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Conserved domains on  [gi|296011030|ref|NP_001171607|]
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pseudouridine-5'-phosphatase isoform d [Homo sapiens]

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 ...
 8-153 2.82e-87

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 cd07529:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 192  Bit Score: 254.19  E-value: 2.82e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   8 VTHLIFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMG------------------------------------ 51
Cdd:cd07529    1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGrpaseaariivdelklpmsleeefdeqqealaelfm 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  52 --------AEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEV-QHGKPDPDIFLACAKRFSPP 122
Cdd:cd07529   81 gtaklmpgAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVkGRGKPAPDIFLVAAKRFNEP 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 296011030 123 PA-MEKCLVFEDAPNGVEAALAAGMQVVMVPD 153
Cdd:cd07529  161 PKdPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
 
Name Accession Description Interval E-value
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 8-153 2.82e-87

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: 254.19  E-value: 2.82e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   8 VTHLIFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMG------------------------------------ 51
Cdd:cd07529    1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGrpaseaariivdelklpmsleeefdeqqealaelfm 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  52 --------AEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEV-QHGKPDPDIFLACAKRFSPP 122
Cdd:cd07529   81 gtaklmpgAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVkGRGKPAPDIFLVAAKRFNEP 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 296011030 123 PA-MEKCLVFEDAPNGVEAALAAGMQVVMVPD 153
Cdd:cd07529  161 PKdPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
PLN02811 PLN02811
hydrolase
 15-185 6.91e-77

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 229.26  E-value: 6.91e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  15 MDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMG------------------------------------------- 51
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGkkaieaarifveesglsdslspedflvereamlqdlfptsdlm 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  52 --AEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEVQHGKPDPDIFLACAKRFS-PPPAMEKC 128
Cdd:PLN02811  81 pgAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAPDIFLAAARRFEdGPVDPGKV 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 296011030 129 LVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQDFQPELFGLPSYE 185
Cdd:PLN02811 161 LVFEDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEEWGLPPFP 217
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
11-174 2.02e-45

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 148.43  E-value: 2.02e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  11 LIFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMG--------------------------------------- 51
Cdd:COG0637    5 VIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGrsredilrylleeygldlpeeelaarkeelyrellaeeg 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  52 ------AEKLIIHLRKHGIPFALATSSGSASFDMKTSRHkEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPam 125
Cdd:COG0637   85 lplipgVVELLEALKEAGIKIAVATSSPRENAEAVLEAA-GLLDYFDVIVTGDD--VARGKPDPDIYLLAAERLGVDP-- 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 296011030 126 EKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQDF 174
Cdd:COG0637  160 EECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 11-151 4.19e-26

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 98.18  E-value: 4.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   11 LIFDMDGLLLDTERL-----------YSVVF-----------------QEICNRYDKKYSwDVKSLVMGAEK-------- 54
Cdd:TIGR02009   4 VIFDMDGVITDTAPLhaqawkhiaakYGISFdkqyneslkglsredilRAILKLRGDGLS-LEEIHQLAERKnelyrell 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   55 -------------LIIHLRKHGIPFALATSSGSASFDMKTSrhkEFFSLFSHIVLGDdpEVQHGKPDPDIFLACAKRFSP 121
Cdd:TIGR02009  83 rltgvavlpgirnLLKRLKAKGIAVGLGSSSKNAPRILAKL---GLRDYFDAIVDAS--EVKNGKPHPETFLLAAELLGV 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 296011030  122 PPamEKCLVFEDAPNGVEAALAAGMQVVMV 151
Cdd:TIGR02009 158 PP--NECIVFEDALAGVQAARAAGMFAVAV 185
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
11-151 2.11e-20

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 83.40  E-value: 2.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   11 LIFDMDGLLLDTERLYSVVFQEICNRYD----------KKYSWDVKSLVM------------------------------ 50
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGygelseeeilKFIGLPLREIFRylgvsedeeekiefylrkyneelhdklvkp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   51 --GAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKeFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPamEKC 128
Cdd:pfam13419  81 ypGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLG-LEDYFDVIVGGDD--VEGKKPDPDPILKALEQLGLKP--EEV 155

                         170       180
                  ....*....|....*....|...
gi 296011030  129 LVFEDAPNGVEAALAAGMQVVMV 151
Cdd:pfam13419 156 IYVGDSPRDIEAAKNAGIKVIAV 178
 
