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Conserved domains on  [gi|1518078120|gb|AYX13966|]
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hexitol phosphatase HxpB [Yersinia pseudotuberculosis]

Protein Classification

hexitol phosphatase HxpB( domain architecture ID 10793483)

hexitol phosphatase HxpB is a sugar-phosphate phosphohydrolase that catalyzes the dephosphorylation of D-mannitol 1-phosphate and D-sorbitol 6-phosphate; also catalyzes the dephosphorylation of 2-deoxyglucose 6-phosphate (2dGlu6P)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10826 PRK10826
hexitol phosphatase HxpB;
1-220 1.51e-152

hexitol phosphatase HxpB;


:

Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 422.05  E-value: 1.51e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   1 MATAHPIKAAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLPDTLGLRIDLVVKLWYQTMPWQGPSQEEVCNRII 80
Cdd:PRK10826    1 MSTPRQILAAIFDMDGLLIDSEPLWDRAELDVMASLGVDISRREELPDTLGLRIDQVVDLWYARQPWNGPSRQEVVQRII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  81 ARAIDLVEDTRPVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQ 160
Cdd:PRK10826   81 ARVISLIEETRPLLPGVREALALCKAQGLKIGLASASPLHMLEAVLTMFDLRDYFDALASAEKLPYSKPHPEVYLNCAAK 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120 161 LDVDPLQCVTLEDSVNGMIATKAARMRSIVIPSVEYRADPRWALADIQLESLDQLRKDDI 220
Cdd:PRK10826  161 LGVDPLTCVALEDSFNGMIAAKAARMRSIVVPAPEQQNDPRWALADVKLESLTELTAADL 220
 
Name Accession Description Interval E-value
PRK10826 PRK10826
hexitol phosphatase HxpB;
1-220 1.51e-152

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 422.05  E-value: 1.51e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   1 MATAHPIKAAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLPDTLGLRIDLVVKLWYQTMPWQGPSQEEVCNRII 80
Cdd:PRK10826    1 MSTPRQILAAIFDMDGLLIDSEPLWDRAELDVMASLGVDISRREELPDTLGLRIDQVVDLWYARQPWNGPSRQEVVQRII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  81 ARAIDLVEDTRPVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQ 160
Cdd:PRK10826   81 ARVISLIEETRPLLPGVREALALCKAQGLKIGLASASPLHMLEAVLTMFDLRDYFDALASAEKLPYSKPHPEVYLNCAAK 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120 161 LDVDPLQCVTLEDSVNGMIATKAARMRSIVIPSVEYRADPRWALADIQLESLDQLRKDDI 220
Cdd:PRK10826  161 LGVDPLTCVALEDSFNGMIAAKAARMRSIVVPAPEQQNDPRWALADVKLESLTELTAADL 220
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
6-215 8.81e-68

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 206.98  E-value: 8.81e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   6 PIKAAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSsRDSLPDTLGLRIDLVVKLWYQTMPWQgPSQEEVCNRIIARAID 85
Cdd:COG0637     1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLT-EEEYRRLMGRSREDILRYLLEEYGLD-LPEEELAARKEELYRE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  86 LVEDTR-PVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQLDVD 164
Cdd:COG0637    79 LLAEEGlPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVD 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1518078120 165 PLQCVTLEDSVNGMIATKAARMRSIVIPSvEYRADPRWALADIQLESLDQL 215
Cdd:COG0637   159 PEECVVFEDSPAGIRAAKAAGMRVVGVPD-GGTAEEELAGADLVVDDLAEL 208
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 9-211 5.38e-39

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: 132.38  E-value: 5.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   9 AAIFDMDGLLIDSEPLWLQAELDIFTALGldtssrdslpdtlglridlvvklwyqtmpwqgpsqeevcNRIIARAIDLVE 88
Cdd:cd16423     1 AVIFDFDGVIVDTEPLWYEAWQELLNERR---------------------------------------NELIKRQFSEKT 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  89 DTRPvLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQLDVDPLQC 168
Cdd:cd16423    42 DLPP-IEGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGVNPEEC 120

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1518078120 169 VTLEDSVNGMIATKAARMRSIVIPSVEYRADPrWALADIQLES 211
Cdd:cd16423   121 VVIEDSRNGVLAAKAAGMKCVGVPNPVTGSQD-FSKADLVLSS 162
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 7-191 9.81e-31

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: 111.67  E-value: 9.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   7 IKAAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSR-----DSLP--DTLGLRIDLVVKlwyqtmpwqGPSQEEVC--- 76
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQyneslKGLSreDILRAILKLRGD---------GLSLEEIHqla 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  77 ---NRIIARAIDLVEDTrpVLPGVEYALALCRQQGLKIGLASASplHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEV 153
Cdd:TIGR02009  72 erkNELYRELLRLTGVA--VLPGIRNLLKRLKAKGIAVGLGSSS--KNAPRILAKLGLRDYFDAIVDASEVKNGKPHPET 147

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1518078120 154 YLNAAAQLDVDPLQCVTLEDSVNGMIATKAARMRSIVI 191
Cdd:TIGR02009 148 FLLAAELLGVPPNECIVFEDALAGVQAARAAGMFAVAV 185
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
11-191 9.01e-27

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 101.12  E-value: 9.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  11 IFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLPDTLGL-RIDLVVKLwyqtmpwqGPSQEEvcNRIIARAIDLVED 89
Cdd:pfam13419   2 IFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLpLREIFRYL--------GVSEDE--EEKIEFYLRKYNE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  90 ------TRPvLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQLDV 163
Cdd:pfam13419  72 elhdklVKP-YPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGL 150

                         170       180
                  ....*....|....*....|....*...
gi 1518078120 164 DPLQCVTLEDSVNGMIATKAARMRSIVI 191
Cdd:pfam13419 151 KPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
 
Name Accession Description Interval E-value
PRK10826 PRK10826
hexitol phosphatase HxpB;
1-220 1.51e-152

