLHRSRsEEVAKEFLARQVAlRPGAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379 114 ALFQFLRHcppQDFEVVLVSDANTFFIESWLRRVGarqlFVKIFTNPATFDKDGRLVLRPfhshSCLRCPENMCKqvilr 193
Cdd:TIGR01488  80 ELISWLKE---RGIDTVIVSGGFDFFVEPVAEKLG----IDDVFANRLEFDDNGLLTGPI----EGQVNPEGECK----- 143

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2047148379 194 DYVMRRTQ-ERGRPFQRVFYVGDGANDFCPSLIL 226
Cdd:TIGR01488 144 GKVLKELLeESKITLKKIIAVGDSVNDLPMLKLA 177
MtnX COG4359
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase (methionine salvage) [Amino acid ...
 36-237 1.27e-20

2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase (methionine salvage) [Amino acid transport and metabolism];


Pssm-ID: 443493 [Multi-domain]  Cd Length: 209  Bit Score: 87.18  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379  36 RFLIFFDFDETIvdeSSDDVVVQ-----AAPGqnlptW--LKDTYRPGHYN--EYMQRVLAYMaekGVNESAIRSVIEKI 106
Cdd:COG4359     1 KPVIFCDFDGTI---TEKDVIDAilerfAPPG-----WeeIEDDWLAGEISsrECLGRQFALL---PASKEELDALLENI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379 107 PASPGMLAlfqFLRHCPPQDFEVVLVSDANTFFIESWLRRVGARqlFVKIFTNPATFDkDGRLVLRPFHSHSclRCPEN- 185
Cdd:COG4359    70 EIDPGFKE---FVQFCRERGIPLYIVSDGLDFYIEPILERYGLS--DVPIYANRLVFD-GGGIRIEFPYADP--DCSNGc 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2047148379 186 -MCKQVILRDYvmrrtqerGRPFQRVFYVGDGANDFCPSLILgprDTAFARRD 237
Cdd:COG4359   142 gTCKCAVIRKL--------KSDGYKVIYIGDGRSDFCAAKLA---DLVFAKGK 183
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 34-239 5.65e-17

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: 77.57  E-value: 5.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379  34 DRRFLIFFDFDETIVDESSDDVVVQAApGQNLPTWLKDT----------YRPGH--YNEYMQRVLAYMaeKGVNESAIRS 101
Cdd:COG0560     1 RKMRLAVFDLDGTLIAGESIDELARFL-GRRGLVDRREVleevaaiterAMAGEldFEESLRFRVALL--AGLPEEELEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379 102 VIEKIPA-----SPGMLALFQFLRHcppQDFEVVLVSDANTFFIESWLRRVGARQLFvkiftnpAT--FDKDGRLV--LR 172
Cdd:COG0560    78 LAERLFEevprlYPGARELIAEHRA---AGHKVAIVSGGFTFFVEPIAERLGIDHVI-------ANelEVEDGRLTgeVV 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2047148379 173 PFHSHSclrcpenMCKQVILRDYVmrrtQERGRPFQRVFYVGDGAND------------FCPSLILgpRDTAFARRDYP 239
Cdd:COG0560   148 GPIVDG-------EGKAEALRELA----AELGIDLEQSYAYGDSANDlpmleaaglpvaVNPDPAL--REAADRERGWP 213
HAD pfam12710
haloacid dehalogenase-like hydrolase;
39-221 4.28e-10

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 57.93  E-value: 4.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379  39 IFFDFDETIVDESSDDVVVQAAPGQNLPT--------WLKDTYRPGHYNEYMQRVLAYMAEKGVNESAIRSVIEKIPAS- 109
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDlwrallvlLLLALLRLLGRLSRAGARELLRALLAGLPEEDAAELERFVAEv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379 110 ------PGMLALFQFLRHcppQDFEVVLVSDANTFFIESWLRRVGARQLF-VKIFTNPATFDKDGRLVLRPFHSHSCLRC 182
Cdd:pfam12710  81 alprlhPGALELLAAHRA---AGDRVVVVTGGLRPLVEPVLAELGFDEVLaTELEVDDGRFTGELRLIGPPCAGEGKVRR 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2047148379 183 penmckqviLRDYVMRRtqERGRPFQRVFYVGDGANDFC 221
Cdd:pfam12710 158 ---------LRAWLAAR--GLGLDLADSVAYGDSPSDLP 185
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 39-158 1.13e-05

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: 45.40  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379  39 IFFDFDETIVDESSD-----DVVVQAAPGQNLPTWLKDTYRPGHYNEY---------MQRVLAYMAEK-GVNESA----- 98
Cdd:COG1011     4 VLFDLDGTLLDFDPViaealRALAERLGLLDEAEELAEAYRAIEYALWrryergeitFAELLRRLLEElGLDLAEelaea 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2047148379  99 -IRSVIEKIPASPGMLALFQFLRHcppQDFEVVLVSDANTFFIESWLRRVGARQLFVKIFT 158
Cdd:COG1011    84 fLAALPELVEPYPDALELLEALKA---RGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVS 141
HAD_Pase cd07524
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like ...
 39-220 2.68e-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: 44.25  E-value: 2.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379  39 IFFDFDETIVDESSDDvvvqaapgqnlptWLKDTYRPGHYN--EYMQRVLAYMA--EKGVNE-----------SAIRSVI 103
Cdd:cd07524     2 VFCDFDGTITENDNII-------------YLMDEFAPPLEEweALKEGVLSQTLsfREGVGQmfellpsslkdEIIEFLE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379 104 EKIPASPGmlaLFQFLRHCPPQDFEVVLVSDANTFFIESWLRRVGARQlfVKIFTNPATFDKDGRLVLRPFHSHSCLRCp 183
Cdd:cd07524    69 KTAKIRPG---FKEFVAFCQEHGIPFIIVSGGMDFFIEPLLEGLVIEK--IAIYCNGSDFSGEQIHIDWPHECDCTNGC- 142