Name Accession Description Interval E-value
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 8-153 2.82e-87

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: 254.19  E-value: 2.82e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   8 VTHLIFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMG------------------------------------ 51
Cdd:cd07529    1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGrpaseaariivdelklpmsleeefdeqqealaelfm 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  52 --------AEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEV-QHGKPDPDIFLACAKRFSPP 122
Cdd:cd07529   81 gtaklmpgAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVkGRGKPAPDIFLVAAKRFNEP 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 296011030 123 PA-MEKCLVFEDAPNGVEAALAAGMQVVMVPD 153
Cdd:cd07529  161 PKdPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
PLN02811 PLN02811
hydrolase
 15-185 6.91e-77

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 229.26  E-value: 6.91e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  15 MDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMG------------------------------------------- 51
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGkkaieaarifveesglsdslspedflvereamlqdlfptsdlm 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  52 --AEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEVQHGKPDPDIFLACAKRFS-PPPAMEKC 128
Cdd:PLN02811  81 pgAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAPDIFLAAARRFEdGPVDPGKV 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 296011030 129 LVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQDFQPELFGLPSYE 185
Cdd:PLN02811 161 LVFEDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEEWGLPPFP 217
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 11-153 7.12e-50

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: 157.78  E-value: 7.12e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  11 LIFDMDGLLLDTERLYSVVFQEIcNRYDKKYSWDVKSLVM----GAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKE 86
Cdd:cd07505    2 VIFDMDGVLIDTEPLHRQAWQLL-ERKNALLLELIASEGLklkpGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296011030  87 FFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMVPD 153
Cdd:cd07505   81 LRGYFDVIVSGDD--VERGKPAPDIYLLAAERLGVDP--ERCLVFEDSLAGIEAAKAAGMTVVAVPD 143
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
11-174 2.02e-45

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 148.43  E-value: 2.02e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  11 LIFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMG--------------------------------------- 51
Cdd:COG0637    5 VIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGrsredilrylleeygldlpeeelaarkeelyrellaeeg 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  52 ------AEKLIIHLRKHGIPFALATSSGSASFDMKTSRHkEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPam 125
Cdd:COG0637   85 lplipgVVELLEALKEAGIKIAVATSSPRENAEAVLEAA-GLLDYFDVIVTGDD--VARGKPDPDIYLLAAERLGVDP-- 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 296011030 126 EKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQDF 174
Cdd:COG0637  160 EECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
PLN02940 PLN02940
riboflavin kinase
 1-185 1.06e-42

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 146.52  E-value: 1.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   1 MAAP---PQPVTHLIFDMDGLLLDTERLYSVVFQEICNRYDKKysWD--------------------------------- 44
Cdd:PLN02940   1 MSAAkplKKLVSHVILDLDGTLLNTDGIVSDVLKAFLVKYGKQ--WDgreaqkivgktpleaaatvvedyglpcstdefn 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  45 -------------VKSLVmGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDdpEVQHGKPDPDI 111
Cdd:PLN02940  79 seitpllseqwcnIKALP-GANRLIKHLKSHGVPMALASNSPRANIEAKISCHQGWKESFSVIVGGD--EVEKGKPSPDI 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296011030 112 FLACAKRFSPPPAmeKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQDFQPELFGLPSYE 185
Cdd:PLN02940 156 FLEAAKRLNVEPS--NCLVIEDSLPGVMAGKAAGMEVIAVPSIPKQTHLYSSADEVINSLLDLQPEKWGLPPFN 227
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 11-173 1.37e-36

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: 124.67  E-value: 1.37e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  11 LIFDMDGLLLDTERLYSVVFQEICNRYD----KKYSWDVKSLVM--GAEKLIIHLRKHGIPFALATSSgSASFDMKTSRH 84
Cdd:cd16423    2 VIFDFDGVIVDTEPLWYEAWQELLNERRneliKRQFSEKTDLPPieGVKELLEFLKEKGIKLAVASSS-PRRWIEPHLER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  85 KEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKA 164
Cdd:cd16423   81 LGLLDYFEVIVTGDD--VEKSKPDPDLYLEAAERLGVNP--EECVVIEDSRNGVLAAKAAGMKCVGVPNPVTGSQDFSKA 156


                 ....*....
gi 296011030 165 TLVLNSLQD 173
Cdd:cd16423  157 DLVLSSFAE 165
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 11-151 4.19e-26

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 98.18  E-value: 4.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   11 LIFDMDGLLLDTERL-----------YSVVF-----------------QEICNRYDKKYSwDVKSLVMGAEK-------- 54
Cdd:TIGR02009   4 VIFDMDGVITDTAPLhaqawkhiaakYGISFdkqyneslkglsredilRAILKLRGDGLS-LEEIHQLAERKnelyrell 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   55 -------------LIIHLRKHGIPFALATSSGSASFDMKTSrhkEFFSLFSHIVLGDdpEVQHGKPDPDIFLACAKRFSP 121
Cdd:TIGR02009  83 rltgvavlpgirnLLKRLKAKGIAVGLGSSSKNAPRILAKL---GLRDYFDAIVDAS--EVKNGKPHPETFLLAAELLGV 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 296011030  122 PPamEKCLVFEDAPNGVEAALAAGMQVVMV 151
Cdd:TIGR02009 158 PP--NECIVFEDALAGVQAARAAGMFAVAV 185
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 10-151 9.74e-26

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: 97.11  E-value: 9.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   10 HLIFDMDGLLLDTERLY-------------------SVVFQEICNRYDKKYSWDVKS-LVM------------------- 50
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIaklinreelglvpdelgvsAVGRLELALRRFKAQYGRTISpEDAqllykqlfyeqieeeaklk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   51 ---GAEKLIIHLRKHGIPFALATSSgsASFDMKTSRHKEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPamEK 127
Cdd:TIGR01509  81 plpGVRALLEALRARGKKLALLTNS--PRAHKLVLALLGLRDLFDVVIDSSD--VGLGKPDPDIYLQALKALGLEP--SE 154

                         170       180
                  ....*....|....*....|....
gi 296011030  128 CLVFEDAPNGVEAALAAGMQVVMV 151
Cdd:TIGR01509 155 CVFVDDSPAGIEAAKAAGMHTVGV 178
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
11-151 2.37e-23

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 91.29  E-value: 2.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  11 LIFDMDGLLLDTERLYSVVFQEICNRYDKKY------------SW------------DVKSLVMGAEKL----------- 55
Cdd:PRK10725   8 LIFDMDGTILDTEPTHRKAWREVLGRYGLQFdeqamvalngspTWriaqaiielnqaDLDPHALAREKTeavksmlldsv 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  56 ----IIHLRK--HG-IPFALATSSGSASFDMKTsRHKEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPamEKC 128
Cdd:PRK10725  88 eplpLIEVVKawHGrRPMAVGTGSESAIAEALL-AHLGLRRYFDAVVAADD--VQHHKPAPDTFLRCAQLMGVQP--TQC 162

                        170       180
                 ....*....|....*....|...
gi 296011030 129 LVFEDAPNGVEAALAAGMQVVMV 151
Cdd:PRK10725 163 VVFEDADFGIQAARAAGMDAVDV 185
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 11-148 3.34e-23

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: 89.69  E-value: 3.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  11 LIFDMDGLLLDTE----RLYSVVFQEICNRYDKKYSWDVKsLVMGAEKLiihLRKHGIPFALATSSGSASFDMKTSRH-- 84
Cdd:cd07526    3 VIFDCDGVLVDSEviaaRVLVEVLAELGARVLAAFEAELQ-PIPGAAAA---LSALTLPFCVASNSSRERLTHSLGLAgl 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296011030  85 KEFFSlfSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQV 148
Cdd:cd07526   79 LAYFE--GRIFSASD--VGRGKPAPDLFLHAAAQMGVAP--ERCLVIEDSPTGVRAALAAGMTV 136
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 12-151 1.13e-21

beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 86.98  E-value: 1.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   12 IFDMDGLLLDTERLY-----------SVVFQE-----------------ICNRYDKKYS--------------------- 42
Cdd:TIGR01990   3 IFDLDGVITDTAEYHylawkhladelGIPFDEefneslkgvsreeslerILDLGGKKYSeeekeelaerkndyyvellke 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   43 WDVKSLVMGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLfshIVlgDDPEVQHGKPDPDIFLACAKRFSPP 122
Cdd:TIGR01990  83 LTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDA---IV--DPAELKKGKPDPEIFLAAAEGLGVS 157

                         170       180
                  ....*....|....*....|....*....
gi 296011030  123 PamEKCLVFEDAPNGVEAALAAGMQVVMV 151
Cdd:TIGR01990 158 P--SECIGIEDAQAGIEAIKAAGMFAVGV 184
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 11-174 1.53e-21

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: 86.19  E-value: 1.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  11 LIFDMDGLLLDTERLYSVV------FQEICNRYDKKYSWDVKSLVM-----GAEKLIIHLRKHGIPFALATSSGSASfdm 79
Cdd:cd02598    2 VIFDLDGVITDTAEYHYRAwkkladKEELAARKNRIYVELIEELTPvdvlpGIASLLVDLKAKGIKIALASASKNAP--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  80 KTSRHKEFFSLFSHIVlgDDPEVQHGKPDPDIFLACAKRFSPPPAmeKCLVFEDAPNGVEAALAAGMQVVMVPDGNlsrD 159
Cdd:cd02598   79 KILEKLGLAEYFDAIV--DGAVLAKGKPDPDIFLAAAEGLGLNPK--DCIGVEDAQAGIRAIKAAGFLVVGVGREE---D 151

                        170
                 ....*....|....*
gi 296011030 160 LTTKATLVLNSLQDF 174
Cdd:cd02598  152 LLGADIVVPDTTADL 166
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
11-151 2.11e-20

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 83.40  E-value: 2.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   11 LIFDMDGLLLDTERLYSVVFQEICNRYD----------KKYSWDVKSLVM------------------------------ 50
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGygelseeeilKFIGLPLREIFRylgvsedeeekiefylrkyneelhdklvkp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   51 --GAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKeFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPamEKC 128
Cdd:pfam13419  81 ypGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLG-LEDYFDVIVGGDD--VEGKKPDPDPILKALEQLGLKP--EEV 155

                         170       180
                  ....*....|....*....|...
gi 296011030  129 LVFEDAPNGVEAALAAGMQVVMV 151
Cdd:pfam13419 156 IYVGDSPRDIEAAKNAGIKVIAV 178
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 47-173 3.73e-19

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: 80.85  E-value: 3.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  47 SLVMGAEKLIIHLRKHGIPFALATSsgsASFDMKTSRHkEFFSLF--SHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPa 124
Cdd:cd07527   77 IAIPGAVDLLASLPAAGDRWAIVTS---GTRALAEARL-EAAGLPhpEVLVTADD--VKNGKPDPEPYLLGAKLLGLDP- 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 296011030 125 mEKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTK-ATLVLNSLQD 173
Cdd:cd07527  150 -SDCVVFEDAPAGIKAGKAAGARVVAVNTSHDLEQLEAAgADLVVEDLSD 198
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
8-174 6.69e-19

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 80.36  E-value: 6.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   8 VTHLIFDMDGLLLDTERLYSVVFQEICNRYDKK--------------------------YSWDVKSLVM----------- 50
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPpldleelraliglglrellrrllgedPDEELEELLArfrelyeeell 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  51 -------GAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHkEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPP 123
Cdd:COG0546   81 detrlfpGVRELLEALKARGIKLAVVTNKPREFAERLLEAL-GLDDYFDAIVGGDD--VPPAKPKPEPLLEALERLGLDP 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 296011030 124 amEKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRD--LTTKATLVLNSLQDF 174
Cdd:COG0546  158 --EEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAEelEAAGADYVIDSLAEL 208
PRK11587 PRK11587
putative phosphatase; Provisional
 51-175 2.63e-18

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 78.88  E-value: 2.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  51 GAEKLIIHLRKHGIPFALATSsgsASFDMKTSRHKEffslfshivlGDDPE---------VQHGKPDPDIFLACAKRFSP 121
Cdd:PRK11587  87 GAIALLNHLNKLGIPWAIVTS---GSVPVASARHKA----------AGLPApevfvtaerVKRGKPEPDAYLLGAQLLGL 153

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 296011030 122 PPamEKCLVFEDAPNGVEAALAAGMQVVMV--PDGNLSRDlttKATLVLNSLQDFQ 175
Cdd:PRK11587 154 AP--QECVVVEDAPAGVLSGLAAGCHVIAVnaPADTPRLD---EVDLVLHSLEQLT 204
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 11-152 3.27e-17

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: 75.49  E-value: 3.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  11 LIFDMDGLLLDTERLYSVVFQEICNR-YDKKYSWDVK------SLVMGAEKLIIHLRK------------------H--- 62
Cdd:cd07528    2 LIFDVDGTLAETEELHRRAFNNAFFAeRGLDWYWDRElygellRVGGGKERIAAYFEKvgwpesapkdlkeliadlHkak 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  63 -----------------------------GIPFALATSSGSASFDMKTSRH--KEFFSLFSHIVLGDDpeVQHGKPDPDI 111
Cdd:cd07528   82 teryaeliaagllplrpgvarlideakaaGVRLAIATTTSPANVDALLSALlgPERRAIFDAIAAGDD--VAEKKPDPDI 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 296011030 112 FLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMVP 152
Cdd:cd07528  160 YLLALERLGVSP--SDCLAIEDSAIGLQAAKAAGLPCIVTP 198
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 8-145 3.99e-15

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: 69.92  E-value: 3.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030    8 VTHLIFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDvkslvmGAEKLIIHLRKHGIPFALATSsGSASFDMKTSRHKEF 87
Cdd:pfam00702  65 LDILRGLVETLEAEGLTVVLVELLGVIALADELKLYP------GAAEALKALKERGIKVAILTG-DNPEAAEALLRLLGL 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 296011030   88 FSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAG 145
Cdd:pfam00702 138 DDYFDVVISGDD--VGVGKPKPEIYLAALERLGVKP--EEVLMVGDGVNDIPAAKAAG 191
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 51-178 1.40e-13

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: 66.21  E-value: 1.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  51 GAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHkEFFSLFSHIVLGDdpEVQHGKPDPDIFLACAKRFSPPPamEKCLV 130
Cdd:COG1011   97 DALELLEALKARGYRLALLTNGSAELQEAKLRRL-GLDDLFDAVVSSE--EVGVRKPDPEIFELALERLGVPP--EEALF 171

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 296011030 131 FEDAPNG-VEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQDFQPEL 178
Cdd:COG1011  172 VGDSPETdVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAELLELL 220
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 51-178 4.41e-13

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 66.41  E-value: 4.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   51 GAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEvqHGKPDPDIFLACAKRFSPPPAmeKCLV 130
Cdd:PLN02919  165 GALELITQCKNKGLKVAVASSADRIKVDANLAAAGLPLSMFDAIVSADAFE--NLKPAPDIFLAAAKILGVPTS--ECVV 240

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 296011030  131 FEDAPNGVEAALAAGMQVVMVpdgnlsrdlttKATLVLNSLQDFQPEL 178
Cdd:PLN02919  241 IEDALAGVQAARAAGMRCIAV-----------TTTLSEEILKDAGPSL 277
PRK10826 PRK10826
hexitol phosphatase HxpB;
1-153 6.33e-12

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 61.50  E-value: 6.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   1 MAAPPqPVTHLIFDMDGLLLDTERLYS-------------VVFQEICN-----RYD-------KKYSWD----------- 44
Cdd:PRK10826   1 MSTPR-QILAAIFDMDGLLIDSEPLWDraeldvmaslgvdISRREELPdtlglRIDqvvdlwyARQPWNgpsrqevvqri 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  45 ---VKSLVM-------GAEKLIIHLRKHGIPFALATSSGS----ASFDMKTSRHKeFFSLFSHIVLgddpevQHGKPDPD 110
Cdd:PRK10826  80 iarVISLIEetrpllpGVREALALCKAQGLKIGLASASPLhmleAVLTMFDLRDY-FDALASAEKL------PYSKPHPE 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 296011030 111 IFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMVPD 153
Cdd:PRK10826 153 VYLNCAAKLGVDP--LTCVALEDSFNGMIAAKAARMRSIVVPA 193
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 11-181 2.65e-11

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 60.49  E-value: 2.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  11 LIFDMDGLLLDTER-LYSVVFQEICNRYD-KKYSWDVK------SLVMGAEKLIIHLRKHGIPF-----ALATSSGSASF 77
Cdd:PLN02779  43 LLFDCDGVLVETERdGHRVAFNDAFKEFGlRPVEWDVElydellNIGGGKERMTWYFNENGWPTstiekAPKDEEERKEL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  78 -----DMKTSRHKEFF---------------------------------SLFSHIV---------------LGDDpeVQH 104
Cdd:PLN02779 123 vdslhDRKTELFKELIesgalplrpgvlrlmdealaagikvavcstsneKAVSKIVntllgperaqgldvfAGDD--VPK 200

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296011030 105 GKPDPDIFLACAKRFSPPPAmeKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQDFQPELFGL 181
Cdd:PLN02779 201 KKPDPDIYNLAAETLGVDPS--RCVVVEDSVIGLQAAKAAGMRCIVTKSSYTADEDFSGADAVFDCLGDVPLEDFDL 275
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 22-154 2.87e-10

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 56.58  E-value: 2.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  22 TERLYSVVFQEICNRYDKKYSWD-----VKSLVMGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVL 96
Cdd:cd02603   54 TEEEFWEELREELGRPLSAELFEelvlaAVDPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDLFDGVVE 133

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 296011030  97 GDDpeVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMVPDG 154
Cdd:cd02603  134 SCR--LGVRKPDPEIYQLALERLGVKP--EEVLFIDDREENVEAARALGIHAILVTDA 187
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 10-145 3.74e-10

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: 55.86  E-value: 3.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   10 HLIFDMDGLLLDTERLYSVVFQEICNRYD------KKYS-----------------WDV------------KSLVMGAEK 54
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGldpasfKALKqagglaeeewyriatsaLEElqgrfwseydaeEAYIRGAAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030   55 LIIHLRKHGIPFALAtSSGSASFDMKTSRHKEFFSLFSHIVLGDDPevqHGKPDPDIFLACAKRFSPPPameKCLVFEDA 134
Cdd:TIGR01549  81 LLARLKSAGIKLGII-SNGSLRAQKLLLRLFGLGDYFELILVSDEP---GSKPEPEIFLAALESLGVPP---EVLHVGDN 153

                         170
                  ....*....|.
gi 296011030  135 PNGVEAALAAG 145
Cdd:TIGR01549 154 LNDIEGARNAG 164
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 48-182 9.18e-10

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 56.19  E-value: 9.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  48 LVMGAEKLIIHLRKHGIPFALATSSGSASfdmkTSRHKEFFSL---FSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPa 124
Cdd:PLN03243 110 LRPGSREFVQALKKHEIPIAVASTRPRRY----LERAIEAVGMegfFSVVLAAED--VYRGKPDPEMFMYAAERLGFIP- 182

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296011030 125 mEKCLVFEDAPNGVEAALAAGMQVVMV----PDGNLS------RDLTTKATLVLNSLQDFQPELFGLP 182
Cdd:PLN03243 183 -ERCIVFGNSNSSVEAAHDGCMKCVAVagkhPVYELSagdlvvRRLDDLSVVDLKNLSDLDSPEFQIP 249
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 10-151 1.95e-08

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: 50.09  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  10 HLIFDMDGLLLdterlysvvfqeicnrydkkyswdvkslvmgAEKLIIHLRKHGIPFALATSsGSASFDMKTSRHKEFFS 89
Cdd:cd01427    1 AVLFDLDGTLL-------------------------------AVELLKRLRAAGIKLAIVTN-RSREALRALLEKLGLGD 48

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296011030  90 LFSHIVLGDDPEVQHGKPDPDIFLACAKRFSPppamEKCLVFEDAPNGVEAALAAGMQVVMV 151
Cdd:cd01427   49 LFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDP----EEVLFVGDSENDIEAARAAGGRTVAV 106
Hydrolase_like pfam13242
HAD-hyrolase-like;
105-173 6.95e-08

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 47.61  E-value: 6.95e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296011030  105 GKPDPDIFLACAKRFSPPPamEKCLVFEDAPN-GVEAALAAGMQVVMVPDGNLSRDLTTKA----TLVLNSLQD 173
Cdd:pfam13242   3 GKPNPGMLERALARLGLDP--ERTVMIGDRLDtDILGAREAGARTILVLTGVTRPADLEKApirpDYVVDDLAE 74
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 51-185 5.42e-07

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 48.71  E-value: 5.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  51 GAEKLIIHLRKHGIPFALATSSGSASFD--MKTSRHKEFFSLfshIVLGDDpeVQHGKPDPDIFLACAKRFSPPPamEKC 128
Cdd:PLN02575 220 GSQEFVNVLMNYKIPMALVSTRPRKTLEnaIGSIGIRGFFSV---IVAAED--VYRGKPDPEMFIYAAQLLNFIP--ERC 292

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296011030 129 LVFEDAPNGVEAALAAGMQVVMV----PDGNLS------RDLTTKATLVLNSLQDFQPELFGLPSYE 185
Cdd:PLN02575 293 IVFGNSNQTVEAAHDARMKCVAVaskhPIYELGaadlvvRRLDELSIVDLKNLADIESPEFGPPEPE 359
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
58-178 4.54e-05

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 42.49  E-value: 4.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  58 HLRKHGIPFALATSsgsasfdmKTSRHKE-------FFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPamEKCLV 130
Cdd:PRK13222 104 ALKAAGYPLAVVTN--------KPTPFVApllealgIADYFSVVIGGDS--LPNKKPDPAPLLLACEKLGLDP--EEMLF 171

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 296011030 131 FEDAPNGVEAALAAGMQVVMVPDG-NLSRDLTT-KATLVLNSLQDFQPEL 178
Cdd:PRK13222 172 VGDSRNDIQAARAAGCPSVGVTYGyNYGEPIALsEPDVVIDHFAELLPLL 221
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 101-148 7.72e-05

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 41.60  E-value: 7.72e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 296011030 101 EVQHGKPDPDIFLACAKRFSPPpaMEKCLVFEDAPNGVEAALAAGMQV 148
Cdd:PRK10563 137 DIQRWKPDPALMFHAAEAMNVN--VENCILVDDSSAGAQSGIAAGMEV 182
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 91-155 1.27e-04

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 41.36  E-value: 1.27e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296011030  91 FSHIVLGDdpEVQHGKPDPDIFLACAKRFSPppAMEKCLVFEDAPNGVEAALAAGMQVVMVPDGN 155
Cdd:PLN02770 151 FQAVIIGS--ECEHAKPHPDPYLKALEVLKV--SKDHTFVFEDSVSGIKAGVAAGMPVVGLTTRN 211
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 10-149 1.26e-03

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. 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: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 36.75  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  10 HLIFDMDGLLLDterlysvvfqeicnrydkkyswdvkslvmGAEKLIIHLRKhGIPFALATSsGSAsfdmKTSRHK---- 85
Cdd:cd04305    1 AIIFDLDDTLLP-----------------------------GAKELLEELKK-GYKLGIITN-GPT----EVQWEKleql 45

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296011030  86 EFFSLFSHIVLGDdpEVQHGKPDPDIFLACAKRFSPPPamEKCLVFED-APNGVEAALAAGMQVV 149
Cdd:cd04305   46 GIHKYFDHIVISE--EVGVQKPNPEIFDYALNQLGVKP--EETLMVGDsLESDILGAKNAGIKTV 106
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 12-151 4.82e-03

Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGPase; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and phosphate. 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 (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: 319857 [Multi-domain]  Cd Length: 105  Bit Score: 35.13  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  12 IFDMDGLLLDTErlysvvfqeicnrydkkyswdvkslvmgaekLIIHLRKHGIPFALATSSGSASFDMKTsrhKEFFSLF 91
Cdd:cd16421    3 IFDLDGTLLILE-------------------------------LLKALRQKGIKLAVLSNKPNEAVQVLV---EELFPGS 48

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011030  92 SHIVLGDDPEVQHgKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMV 151
Cdd:cd16421   49 FDFVLGEKEGIRR-KPDPT*ALECAKVLGVPP--DEVLYVGDSGVDMQTARNAGMDEIGV 105
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 105-160 5.70e-03

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The haloacid dehalogenase-like (HAD) hydrolases are 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 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. Members 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: 319827 [Multi-domain]  Cd Length: 253  Bit Score: 36.54  E-value: 5.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 296011030 105 GKPDPDIFLACAKRFSPPPAMEKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDL 160
Cdd:cd07525  182 GKPHPPIYDLALARLGRPAKARILAVGDGLHTDILGANAAGLDSLFVTGGIHRRLA 237
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 87-151 6.83e-03

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; The haloacid dehalogenase-like (HAD) hydrolases are 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 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. Members 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: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 34.96  E-value: 6.83e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296011030  87 FFSLFSHIVLGDdpEVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAP-NGVEAALAAGMQVVMV 151
Cdd:cd16415   45 LDDYFDFVVFSY--EVGYEKPDPRIFQKALERLGVSP--EEALHVGDDLkNDYLGARAVGWHALLV 106
 
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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