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 422.05  E-value: 1.51e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   1 MATAHPIKAAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLPDTLGLRIDLVVKLWYQTMPWQGPSQEEVCNRII 80
Cdd:PRK10826    1 MSTPRQILAAIFDMDGLLIDSEPLWDRAELDVMASLGVDISRREELPDTLGLRIDQVVDLWYARQPWNGPSRQEVVQRII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  81 ARAIDLVEDTRPVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQ 160
Cdd:PRK10826   81 ARVISLIEETRPLLPGVREALALCKAQGLKIGLASASPLHMLEAVLTMFDLRDYFDALASAEKLPYSKPHPEVYLNCAAK 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120 161 LDVDPLQCVTLEDSVNGMIATKAARMRSIVIPSVEYRADPRWALADIQLESLDQLRKDDI 220
Cdd:PRK10826  161 LGVDPLTCVALEDSFNGMIAAKAARMRSIVVPAPEQQNDPRWALADVKLESLTELTAADL 220
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
6-215 8.81e-68

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 206.98  E-value: 8.81e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   6 PIKAAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSsRDSLPDTLGLRIDLVVKLWYQTMPWQgPSQEEVCNRIIARAID 85
Cdd:COG0637     1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLT-EEEYRRLMGRSREDILRYLLEEYGLD-LPEEELAARKEELYRE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  86 LVEDTR-PVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQLDVD 164
Cdd:COG0637    79 LLAEEGlPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVD 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1518078120 165 PLQCVTLEDSVNGMIATKAARMRSIVIPSvEYRADPRWALADIQLESLDQL 215
Cdd:COG0637   159 PEECVVFEDSPAGIRAAKAAGMRVVGVPD-GGTAEEELAGADLVVDDLAEL 208
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 9-211 5.38e-39

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: 132.38  E-value: 5.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   9 AAIFDMDGLLIDSEPLWLQAELDIFTALGldtssrdslpdtlglridlvvklwyqtmpwqgpsqeevcNRIIARAIDLVE 88
Cdd:cd16423     1 AVIFDFDGVIVDTEPLWYEAWQELLNERR---------------------------------------NELIKRQFSEKT 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  89 DTRPvLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQLDVDPLQC 168
Cdd:cd16423    42 DLPP-IEGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGVNPEEC 120

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1518078120 169 VTLEDSVNGMIATKAARMRSIVIPSVEYRADPrWALADIQLES 211
Cdd:cd16423   121 VVIEDSRNGVLAAKAAGMKCVGVPNPVTGSQD-FSKADLVLSS 162
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 9-193 2.43e-36

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: 124.65  E-value: 2.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   9 AAIFDMDGLLIDSEPLWLQAELDIftalgldtssrdslpdtlglridlvvkLWYQTMpwqgpsqeevcnriiaRAIDLVE 88
Cdd:cd07505     1 AVIFDMDGVLIDTEPLHRQAWQLL---------------------------ERKNAL----------------LLELIAS 37

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  89 DTRPVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGV-EKYFDCLVSAEYLPYSKPHPEVYLNAAAQLDVDPLQ 167
Cdd:cd07505    38 EGLKLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLlRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPER 117

                         170       180
                  ....*....|....*....|....*.
gi 1518078120 168 CVTLEDSVNGMIATKAARMRSIVIPS 193
Cdd:cd07505   118 CLVFEDSLAGIEAAKAAGMTVVAVPD 143
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
7-215 1.33e-35

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 125.04  E-value: 1.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   7 IKAAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLPDTLGLRIDLVVKLWYQTMPWQGpsQEEVCNRIIARAIDL 86
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRLLGEDPDEE--LEELLARFRELYEEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  87 VEDTRPVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQLDVDPL 166
Cdd:COG0546    79 LLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1518078120 167 QCVTLEDSVNGMIATKAARMRSIVIPS-VEYRADPRWALADIQLESLDQL 215
Cdd:COG0546   159 EVLMVGDSPHDIEAARAAGVPFIGVTWgYGSAEELEAAGADYVIDSLAEL 208
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 7-191 9.81e-31

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: 111.67  E-value: 9.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   7 IKAAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSR-----DSLP--DTLGLRIDLVVKlwyqtmpwqGPSQEEVC--- 76
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQyneslKGLSreDILRAILKLRGD---------GLSLEEIHqla 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  77 ---NRIIARAIDLVEDTrpVLPGVEYALALCRQQGLKIGLASASplHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEV 153
Cdd:TIGR02009  72 erkNELYRELLRLTGVA--VLPGIRNLLKRLKAKGIAVGLGSSS--KNAPRILAKLGLRDYFDAIVDASEVKNGKPHPET 147

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1518078120 154 YLNAAAQLDVDPLQCVTLEDSVNGMIATKAARMRSIVI 191
Cdd:TIGR02009 148 FLLAAELLGVPPNECIVFEDALAGVQAARAAGMFAVAV 185
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 9-191 3.74e-27

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: 102.11  E-value: 3.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   9 AAIFDMDGLLIDSEPL-WLQAELDIFTALGLDtsSRDSLPDTLGLRIDLVVKLWYQTMPwQGPSQEEVCNRIIaRAIDLV 87
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAiAKLINREELGLVPDE--LGVSAVGRLELALRRFKAQYGRTIS-PEDAQLLYKQLFY-EQIEEE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  88 EDTRPvLPGVEYALALCRQQGLKIGLASASPLHMqERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQLDVDPLQ 167
Cdd:TIGR01509  77 AKLKP-LPGVRALLEALRARGKKLALLTNSPRAH-KLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEPSE 154

                         170       180
                  ....*....|....*....|....
gi 1518078120 168 CVTLEDSVNGMIATKAARMRSIVI 191
Cdd:TIGR01509 155 CVFVDDSPAGIEAAKAAGMHTVGV 178
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
11-191 9.01e-27

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 101.12  E-value: 9.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  11 IFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLPDTLGL-RIDLVVKLwyqtmpwqGPSQEEvcNRIIARAIDLVED 89
Cdd:pfam13419   2 IFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLpLREIFRYL--------GVSEDE--EEKIEFYLRKYNE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  90 ------TRPvLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQLDV 163
Cdd:pfam13419  72 elhdklVKP-YPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGL 150

                         170       180
                  ....*....|....*....|....*...
gi 1518078120 164 DPLQCVTLEDSVNGMIATKAARMRSIVI 191
Cdd:pfam13419 151 KPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 7-184 1.27e-25

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: 98.43  E-value: 1.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   7 IKAAIFDMDGLLIDSEPLWLQA------ELDIFTALGLDTSSRDSLPDTLGLRIDLVVKLWYQTMPWQG------PSQEE 74
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAiaelasEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRDWLEELDILRglvetlEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  75 VCNRIIARAIDLVEDTRPVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVY 154
Cdd:pfam00702  81 TVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1518078120 155 LNAAAQLDVDPLQCVTLEDSVNGMIATKAA 184
Cdd:pfam00702 161 LAALERLGVKPEEVLMVGDGVNDIPAAKAA 190
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 7-217 4.81e-24

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: 95.10  E-value: 4.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   7 IKAAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLPDTLGLRIDLVVKLWYQTMPWqgpsqEEVCNRIIARA-ID 85
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAIEYALWRRYERGEITF-----AELLRRLLEELgLD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  86 LVEDTR-----------PVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVY 154
Cdd:COG1011    76 LAEELAeaflaalpelvEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIF 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1518078120 155 LNAAAQLDVDPLQCVTLEDSVNG-MIATKAARMRSIVIPSvEYRADPRWALADIQLESLDQLRK 217
Cdd:COG1011   156 ELALERLGVPPEEALFVGDSPETdVAGARAAGMRTVWVNR-SGEPAPAEPRPDYVISDLAELLE 218
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 77-191 8.03e-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: 85.42  E-value: 8.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  77 NRIIARAIDLVEDtRPVLPGVEYALALCRQQGLKIGLASAS---PLhmqerVLAMLGVEKYFDCLVSAEYLPYSKPHPEV 153
Cdd:cd02598    35 NRIYVELIEELTP-VDVLPGIASLLVDLKAKGIKIALASASknaPK-----ILEKLGLAEYFDAIVDGAVLAKGKPDPDI 108

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1518078120 154 YLNAAAQLDVDPLQCVTLEDSVNGMIATKAARMRSIVI 191
Cdd:cd02598   109 FLAAAEGLGLNPKDCIGVEDAQAGIRAIKAAGFLVVGV 146
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 9-193 4.80e-20

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: 83.97  E-value: 4.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   9 AAIFDMDGLLIDSEPLWLQAELDIFTAL-GLDTSSRDSLPDTLgLRI--DLVVKLWYQTMPWQGPSQEEVCNRIIA---- 81
Cdd:cd07528     1 ALIFDVDGTLAETEELHRRAFNNAFFAErGLDWYWDRELYGEL-LRVggGKERIAAYFEKVGWPESAPKDLKELIAdlhk 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  82 ----RAIDLVEDTR-PVLPGVEYALALCRQQGLKIGLAS-ASPLHMQERVLAMLGVEKY--FDCLVSAEYLPYSKPHPEV 153
Cdd:cd07528    80 akteRYAELIAAGLlPLRPGVARLIDEAKAAGVRLAIATtTSPANVDALLSALLGPERRaiFDAIAAGDDVAEKKPDPDI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1518078120 154 YLNAAAQLDVDPLQCVTLEDSVNGMIATKAARMRSIVIPS 193
Cdd:cd07528   160 YLLALERLGVSPSDCLAIEDSAIGLQAAKAAGLPCIVTPS 199
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
6-189 3.40e-19

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 82.16  E-value: 3.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   6 PIKAAIFDMDGLLIDSEPlwlqaelDI-------FTALGLDTSSRDSLPDTLGLRIDLVVKlwyQTMPWQGPS-QEEVCN 77
Cdd:PRK13222    5 DIRAVAFDLDGTLVDSAP-------DLaaavnaaLAALGLPPAGEERVRTWVGNGADVLVE---RALTWAGREpDEELLE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  78 RIIARAIDLVEDTRPVL----PGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEV 153
Cdd:PRK13222   75 KLRELFDRHYAENVAGGsrlyPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFSVVIGGDSLPNKKPDPAP 154

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1518078120 154 YLNAAAQLDVDPLQCVTLEDSVNGMIATKAARMRSI 189
Cdd:PRK13222  155 LLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSV 190
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 8-187 6.08e-19

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: 79.67  E-value: 6.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   8 KAAIFDMDGLLIDSEPLWLQAELDIFTALGldtssrdslpdtlglridlvvklwyqtmpwqgpsqeevcnRIIARAIDLv 87
Cdd:cd07526     1 DLVIFDCDGVLVDSEVIAARVLVEVLAELG----------------------------------------ARVLAAFEA- 39

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  88 eDTRPVlPGVEYALalcRQQGLKIGLASASPLHMQERVLAMLGVEKYFDC-LVSAEYLPYSKPHPEVYLNAAAQLDVDPL 166
Cdd:cd07526    40 -ELQPI-PGAAAAL---SALTLPFCVASNSSRERLTHSLGLAGLLAYFEGrIFSASDVGRGKPAPDLFLHAAAQMGVAPE 114

                         170       180
                  ....*....|....*....|.
gi 1518078120 167 QCVTLEDSVNGMIATKAARMR 187
Cdd:cd07526   115 RCLVIEDSPTGVRAALAAGMT 135
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 4-191 4.96e-18

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 82.21  E-value: 4.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120    4 AHPIKAAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLP-------DTLGLridlVVKLwYQTmpwQGPSQEEVC 76
Cdd:PLN02919    72 WGKVSAVLFDMDGVLCNSEEPSRRAAVDVFAEMGVEVTVEDFVPfmgtgeaNFLGG----VASV-KGV---KGFDPDAAK 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   77 NRIIAraIDLVEDTRPVlPGVEYALAL-----CRQQGLKIGLASASPLHMQERVLAMLGV-EKYFDCLVSAEYLPYSKPH 150
Cdd:PLN02919   144 KRFFE--IYLEKYAKPN-SGIGFPGALelitqCKNKGLKVAVASSADRIKVDANLAAAGLpLSMFDAIVSADAFENLKPA 220

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1518078120  151 PEVYLNAAAQLDVDPLQCVTLEDSVNGMIATKAARMRSIVI 191
Cdd:PLN02919   221 PDIFLAAAKILGVPTSECVVIEDALAGVQAARAAGMRCIAV 261
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 9-216 1.02e-17

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: 77.77  E-value: 1.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   9 AAIFDMDGLLIDSEPLWLQAELDIFTALGLDtssrdslPDTL-----GLRIDLVVKLWyqtMPWQGPSQEEvcNRIIARA 83
Cdd:cd07527     1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGVD-------PEEVlkvshGRRAIDVIRKL---APDDADIELV--LALETEE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  84 IDLVEDTRPVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYfDCLVSAEYLPYSKPHPEVYLNAAAQLDV 163
Cdd:cd07527    69 PESYPEGVIAIPGAVDLLASLPAAGDRWAIVTSGTRALAEARLEAAGLPHP-EVLVTADDVKNGKPDPEPYLLGAKLLGL 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1518078120 164 DPLQCVTLEDSVNGMIATKAARMRSIVIPSVEYRADPRWALADIQLESLDQLR 216
Cdd:cd07527   148 DPSDCVVFEDAPAGIKAGKAAGARVVAVNTSHDLEQLEAAGADLVVEDLSDIS 200
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 7-215 2.51e-16

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. 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: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 74.24  E-value: 2.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   7 IKAAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLPDTLG--LRiDLVVKLwyqtMPWQGPSQEEV---CNRIIA 81
Cdd:cd02616     1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYGLEGYTREEVLPFIGppLR-ETFEKI----DPDKLEDMVEEfrkYYREHN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  82 RaiDLVEdtrpVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQL 161
Cdd:cd02616    76 D--DLTK----EYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELL 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1518078120 162 DVDPLQCVTLEDSVNGMIATKAARMRS-IVIPSVEYRADPRWALADIQLESLDQL 215
Cdd:cd02616   150 GAEPEEALMVGDSPHDILAGKNAGVKTvGVTWGYKGREYLKAFNPDFIIDKMSDL 204
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 10-215 2.84e-16

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; 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: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 73.97  E-value: 2.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  10 AIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLPDTLGLRIDLVVKLWYqtmPWQGPSQEEVCNRIIARAIDLV-- 87
Cdd:cd07533     2 VIFDWDGTLADSQHNIVAAMTAAFADLGLPVPSAAEVRSIIGLSLDEAIARLL---PMATPALVAVAERYKEAFDILRll 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  88 -EDTRPVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPySKPHPEVYLNAAAQLDVDPL 166
Cdd:cd07533    79 pEHAEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFDATRTADDTP-SKPHPEMLREILAELGVDPS 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1518078120 167 QCVTLEDSVNGMIATKAARMRSIvipSVEY----RADPRWALADIQLESLDQL 215
Cdd:cd07533   158 RAVMVGDTAYDMQMAANAGAHAV---GVAWgyhsLEDLRSAGADAVVDHFSEL 207
CTE7 TIGR02253
HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and ...
 7-215 2.94e-16

HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and metazoans includes the human uncharacterized protein CTE7. Pyrococcus species appear to have three different forms of this enzyme, so it is unclear whether all members of this family have the same function. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 274057 [Multi-domain]  Cd Length: 221  Bit Score: 74.36  E-value: 2.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   7 IKAAIFDMDGLLIDSEPLWLQAE---LDIFTALGLDTSSRDSLPDTLGLRID-----------LVVKLWYQTMPwqgpsq 72
Cdd:TIGR02253   2 IKAIFFDLDDTLIDTSGLAEKARrnaIEVLIEAGLNVDFEEAYEELLKLIKEygsnypthfdyLIRRLWEEYNP------ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  73 EEVCNRIIARaIDLVEDTRPVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPE 152
Cdd:TIGR02253  76 KLVAAFVYAY-HKLKFAYLRVYPGVRDTLMELRESGYRLGIITDGLPVKQWEKLERLGVRDFFDAVITSEEEGVEKPHPK 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1518078120 153 VYLNAAAQLDVDPLQCVTLEDSVNGMI-ATKAARMRSIVIPSVEY--RADPRWALADIQLESLDQL 215
Cdd:TIGR02253 155 IFYAALKRLGVKPEEAVMVGDRLDKDIkGAKNAGMKTVWINQGKSskMEDDVYPYPDYEISSLREL 220
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 9-192 8.24e-16

Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGP; 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: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 73.04  E-value: 8.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   9 AAIFDMDGLLIDSEP-LWLQAELdIFTALGLDTSSRDSLPDTLGLRIDLVVKlwyQTMPWqgpsqeevcNRIIARAIDLV 87
Cdd:cd16417     1 LVAFDLDGTLVDSAPdLAEAANA-MLAALGLPPLPEETVRTWIGNGADVLVE---RALTG---------AREAEPDEELF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  88 EDTRPVL---------------PGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPE 152
Cdd:cd16417    68 KEARALFdrhyaetlsvhshlyPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSLPEKKPDPA 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1518078120 153 VYLNAAAQLDVDPLQCVTLEDSVNGMIATKAARMRSIVIP 192
Cdd:cd16417   148 PLLHACEKLGIAPAQMLMVGDSRNDILAARAAGCPSVGLT 187
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
11-186 8.64e-16

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 72.41  E-value: 8.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  11 IFDMDGLLIDSEPLWLQAELDIFTALGL--DTSSRDSLPDTLGLRIDLVVKLWYQTM--PWQGPSQEEVCNRIIaraidL 86
Cdd:PRK10725    9 IFDMDGTILDTEPTHRKAWREVLGRYGLqfDEQAMVALNGSPTWRIAQAIIELNQADldPHALAREKTEAVKSM-----L 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  87 VEDTRPvLPGVEYALALCRQQGLKIGLASASPlhMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQLDVDPL 166
Cdd:PRK10725   84 LDSVEP-LPLIEVVKAWHGRRPMAVGTGSESA--IAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQPT 160

                         170       180
                  ....*....|....*....|
gi 1518078120 167 QCVTLEDSVNGMIATKAARM 186
Cdd:PRK10725  161 QCVVFEDADFGIQAARAAGM 180
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 9-200 2.44e-15

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: 71.58  E-value: 2.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   9 AAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLPDTLGLRIDLVVKLWYQT--MPWQGPSQEEVCNRIIARAIDL 86
Cdd:cd07512     1 AVIFDLDGTLIDSAPDLHAALNAVLAAEGLAPLSLAEVRSFVGHGAPALIRRAFAAagEDLDGPLHDALLARFLDHYEAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  87 VEDTRPVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQLDVDPL 166
Cdd:cd07512    81 PPGLTRPYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAIRRLGGDVS 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1518078120 167 QCVTLEDSVNGMIATKAARMRSIVIpSVEYRADP 200
Cdd:cd07512   161 RALMVGDSETDAATARAAGVPFVLV-TFGYRHAP 193
PLN02940 PLN02940
riboflavin kinase
 1-216 2.77e-15

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 73.71  E-value: 2.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   1 MATAHPIK----AAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLpdtlglriDLVVKLWYQTMP-----WQGP- 70
Cdd:PLN02940    1 MSAAKPLKklvsHVILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQ--------KIVGKTPLEAAAtvvedYGLPc 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  71 SQEEVCNRIIARAIDLVEDTRPvLPGVEYALALCRQQGLKIGLASASP-LHMQERVLAMLGVEKYFDCLVSAEYLPYSKP 149
Cdd:PLN02940   73 STDEFNSEITPLLSEQWCNIKA-LPGANRLIKHLKSHGVPMALASNSPrANIEAKISCHQGWKESFSVIVGGDEVEKGKP 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1518078120 150 HPEVYLNAAAQLDVDPLQCVTLEDSVNGMIATKAARMRSIVIPSVEYRaDPRWALADIQLESLDQLR 216
Cdd:PLN02940  152 SPDIFLEAAKRLNVEPSNCLVIEDSLPGVMAGKAAGMEVIAVPSIPKQ-THLYSSADEVINSLLDLQ 217
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 7-192 2.52e-14

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: 68.53  E-value: 2.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   7 IKAAIFDMDGLLIDSEPLWLQAELDIFTALGlDTSSRDSLPDTLGLRID----LVVKlWYQ-TMPWQgpsqEEVCNRIIA 81
Cdd:cd07529     1 VTHCIFDMDGLLLDTERIYTETTQEILARYG-KTYTWDVKAKMMGRPASeaarIIVD-ELKlPMSLE----EEFDEQQEA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  82 RAIDLVEDTRPvLPGVEYALALCRQQGLKIGLASAS-PLHMQERVLAMLGVEKYFDCLVSA---EYLPYSKPHPEVYLNA 157
Cdd:cd07529    75 LAELFMGTAKL-MPGAERLLRHLHAHNIPIALATSScTRHFKLKTSRHKELFSLFHHVVTGddpEVKGRGKPAPDIFLVA 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1518078120 158 AAQLD---VDPLQCVTLEDSVNGMIATKAARMRSIVIP 192
Cdd:cd07529   154 AKRFNeppKDPSKCLVFEDSPNGVKAAKAAGMQVVMVP 191
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 8-206 2.86e-14

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 69.74  E-value: 2.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   8 KAAIFDMDGLLIDSEP-LWLQAELDIFTALGLDTSSRDslpdtlglrIDLVVKL-----------WY-QTMPW------Q 68
Cdd:PLN02779   41 EALLFDCDGVLVETERdGHRVAFNDAFKEFGLRPVEWD---------VELYDELlnigggkermtWYfNENGWptstieK 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  69 GPSQEEVCNRIIA--------RAIDLVED-TRPVLPGVEYALALCRQQGLKIGLASASPLHMQERVL-AMLGVEKY--FD 136
Cdd:PLN02779  112 APKDEEERKELVDslhdrkteLFKELIESgALPLRPGVLRLMDEALAAGIKVAVCSTSNEKAVSKIVnTLLGPERAqgLD 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120 137 CLvSAEYLPYSKPHPEVYLNAAAQLDVDPLQCVTLEDSVNGMIATKAARMRSIVIPSVeYRADPRWALAD 206
Cdd:PLN02779  192 VF-AGDDVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGMRCIVTKSS-YTADEDFSGAD 259
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 9-185 1.54e-12

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: 63.18  E-value: 1.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   9 AAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLPDTLGLRIDLVVklWYQTMPWQgpsqeevcnRIIARAIDLVE 88
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPASFKALKQAGGLAEEEWY--RIATSALE---------ELQGRFWSEYD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  89 DTRPVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDcLVSAEYLPYSKPHPEVYLNAAAQLDVDPlQC 168
Cdd:TIGR01549  70 AEEAYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFE-LILVSDEPGSKPEPEIFLAALESLGVPP-EV 147

                         170
                  ....*....|....*..
gi 1518078120 169 VTLEDSVNGMIATKAAR 185
Cdd:TIGR01549 148 LHVGDNLNDIEGARNAG 164
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 97-191 2.37e-12

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: 61.26  E-value: 2.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  97 VEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQLDVDPLQCVTLEDSVN 176
Cdd:cd01427    12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEN 91

                          90
                  ....*....|....*
gi 1518078120 177 GMIATKAARMRSIVI 191
Cdd:cd01427    92 DIEAARAAGGRTVAV 106
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 7-184 3.13e-12

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 63.13  E-value: 3.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   7 IKAAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRD--------SLPDTLGlRIDlvvklwyqtmpwqgpsqEEVCNR 78
Cdd:PRK13288    3 INTVLFDLDGTLINTNELIISSFLHTLKTYYPNQYKREdvlpfigpSLHDTFS-KID-----------------ESKVEE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  79 IIA--RAI------DLVEDtrpvLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPH 150
Cdd:PRK13288   65 MITtyREFnhehhdELVTE----YETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPD 140

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1518078120 151 PEVYLNAAAQLDVDPLQCVTLEDSVNGMIATKAA 184
Cdd:PRK13288  141 PEPVLKALELLGAKPEEALMVGDNHHDILAGKNA 174
Pyr-5-nucltdase TIGR01993
pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast ...
 92-191 7.19e-12

pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast which has been shown to code for a pyrimidine (UMP/CMP) 5'nucleotidase. The family spans plants, fungi and a small number of bacteria. These enzymes are members of the haloacid dehalogenase (HAD) superfamily of hydrolases, specifically the IA subfamily (variant 3, TIGR01509).


Pssm-ID: 273917 [Multi-domain]  Cd Length: 183  Bit Score: 61.60  E-value: 7.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  92 PVLPGVEYALALCRQQGLKIGLASASPLHMQeRVLAMLGVEKYFD---CLVSAEYLPYSKPHPEVYLNAAAQLDVDPLQC 168
Cdd:TIGR01993  82 KLKPDPELRNLLLRLPGRKIIFTNGDRAHAR-RALRRLGIEDCFDgifCFDTANPDLLPKPSPQAYEKALREAGVDPERA 160

                          90       100
                  ....*....|....*....|...
gi 1518078120 169 VTLEDSVNGMIATKAARMRSIVI 191
Cdd:TIGR01993 161 IFFDDSARNIAAGKALGMKTVLV 183
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 78-220 1.39e-11

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 61.97  E-value: 1.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  78 RIIARAIDLVE----DTRPVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEV 153
Cdd:PLN03243   91 RLAIRKEDLYEymqgGLYRLRPGSREFVQALKKHEIPIAVASTRPRRYLERAIEAVGMEGFFSVVLAAEDVYRGKPDPEM 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1518078120 154 YLNAAAQLDVDPLQCVTLEDSVNGMIATKAARMRSIVI----PSVEYRAdprwalADIQLESLDQLRKDDI 220
Cdd:PLN03243  171 FMYAAERLGFIPERCIVFGNSNSSVEAAHDGCMKCVAVagkhPVYELSA------GDLVVRRLDDLSVVDL 235
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 87-176 1.68e-10

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: 56.40  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  87 VEDTrpVLPGVEYALALCRQqGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQLDVDPL 166
Cdd:cd04305     6 LDDT--LLPGAKELLEELKK-GYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPE 82

                          90
                  ....*....|
gi 1518078120 167 QCVTLEDSVN 176
Cdd:cd04305    83 ETLMVGDSLE 92
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 8-169 7.42e-10

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. 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: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 56.51  E-value: 7.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   8 KAAIFDMDGLLIDSEPLWLQAELDIftalgldtssrdslpdtlGLRIDLVVKLWYQ-----------TMPWQ------GP 70
Cdd:cd02588     1 KALVFDVYGTLIDWHSGLAAAERAF------------------PGRGEELSRLWRQkqleytwlvtlMGPYVdfdeltRD 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  71 SQEEVCNRiiaRAIDLVEDTRPVL----------PGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVS 140
Cdd:cd02588    63 ALRATAAE---LGLELDESDLDELgdaylrlppfPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLS 139

                         170       180
                  ....*....|....*....|....*....
gi 1518078120 141 AEYLPYSKPHPEVYLNAAAQLDVDPLQCV 169
Cdd:cd02588   140 AEDVRAYKPAPAVYELAAERLGVPPDEIL 168
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 6-186 2.14e-09

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 55.62  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   6 PIKAAIFDMDGLLIDSEPLWLQAeldiFTALGLDTSSRDSLPDTLGLRIDLVVklwyqtmpwqGPSQEEVCNRI----IA 81
Cdd:PLN02770   21 PLEAVLFDVDGTLCDSDPLHYYA----FREMLQEINFNGGVPITEEFFVENIA----------GKHNEDIALGLfpddLE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  82 RAIDLVEDTRPV-----------LPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPH 150
Cdd:PLN02770   87 RGLKFTDDKEALfrklaseqlkpLNGLYKLKKWIEDRGLKRAAVTNAPRENAELMISLLGLSDFFQAVIIGSECEHAKPH 166

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1518078120 151 PEVYLNAAAQLDVDPLQCVTLEDSVNGMIATKAARM 186
Cdd:PLN02770  167 PDPYLKALEVLKVSKDHTFVFEDSVSGIKAGVAAGM 202
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 111-215 4.38e-09

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 55.64  E-value: 4.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120 111 IGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQLDVDPLQCVTLEDSVNGMIATKAARMRSIV 190
Cdd:PLN02575  235 MALVSTRPRKTLENAIGSIGIRGFFSVIVAAEDVYRGKPDPEMFIYAAQLLNFIPERCIVFGNSNQTVEAAHDARMKCVA 314

                          90       100
                  ....*....|....*....|....*..
gi 1518078120 191 IPSveyrADPRWAL--ADIQLESLDQL 215
Cdd:PLN02575  315 VAS----KHPIYELgaADLVVRRLDEL 337
PRK13226 PRK13226
phosphoglycolate phosphatase; Provisional
 1-190 1.63e-08

phosphoglycolate phosphatase; Provisional


Pssm-ID: 237311 [Multi-domain]  Cd Length: 229  Bit Score: 52.93  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   1 MATAHPIKAAIFDMDGLLIDSEPlwlqaelDIFTALGLDTSSRDSLPDTLGLRIDLVVKLWYQTMPWQGPSQE-EVCNRI 79
Cdd:PRK13226    6 VAAVRFPRAVLFDLDGTLLDSAP-------DMLATVNAMLAARGRAPITLAQLRPVVSKGARAMLAVAFPELDaAARDAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  80 I----ARAIDLVEDTRPVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYL 155
Cdd:PRK13226   79 IpeflQRYEALIGTQSQLFDGVEGMLQRLECAGCVWGIVTNKPEYLARLILPQLGWEQRCAVLIGGDTLAERKPHPLPLL 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1518078120 156 NAAAQLDVDPLQCVTLEDSVNGMIATKAARMRSIV 190
Cdd:PRK13226  159 VAAERIGVAPTDCVYVGDDERDILAARAAGMPSVA 193
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 7-200 1.75e-08

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 52.77  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   7 IKAAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLPDTLGLR----IDLVVKLWYQTMPWQgpSQEEVCNRIIAR 82
Cdd:PRK10563    4 IEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKRFKGVKlyeiIDIISKEHGVTLAKA--ELEPVYRAEVAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  83 AIDLVedtrpvLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYF-DCLVSAEYLPYSKPHPEVYLNAAAQL 161
Cdd:PRK10563   82 LFDSE------LEPIAGANALLESITVPMCVVSNGPVSKMQHSLGKTGMLHYFpDKLFSGYDIQRWKPDPALMFHAAEAM 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1518078120 162 DVDPLQCVTLEDSVNGMIATKAARMrsiviPSVEYRADP 200
Cdd:PRK10563  156 NVNVENCILVDDSSAGAQSGIAAGM-----EVFYFCADP 189
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 7-195 3.14e-08

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: 51.96  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   7 IKAAIFDMDGLLIDSEPLWLQAELdiFTALGLDTSSRDSLPDTLGLRIDLVVKLWyqTMP--WQGPSQEevCNRIIARAI 84
Cdd:cd02603     1 IRAVLFDFGGVLIDPDPAAAVARF--EALTGEPSEFVLDTEGLAGAFLELERGRI--TEEefWEELREE--LGRPLSAEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  85 --DLVEDTRPVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAML-GVEKYFDCLVsaeylpYS------KPHPEVYL 155
Cdd:cd02603    75 feELVLAAVDPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLpRRGDLFDGVV------EScrlgvrKPDPEIYQ 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1518078120 156 NAAAQLDVDPLQCVTLEDSV-NgmiaTKAAR---MRSIVIPSVE 195
Cdd:cd02603   149 LALERLGVKPEEVLFIDDREeN----VEAARalgIHAILVTDAE 188
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
 7-189 4.37e-07

Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; Degradation of the ubiquitous natural phosphonate 2-aminoethylphosphonate (AEP) into useable forms of nitrogen, carbon, and phosphorus is a two-step metabolic pathway. The first step, catalyzed by AEP transaminase, involves the transfer of NH3 from AEP to pyruvate, yielding phosphonoacetaldehyde (P-Ald) and alanine. In the second step, phosphonatase catalyzes the hydrolytic P-C bond cleavage of P-Ald to form orthophosphate and acetaldehyde. 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: 319785 [Multi-domain]  Cd Length: 242  Bit Score: 48.84  E-value: 4.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   7 IKAAIFDMDGLLIDS---EPLwlQAELDIFTALGLDTSSRDSLPDTLGLRIDLVVKLwyQTMP-----WQ-----GPSQE 73
Cdd:cd02586     1 IEAVIFDWAGTTVDYgsfAPV--NAFVEAFAQRGVQITLEEARKPMGLLKIDHIRAL--LEMPrvaeaWRavfgrLPTEA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  74 EVcNRIIAR------AIdLVEDTRPVlPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYF-DCLVSAEYLPY 146
Cdd:cd02586    77 DV-DALYEEfepiliAS-LAEYSSPI-PGVLEVIAKLRARGIKIGSTTGYTREMMDIVLPEAAAQGYRpDSLVTPDDVPA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1518078120 147 SKPHPEVYLNAAAQLDVDPL-QCVTLEDSVNGMIATKAARMRSI 189
Cdd:cd02586   154 GRPYPWMCYKNAIELGVYDVaAVVKVGDTVPDIKEGLNAGMWTV 197
PRK11587 PRK11587
putative phosphatase; Provisional
 138-216 1.68e-06

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 46.91  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120 138 LVSAEYLPYSKPHPEVYLNAAAQLDVDPLQCVTLEDSVNGMIATKAARMRSIVipsVEYRAD-PRWALADIQLESLDQLR 216
Cdd:PRK11587  128 FVTAERVKRGKPEPDAYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAGCHVIA---VNAPADtPRLDEVDLVLHSLEQLT 204
PLN02811 PLN02811
hydrolase
 90-213 2.56e-06

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 46.67  E-value: 2.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  90 TRPVLPGVEYALALCRQQGLKIGLASASPLHM--------QERVLAMLGVEKYFDCLVSAeylpySKPHPEVYLNAAAQL 161
Cdd:PLN02811   76 TSDLMPGAERLVRHLHAKGIPIAIATGSHKRHfdlktqrhGELFSLMHHVVTGDDPEVKQ-----GKPAPDIFLAAARRF 150

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120 162 ---DVDPLQCVTLEDSVNGMIATKAARMRSIVIPsveyraDPRWAL-----ADIQLESLD 213
Cdd:PLN02811  151 edgPVDPGKVLVFEDAPSGVEAAKNAGMSVVMVP------DPRLDKsyckgADQVLSSLL 204
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
 6-189 3.64e-06

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 46.39  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   6 PIKAAIFDMDGLLIDS---EPLwlQAELDIFTALGLDTSSRDSLPDTLGLRIDLVVKLWyqTMP-----WQG----PSQE 73
Cdd:PRK13478    3 KIQAVIFDWAGTTVDFgsfAPT--QAFVEAFAQFGVEITLEEARGPMGLGKWDHIRALL--KMPrvaarWQAvfgrLPTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  74 EVCNRIIARAID-----LVEDTRPVlPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYF-DCLVSAEYLPYS 147
Cdd:PRK13478   79 ADVDALYAAFEPlqiakLADYATPI-PGVLEVIAALRARGIKIGSTTGYTREMMDVVVPLAAAQGYRpDHVVTTDDVPAG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1518078120 148 KPHPEVYLNAAAQLDVDPLQ-CVTLEDSVNGMIATKAARMRSI 189
Cdd:PRK13478  158 RPYPWMALKNAIELGVYDVAaCVKVDDTVPGIEEGLNAGMWTV 200
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 92-165 5.17e-06

2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related.


Pssm-ID: 130495 [Multi-domain]  Cd Length: 198  Bit Score: 45.41  E-value: 5.17e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1518078120  92 PVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQLDVDP 165
Cdd:TIGR01428  92 PPHPDVPAGLRALKERGYRLAILSNGSPAMLKSLVKHAGLDDPFDAVLSADAVRAYKPAPQVYQLALEALGVPP 165
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 100-218 5.29e-06

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: 44.20  E-value: 5.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120 100 ALALCRQQGLKIGLAS-ASPLhmQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQLDVDPLQCVTLEDS-VNG 177
Cdd:cd16415    15 TLKDLKEKGLKLAVVSnFDRR--LRELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALHVGDDlKND 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1518078120 178 MIATKAARMRSIVIpsveYRADPRWALADIqLESLDQLRKD 218
Cdd:cd16415    93 YLGARAVGWHALLV----DREGALHELPSL-ANLLERLLEL 128
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 8-189 6.88e-06

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 45.62  E-value: 6.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   8 KAAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLPDTLGLRIDLVVKLWYQTMPWQGPSQEEVCNRIIARAIDLV 87
Cdd:PRK13223   14 RLVMFDLDGTLVDSVPDLAAAVDRMLLELGRPPAGLEAVRHWVGNGAPVLVRRALAGSIDHDGVDDELAEQALALFMEAY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  88 EDTRP---VLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEYLPYSKPHPEVYLNAAAQLDVD 164
Cdd:PRK13223   94 ADSHEltvVYPGVRDTLKWLKKQGVEMALITNKPERFVAPLLDQMKIGRYFRWIIGGDTLPQKKPDPAALLFVMKMAGVP 173

                         170       180
                  ....*....|....*....|....*
gi 1518078120 165 PLQCVTLEDSVNGMIATKAARMRSI 189
Cdd:PRK13223  174 PSQSLFVGDSRSDVLAAKAAGVQCV 198
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 6-132 8.88e-06

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 44.83  E-value: 8.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   6 PIKAAIFDMDGLLIDSEPLWLQAEldiftALGldtSSRDSLPDTLGLRIDLVVKLW------YQTM------PWQGPSQE 73
Cdd:COG0560     2 KMRLAVFDLDGTLIAGESIDELAR-----FLG---RRGLVDRREVLEEVAAITERAmageldFEESlrfrvaLLAGLPEE 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1518078120  74 EVcNRIIARaidLVEDTRPVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVE 132
Cdd:COG0560    74 EL-EELAER---LFEEVPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGID 128
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 110-191 3.55e-05

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and CMP. 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: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 43.01  E-value: 3.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120 110 KIGLASASPLHMQeRVLAMLGVEKYFDCLVSAEYL-PYSKPHPEVYLNAAAQLDVDPLQCVTLEDSVNGMIATKAARMRS 188
Cdd:cd02604    99 KIIFTNASKNHAI-RVLKRLGLADLFDGIFDIEYAgPDPKPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKT 177


                  ...
gi 1518078120 189 IVI 191
Cdd:cd02604   178 VLV 180
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 9-137 4.31e-05

phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase PGP/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: 319799 [Multi-domain]  Cd Length: 201  Bit Score: 42.73  E-value: 4.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   9 AAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLPDTLGLRIDLVVKlWYQTMPWQGPsqeevcnRIIARAIDLVE 88
Cdd:cd04303     1 LIIFDFDGTLADSFPWFLSILNQLAARHGFKTVDEEEIEQLRQLSSREILK-QLGVPLWKLP-------LIAKDFRRLMA 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1518078120  89 DTRPVL---PGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDC 137
Cdd:cd04303    73 EAAPELalfPGVEDMLRALHARGVRLAVVSSNSEENIRRVLGPEELISLFAV 124
HAD pfam12710
haloacid dehalogenase-like hydrolase;
10-132 7.34e-05

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 42.13  E-value: 7.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  10 AIFDMDGLLIDSeplwlqaelDIFTALGLDTSSRDSLPDTLGLRIDLVVKLWYQTMPWQGPSQEEVCNRIIARAIDLVED 89
Cdd:pfam12710   1 ALFDLDGTLLDG---------DSLFLLIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLPEEDAA 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1518078120  90 ----------TRPVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVE 132
Cdd:pfam12710  72 elerfvaevaLPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFD 124
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 11-191 8.67e-05

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. 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: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 42.19  E-value: 8.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  11 IFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLPDTLGLRIdlvvklwYQTMPWQGPSQEEVCNRII--------AR 82
Cdd:cd04302     3 LFDLDGTLTDSAEGITASVQYALEELGIPVPDESELRRFIGPPL-------EDSFRELLPFDEEEAQRAVdayreyykEK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  83 AIDLVEdtrpVLPGVEYALALCRQQGLKIGLASASPLHMQERVLAMLGVEKYFDCLVSAEyLPYSKPH-PEVYLNAAAQL 161
Cdd:cd04302    76 GLFENE----VYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAGAS-LDGSRVHkADVIRYALDTL 150

                         170       180       190
                  ....*....|....*....|....*....|
gi 1518078120 162 DVDPLQCVTLEDSVNGMIATKAARMRSIVI 191
Cdd:cd04302   151 GIAPEQAVMIGDRKHDIIGARANGIDSIGV 180
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 9-164 2.32e-03

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases


Pssm-ID: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 37.36  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120   9 AAIFDMDGLLIDSEPLWLQAELDIFTALGLDTSSRDSLPDTLGLRIDLVVKLWyqtmpWQGPSQEEVCNRIIARaidlvE 88
Cdd:cd07523     1 NFIWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIIKESSVQFAIQYY-----AEVPDLEEEYKELEAE-----Y 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518078120  89 DTRPVL-PGVEYALALCRQQGLKIGLASasplHMQERVLAML---GVEKYFDCLVSAEYLPYSKPHPEV--YLNAAAQLD 162
Cdd:cd07523    71 LAKPILfPGAKAVLRWIKEQGGKNFLMT----HRDHSALTILkkdGIASYFTEIVTSDNGFPRKPNPEAinYLLNKYQLN 146


                  ..
gi 1518078120 163 VD 164
Cdd:cd07523   147 PE 148
 
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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