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2047148379 184 eNMCKQVILRDYVmrrtqeRGRPFqrVFYVGDGANDF 220
Cdd:cd07524   143 -GCCKSSIIRKYS------KPRPF--IIVIGDSVTDL 170
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 38-219 2.77e-04

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: 41.03  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379  38 LIFFDFDETIVDesSDDVVVQAAP--------GQNLPTWLKDTYRPGHYN---------EYMQRVLAYMAEKGVNESAIR 100
Cdd:pfam00702   3 AVVFDLDGTLTD--GEPVVTEAIAelasehplAKAIVAAAEDLPIPVEDFtarlllgkrDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379 101 SVI-----------EKIPASPGMLALFQFLRhcpPQDFEVVLVSDANTFFIESWLRRVGARQLFVKIFtnpaTFDKDGRL 169
Cdd:pfam00702  81 TVVlvellgvialaDELKLYPGAAEALKALK---ERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVI----SGDDVGVG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2047148379 170 VLRPFhshsclrcpenmCKQVILRDYvmrrtqerGRPFQRVFYVGDGAND 219
Cdd:pfam00702 154 KPKPE------------IYLAALERL--------GVKPEEVLMVGDGVND 183
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 39-153 3.69e-04

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; 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, (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 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the 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 related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 40.48  E-value: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379  39 IFFDFDETIVDESSDDVVVQAAPGQNL-PTWLKDTYR-------PGHYNEY---MQRVLAYMAEKGVNESAIRSViEKIP 107
Cdd:TIGR01509   2 ILFDLDGVLVDTEFAIAKLINREELGLvPDELGVSAVgrlelalRRFKAQYgrtISPEDAQLLYKQLFYEQIEEE-AKLK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2047148379 108 ASPGMLalfQFLRHCPPQDFEVVLVSDANtFFIESWLRRVGARQLF 153
Cdd:TIGR01509  81 PLPGVR---ALLEALRARGKKLALLTNSP-RAHKLVLALLGLRDLF 122
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
38-219 4.88e-04

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 40.30  E-value: 4.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379  38 LIFFDFDETIVDeSSDDVV---VQAAPGQNLPTWLKDTYR-------------------PGHYNEYMQRVLAYMAEKGvn 95
Cdd:COG0546     3 LVLFDLDGTLVD-SAPDIAaalNEALAELGLPPLDLEELRaliglglrellrrllgedpDEELEELLARFRELYEEEL-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379  96 esairsvIEKIPASPGMLALFQFLRHcppQDFEVVLVSDANTFFIESWLRRVGARQLFVKIFTnpatfdkdGRLVLRPFH 175
Cdd:COG0546    80 -------LDETRLFPGVRELLEALKA---RGIKLAVVTNKPREFAERLLEALGLDDYFDAIVG--------GDDVPPAKP 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2047148379 176 SHSCLRcpenmckqvilrdYVMRRTqerGRPFQRVFYVGDGAND 219
Cdd:COG0546   142 KPEPLL-------------EALERL---GLDPEEVLMVGDSPHD 169
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 38-219 4.95e-03

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: 37.32  E-value: 4.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379  38 LIFFDFDETIVDESSDDVVVQAAPGQN-LPTWLKDT-YRPGhYNEYMQRVLAYMAE---------KGVNESAIRSVIEKI 106
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNiLFEELRLPkVLAR-FEFFLNRGLDYMAYyrafaldalAGLLEEDVRAIVEEF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379 107 PAS-------PGMLALFQFLRHCPPQdfeVVLVSDANTFFIESWLRRVGARQLFVKIFTNpatfDKDGRLVLRpfhshsc 179
Cdd:TIGR01490  80 VNQkiesilyPEARDLIRWHKAEGHT---IVLVSASLTILVKPLARILGIDNAIGTRLEE----SEDGIYTGN------- 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2047148379 180 LRCPENMCKQVILRdyVMRRTQERGRPFQRVFYVGDGAND 219
Cdd:TIGR01490 146 IDGNNCKGEGKVHA--LAELLAEEQIDLKDSYAYGDSISD 183
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 112-220 5.61e-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: 35.83  E-value: 5.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047148379 112 MLALFQFLRhcpPQDFEVVLVSDANTFFIESWLRRVGARQLFVKIFTNPATFDKDGRlvlrpfhshsclrcpenmckqvi 191
Cdd:cd01427    12 AVELLKRLR---AAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPK----------------------- 65

                          90       100
                  ....*....|....*....|....*....
gi 2047148379 192 lRDYVMRRTQERGRPFQRVFYVGDGANDF 220
Cdd:cd01427    66 -PKPLLLLLLKLGVDPEEVLFVGDSENDI 93
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH