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Conserved domains on  [gi|665404093|ref|NP_001285559|]
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uncharacterized protein Dmel_CG5556, isoform B [Drosophila melanogaster]

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

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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 ...
 40-249 6.73e-35

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 PLN02811:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 220  Bit Score: 125.64  E-value: 6.73e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  40 DTRHVYKRAVIELAASYNKIIPEAVLIKSGPMETAEMAELICRKCDLP--VSWESFrfqLNERTS---DLIANPTLMPGV 114
Cdd:PLN02811   7 DTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSdsLSPEDF---LVEREAmlqDLFPTSDLMPGA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093 115 ERLVTHLGRCCMGLGLITSCSESMYCTKIRDREDFFQNFSSVICADDADLKAPKPEPDVYLIAMRR--LGDAGPDCTLVF 192
Cdd:PLN02811  84 ERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAPDIFLAAARRfeDGPVDPGKVLVF 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 665404093 193 DGTPKGVQAATDARLPVVMLAEKDLPCCWSELATLRLETLEEFDPAEFNMPPYSCTE 249
Cdd:PLN02811 164 EDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEEWGLPPFPDSS 220
 
Name Accession Description Interval E-value
PLN02811 PLN02811
hydrolase
 40-249 6.73e-35

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 125.64  E-value: 6.73e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  40 DTRHVYKRAVIELAASYNKIIPEAVLIKSGPMETAEMAELICRKCDLP--VSWESFrfqLNERTS---DLIANPTLMPGV 114
Cdd:PLN02811   7 DTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSdsLSPEDF---LVEREAmlqDLFPTSDLMPGA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093 115 ERLVTHLGRCCMGLGLITSCSESMYCTKIRDREDFFQNFSSVICADDADLKAPKPEPDVYLIAMRR--LGDAGPDCTLVF 192
Cdd:PLN02811  84 ERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAPDIFLAAARRfeDGPVDPGKVLVF 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 665404093 193 DGTPKGVQAATDARLPVVMLAEKDLPCCWSELATLRLETLEEFDPAEFNMPPYSCTE 249
Cdd:PLN02811 164 EDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEEWGLPPFPDSS 220
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 27-211 6.98e-30

subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and Gpp2; This subfamily includes Arabidopsis thaliana AtGpp1 and AtGpp2, and Drosophila GS1-like protein (Dmel\Gs1l) of unknown function. AtGpp1 and AtGpp2 are constitutively expressed in all the Arabidopsis tissues and unaffected under abiotic stress. Overexpression of AtGpp2 in transgenic Arabidopsis plants increases the specific DL-glycerol-3-phosphatase activity and improves the plants tolerance to salt, osmotic and oxidative stress. 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: 319831 [Multi-domain]  Cd Length: 192  Bit Score: 111.67  E-value: 6.98e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  27 ISYCIFDLESAVFDTRHVYKRAVIELAASYNKIIPEAVLIKSGPMETAEMAELICRKCDLPVSW-ESFRFQLNERTSDLI 105
Cdd:cd07529    1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLeEEFDEQQEALAELFM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093 106 ANPTLMPGVERLVTHLGRCCMGLGLITSCSESMYCTKIRDREDFFQNFSSVICADDADLKAP-KPEPDVYLIAMRRLGD- 183
Cdd:cd07529   81 GTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVKGRgKPAPDIFLVAAKRFNEp 160

                        170       180
                 ....*....|....*....|....*....
gi 665404093 184 -AGPDCTLVFDGTPKGVQAATDARLPVVM 211
Cdd:cd07529  161 pKDPSKCLVFEDSPNGVKAAKAAGMQVVM 189
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
30-235 2.59e-27

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 105.29  E-value: 2.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  30 CIFDLESAVFDTRHVYKRAVIELAASYNKIIPEAVLIKSGPMETAEMAELICRKCDLPVSWESFRFQLNERTSDLIANP- 108
Cdd:COG0637    5 VIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELLAEEg 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093 109 -TLMPGVERLVTHLGRCCMGLGLITSCSESMyCTKIRDREDFFQNFSSVICADDadLKAPKPEPDVYLIAMRRLGdAGPD 187
Cdd:COG0637   85 lPLIPGVVELLEALKEAGIKIAVATSSPREN-AEAVLEAAGLLDYFDVIVTGDD--VARGKPDPDIYLLAAERLG-VDPE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 665404093 188 CTLVFDGTPKGVQAATDARLPVVMLAEKDLPCCWSELATLRLETLEEF 235
Cdd:COG0637  161 ECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 30-212 4.47e-13

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: 66.29  E-value: 4.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093   30 CIFDLESAVFDTRHVYKRAVielAASYNKIIPEAVLIKSGPMETaEMAELICRKCDLPVSWESFR-FQLNERTSDLI--A 106
Cdd:TIGR01509   2 ILFDLDGVLVDTEFAIAKLI---NREELGLVPDELGVSAVGRLE-LALRRFKAQYGRTISPEDAQlLYKQLFYEQIEeeA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  107 NPTLMPGVERLVTHLGRCCMGLGLITScSESMYCTKIRdREDFFQNFSSVICADDadLKAPKPEPDVYLIAMRRLGDAgP 186
Cdd:TIGR01509  78 KLKPLPGVRALLEALRARGKKLALLTN-SPRAHKLVLA-LLGLRDLFDVVIDSSD--VGLGKPDPDIYLQALKALGLE-P 152

                         170       180
                  ....*....|....*....|....*.
gi 665404093  187 DCTLVFDGTPKGVQAATDARLPVVML 212
Cdd:TIGR01509 153 SECVFVDDSPAGIEAAKAAGMHTVGV 178
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
30-211 1.00e-05

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 45.27  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093   30 CIFDLESAVFDTRHVYKRAVIELAASYNKII--PEAVLIKSGPmETAEMAELICRKCDLPVSWESFRFQLNERTSDLiaN 107
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGElsEEEILKFIGL-PLREIFRYLGVSEDEEEKIEFYLRKYNEELHDK--L 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  108 PTLMPGVERLVTHLGRCCMGLGLITSCS--ESMYCTKIRDREDFFQnfsSVICADDadLKAPKPEPDVYLIAMRRLGdAG 185
Cdd:pfam13419  78 VKPYPGIKELLEELKEQGYKLGIVTSKSreNVEEFLKQLGLEDYFD---VIVGGDD--VEGKKPDPDPILKALEQLG-LK 151

                         170       180
                  ....*....|....*....|....*.
gi 665404093  186 PDCTLVFDGTPKGVQAATDARLPVVM 211
Cdd:pfam13419 152 PEEVIYVGDSPRDIEAAKNAGIKVIA 177
 
Name Accession Description Interval E-value
PLN02811 PLN02811
hydrolase
 40-249 6.73e-35

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 125.64  E-value: 6.73e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  40 DTRHVYKRAVIELAASYNKIIPEAVLIKSGPMETAEMAELICRKCDLP--VSWESFrfqLNERTS---DLIANPTLMPGV 114
Cdd:PLN02811   7 DTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSdsLSPEDF---LVEREAmlqDLFPTSDLMPGA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093 115 ERLVTHLGRCCMGLGLITSCSESMYCTKIRDREDFFQNFSSVICADDADLKAPKPEPDVYLIAMRR--LGDAGPDCTLVF 192
Cdd:PLN02811  84 ERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAPDIFLAAARRfeDGPVDPGKVLVF 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 665404093 193 DGTPKGVQAATDARLPVVMLAEKDLPCCWSELATLRLETLEEFDPAEFNMPPYSCTE 249
Cdd:PLN02811 164 EDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEEWGLPPFPDSS 220
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 27-211 6.98e-30

subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and Gpp2; This subfamily includes Arabidopsis thaliana AtGpp1 and AtGpp2, and Drosophila GS1-like protein (Dmel\Gs1l) of unknown function. AtGpp1 and AtGpp2 are constitutively expressed in all the Arabidopsis tissues and unaffected under abiotic stress. Overexpression of AtGpp2 in transgenic Arabidopsis plants increases the specific DL-glycerol-3-phosphatase activity and improves the plants tolerance to salt, osmotic and oxidative stress. 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: 319831 [Multi-domain]  Cd Length: 192  Bit Score: 111.67  E-value: 6.98e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  27 ISYCIFDLESAVFDTRHVYKRAVIELAASYNKIIPEAVLIKSGPMETAEMAELICRKCDLPVSW-ESFRFQLNERTSDLI 105
Cdd:cd07529    1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLeEEFDEQQEALAELFM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093 106 ANPTLMPGVERLVTHLGRCCMGLGLITSCSESMYCTKIRDREDFFQNFSSVICADDADLKAP-KPEPDVYLIAMRRLGD- 183
Cdd:cd07529   81 GTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVKGRgKPAPDIFLVAAKRFNEp 160

                        170       180
                 ....*....|....*....|....*....
gi 665404093 184 -AGPDCTLVFDGTPKGVQAATDARLPVVM 211
Cdd:cd07529  161 pKDPSKCLVFEDSPNGVKAAKAAGMQVVM 189
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
30-235 2.59e-27

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 105.29  E-value: 2.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  30 CIFDLESAVFDTRHVYKRAVIELAASYNKIIPEAVLIKSGPMETAEMAELICRKCDLPVSWESFRFQLNERTSDLIANP- 108
Cdd:COG0637    5 VIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELLAEEg 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093 109 -TLMPGVERLVTHLGRCCMGLGLITSCSESMyCTKIRDREDFFQNFSSVICADDadLKAPKPEPDVYLIAMRRLGdAGPD 187
Cdd:COG0637   85 lPLIPGVVELLEALKEAGIKIAVATSSPREN-AEAVLEAAGLLDYFDVIVTGDD--VARGKPDPDIYLLAAERLG-VDPE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 665404093 188 CTLVFDGTPKGVQAATDARLPVVMLAEKDLPCCWSELATLRLETLEEF 235
Cdd:COG0637  161 ECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 87-213 1.31e-17

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family 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. It 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: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 77.66  E-value: 1.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  87 PVSWESFRF--QLNERTSDLIA--NPTLMPGVERLVTHLGRCCMGLGLITSCSESMYCTKIRDREDFFQNFSSVICADDa 162
Cdd:cd07505   15 PLHRQAWQLleRKNALLLELIAseGLKLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYFDVIVSGDD- 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 665404093 163 dLKAPKPEPDVYLIAMRRLGDAGPDCtLVFDGTPKGVQAATDARLPVVMLA 213
Cdd:cd07505   94 -VERGKPAPDIYLLAAERLGVDPERC-LVFEDSLAGIEAAKAAGMTVVAVP 142
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 30-212 4.47e-13

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: 66.29  E-value: 4.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093   30 CIFDLESAVFDTRHVYKRAVielAASYNKIIPEAVLIKSGPMETaEMAELICRKCDLPVSWESFR-FQLNERTSDLI--A 106
Cdd:TIGR01509   2 ILFDLDGVLVDTEFAIAKLI---NREELGLVPDELGVSAVGRLE-LALRRFKAQYGRTISPEDAQlLYKQLFYEQIEeeA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  107 NPTLMPGVERLVTHLGRCCMGLGLITScSESMYCTKIRdREDFFQNFSSVICADDadLKAPKPEPDVYLIAMRRLGDAgP 186
Cdd:TIGR01509  78 KLKPLPGVRALLEALRARGKKLALLTN-SPRAHKLVLA-LLGLRDLFDVVIDSSD--VGLGKPDPDIYLQALKALGLE-P 152

                         170       180
                  ....*....|....*....|....*.
gi 665404093  187 DCTLVFDGTPKGVQAATDARLPVVML 212
Cdd:TIGR01509 153 SECVFVDDSPAGIEAAKAAGMHTVGV 178
PLN02940 PLN02940
riboflavin kinase
 27-246 4.98e-13

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 68.71  E-value: 4.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  27 ISYCIFDLESAVFDTRHVYKRAVIELAASYNKIIPEAVLIKSGPMETAEMAELICRKCDLPVSWESFRFQLNERTSDLIA 106
Cdd:PLN02940  11 VSHVILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQKIVGKTPLEAAATVVEDYGLPCSTDEFNSEITPLLSEQWC 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093 107 NPTLMPGVERLVTHLGRCCMGLGLITSCSESMYCTKIRDREDFFQNFSSVICADdaDLKAPKPEPDVYLIAMRRLGDAGP 186
Cdd:PLN02940  91 NIKALPGANRLIKHLKSHGVPMALASNSPRANIEAKISCHQGWKESFSVIVGGD--EVEKGKPSPDIFLEAAKRLNVEPS 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665404093 187 DCtLVFDGTPKGVQAATDARLPVVmlAEKDLPCCWSEL--ATLRLETLEEFDPAEFNMPPYS 246
Cdd:PLN02940 169 NC-LVIEDSLPGVMAGKAAGMEVI--AVPSIPKQTHLYssADEVINSLLDLQPEKWGLPPFN 227
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 27-235 2.88e-11

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: 61.97  E-value: 2.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  27 ISYCIFDLESAVFDTRHVYKRAVIELAASYNKIIPEAVLIK--------------SGPMETAEMAELICRKCDLPVSWES 92
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEayraieyalwrryeRGEITFAELLRRLLEELGLDLAEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  93 FRFQLNERTSDLianpTLMPGVERLVTHLGRCCMGLGLITSCSESMYCTKIRdREDFFQNFSSVICADDadLKAPKPEPD 172
Cdd:COG1011   81 AEAFLAALPELV----EPYPDALELLEALKARGYRLALLTNGSAELQEAKLR-RLGLDDLFDAVVSSEE--VGVRKPDPE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665404093 173 VYLIAMRRLGdAGPDCTLVFDGTPKG-VQAATDARLPVVMLAEKDLPCCWSELATLRLETLEEF 235
Cdd:COG1011  154 IFELALERLG-VPPEEALFVGDSPETdVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAEL 216
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 87-210 2.41e-10

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: 58.42  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  87 PVSWESFRFQLNERTSDLIA-------NPTLMPGVERLVTHLGRccMGLGLITSCSESMYCTKIR-DREDFFQNFSSVIC 158
Cdd:cd16423   15 PLWYEAWQELLNERRNELIKrqfsektDLPPIEGVKELLEFLKE--KGIKLAVASSSPRRWIEPHlERLGLLDYFEVIVT 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 665404093 159 ADDadLKAPKPEPDVYLIAMRRLGDAGPDCtLVFDGTPKGVQAATDARLPVV 210
Cdd:cd16423   93 GDD--VEKSKPDPDLYLEAAERLGVNPEEC-VVIEDSRNGVLAAKAAGMKCV 141
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
31-235 5.48e-10

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 58.02  E-value: 5.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  31 IFDLESAVFDTRHVYKRAVIELAASYNKIIPEAVLIKS--GPMETAEMAELIcrKCDLPVSWESFRFQLNER-TSDLIAN 107
Cdd:COG0546    5 LFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRAliGLGLRELLRRLL--GEDPDEELEELLARFRELyEEELLDE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093 108 PTLMPGVERLVTHLGRCCMGLGLITSCSESmYCTKIRDREDFFQNFSSVICADDadLKAPKPEPDVYLIAMRRLGDAGPD 187
Cdd:COG0546   83 TRLFPGVRELLEALKARGIKLAVVTNKPRE-FAERLLEALGLDDYFDAIVGGDD--VPPAKPKPEPLLEALERLGLDPEE 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 665404093 188 CTLVFDgTPKGVQAATDARLPVVMLA-----EKDLpccWSELATLRLETLEEF 235
Cdd:COG0546  160 VLMVGD-SPHDIEAARAAGVPFIGVTwgygsAEEL---EAAGADYVIDSLAEL 208
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 110-211 1.11e-09

subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides xylulose-1,5-bisphosphate phosphatase CbbY; This family includes Rhodobacter sphaeroides and Arabidopsis thaliana xylulose-1,5-bisphosphate phosphatase CbbY which convert xylulose-1,5-bisphosphate (a potent inhibitor of Ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco), to the non-inhibitory compound xylulose-5-phosphate. 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: 319830 [Multi-domain]  Cd Length: 199  Bit Score: 57.00  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093 110 LMPGVERLVTHLGRCCMGLGLITSCSESMYCTKIRD--REDFFQNFSSVICADDADLKapKPEPDVYLIAMRRLGDAGPD 187
Cdd:cd07528   96 LRPGVARLIDEAKAAGVRLAIATTTSPANVDALLSAllGPERRAIFDAIAAGDDVAEK--KPDPDIYLLALERLGVSPSD 173

                         90       100
                 ....*....|....*....|....
gi 665404093 188 CtLVFDGTPKGVQAATDARLPVVM 211
Cdd:cd07528  174 C-LAIEDSAIGLQAAKAAGLPCIV 196
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 31-210 1.22e-06

beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include 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: 319788 [Multi-domain]  Cd Length: 174  Bit Score: 47.67  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  31 IFDLESAVFDTRHVYKRAVIELAasynkiipeavliksgpmETAEMAElicRKCDLPVSwesfrfQLNERTSdliaNPTL 110
Cdd:cd02598    3 IFDLDGVITDTAEYHYRAWKKLA------------------DKEELAA---RKNRIYVE------LIEELTP----VDVL 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093 111 mPGVERLVTHLGRCCMGLGLitsCSESMYCTKIRDR---EDFFQnfssvICADDADLKAPKPEPDVYLIAMRRLGDAGPD 187
Cdd:cd02598   52 -PGIASLLVDLKAKGIKIAL---ASASKNAPKILEKlglAEYFD-----AIVDGAVLAKGKPDPDIFLAAAEGLGLNPKD 122

                        170       180
                 ....*....|....*....|...
gi 665404093 188 CtLVFDGTPKGVQAATDARLPVV 210
Cdd:cd02598  123 C-IGVEDAQAGIRAIKAAGFLVV 144
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 153-243 1.69e-06

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 48.49  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093 153 FSSVICADDadLKAPKPEPDVYLIAMRRLGDAgPDCTLVFDGTPKGVQAATDARL---------PVVMLAEKDLPCC-WS 222
Cdd:PLN03243 152 FSVVLAAED--VYRGKPDPEMFMYAAERLGFI-PERCIVFGNSNSSVEAAHDGCMkcvavagkhPVYELSAGDLVVRrLD 228

                         90       100
                 ....*....|....*....|.
gi 665404093 223 ELATLRLETLEEFDPAEFNMP 243
Cdd:PLN03243 229 DLSVVDLKNLSDLDSPEFQIP 249
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 163-205 8.66e-06

subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli 6-phosphogluconate phosphatase YieH; This subfamily includes Escherichia coli YieH/HAD3 an 6-phosphogluconate phosphatase, which can hydrolyzed purines and pyrimidines as secondary substrates. 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. 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: 319828 [Multi-domain]  Cd Length: 141  Bit Score: 44.62  E-value: 8.66e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 665404093 163 DLKAPKPEPDVYLIAMRRLGdAGPDCTLVFDGTPKGVQAATDA 205
Cdd:cd07526   91 DVGRGKPAPDLFLHAAAQMG-VAPERCLVIEDSPTGVRAALAA 132
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
30-211 1.00e-05

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 45.27  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093   30 CIFDLESAVFDTRHVYKRAVIELAASYNKII--PEAVLIKSGPmETAEMAELICRKCDLPVSWESFRFQLNERTSDLiaN 107
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGElsEEEILKFIGL-PLREIFRYLGVSEDEEEKIEFYLRKYNEELHDK--L 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  108 PTLMPGVERLVTHLGRCCMGLGLITSCS--ESMYCTKIRDREDFFQnfsSVICADDadLKAPKPEPDVYLIAMRRLGdAG 185
Cdd:pfam13419  78 VKPYPGIKELLEELKEQGYKLGIVTSKSreNVEEFLKQLGLEDYFD---VIVGGDD--VEGKKPDPDPILKALEQLG-LK 151

                         170       180
                  ....*....|....*....|....*.
gi 665404093  186 PDCTLVFDGTPKGVQAATDARLPVVM 211
Cdd:pfam13419 152 PEEVIYVGDSPRDIEAAKNAGIKVIA 177
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 30-202 1.03e-05

subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p); This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong 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), 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: 319829 [Multi-domain]  Cd Length: 205  Bit Score: 45.41  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  30 CIFDLESAVFDTRHVYKRAVIELAASYNkIIPEAVLIKSGPMETAEMAELICrkcDLPVSWESFRFQLNERTSDLIANPT 109
Cdd:cd07527    2 LLFDMDGTLVDSTPAVERAWHKWAKEHG-VDPEEVLKVSHGRRAIDVIRKLA---PDDADIELVLALETEEPESYPEGVI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093 110 LMPGVERLVTHLGRCCMGLGLITSCSESMyctkIRDREDFFQNF--SSVICADDadLKAPKPEPDVYLIAMRRLGDAGPD 187
Cdd:cd07527   78 AIPGAVDLLASLPAAGDRWAIVTSGTRAL----AEARLEAAGLPhpEVLVTADD--VKNGKPDPEPYLLGAKLLGLDPSD 151

                        170
                 ....*....|....*
gi 665404093 188 CtLVFDGTPKGVQAA 202
Cdd:cd07527  152 C-VVFEDAPAGIKAG 165
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 30-205 3.56e-05

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: 43.73  E-value: 3.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093   30 CIFDLESAVFDTRHVYKRAVIELAASYNKIIPEAVLIKSGPMETAEMAELICRKCDLPVSWESFRFQLNERTSD------ 103
Cdd:pfam00702   4 VVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAegltvv 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  104 ---------LIANPTLMPGVERLVTHLGRccMG--LGLITSCSESMYcTKIRDREDFFQNFSSVICADDadLKAPKPEPD 172
Cdd:pfam00702  84 lvellgviaLADELKLYPGAAEALKALKE--RGikVAILTGDNPEAA-EALLRLLGLDDYFDVVISGDD--VGVGKPKPE 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 665404093  173 VYLIAMRRLGdAGPDCTLVFDGTPKGVQAATDA 205
Cdd:pfam00702 159 IYLAALERLG-VKPEEVLMVGDGVNDIPAAKAA 190
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
153-210 6.42e-05

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 42.75  E-value: 6.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 665404093 153 FSSVICADDadLKAPKPEPDVYLIAMRRLGDAGPDCtLVFDGTPKGVQAATDARLPVV 210
Cdd:PRK10725 129 FDAVVAADD--VQHHKPAPDTFLRCAQLMGVQPTQC-VVFEDADFGIQAARAAGMDAV 183
PRK11587 PRK11587
putative phosphatase; Provisional
 109-210 6.44e-04

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 40.36  E-value: 6.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093 109 TLMPGVERLVTHLGRCCMGLGLITSCSesMYCTKIRDREdffqnfssvicaddADLKAP------------KPEPDVYLI 176
Cdd:PRK11587  83 TALPGAIALLNHLNKLGIPWAIVTSGS--VPVASARHKA--------------AGLPAPevfvtaervkrgKPEPDAYLL 146

                         90       100       110
                 ....*....|....*....|....*....|....
gi 665404093 177 AMRRLGDAGPDCTLVFDGtPKGVQAATDARLPVV 210
Cdd:PRK11587 147 GAQLLGLAPQECVVVEDA-PAGVLSGLAAGCHVI 179
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 31-193 3.01e-03

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


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 37.76  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093   31 IFDLESAVFDTRHVYKRAVIELAASYNKIIPEAVLIKSGPMETAEMAELICrkcdlPVSWESFRfqlNERTSDLIANPTL 110
Cdd:TIGR01549   3 LFDIDGTLVDIKFAIRRAFPQTFEEFGLDPASFKALKQAGGLAEEEWYRIA-----TSALEELQ---GRFWSEYDAEEAY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093  111 MPGVERLVTHLGRCCMGLGLITSCSESMYcTKIRDREDFFQNFSSVICADDAdlkAPKPEPDVYLIAMRRLGdAGPDCTL 190
Cdd:TIGR01549  75 IRGAADLLARLKSAGIKLGIISNGSLRAQ-KLLLRLFGLGDYFELILVSDEP---GSKPEPEIFLAALESLG-VPPEVLH 149


                  ...
gi 665404093  191 VFD 193
Cdd:TIGR01549 150 VGD 152
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 153-214 3.74e-03

haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. 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: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 38.07  E-value: 3.74e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665404093 153 FSSVICADDADLKAPKPEPdvYLIAMRRLGDAGPDCTLVFDgTPKGVQAATDARLPVVMLAE 214
Cdd:cd07512  129 FAAVVGGDTLPQRKPDPAP--LRAAIRRLGGDVSRALMVGD-SETDAATARAAGVPFVLVTF 187
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 153-243 5.97e-03

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 37.92  E-value: 5.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404093 153 FSSVICADDadLKAPKPEPDVYLIAMRRLgDAGPDCTLVFDGTPKGVQAATDARLPVVMLAEK---------DLPC-CWS 222
Cdd:PLN02575 259 FSVIVAAED--VYRGKPDPEMFIYAAQLL-NFIPERCIVFGNSNQTVEAAHDARMKCVAVASKhpiyelgaaDLVVrRLD 335

                         90       100
                 ....*....|....*....|.
gi 665404093 223 ELATLRLETLEEFDPAEFNMP 243
Cdd:PLN02575 336 ELSIVDLKNLADIESPEFGPP 356
 
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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