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Conserved domains on  [gi|1008856398|gb|KYK38947|]
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hypothetical protein AYK18_00325 [Theionarchaea archaeon DG-70]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 2-141 2.68e-12

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


The actual alignment was detected with superfamily member cd07501:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 129  Bit Score: 60.05  E-value: 2.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008856398   2 LVIFDGDGTLWSGdVLAGYLTTPLHqidentveDHQGKRIQLKEGVIDVLRELRSRNIYVALASENRKLPV-IALLRRLQ 80
Cdd:cd07501     3 CLVFDLDYTLWPG-VVDEHGIPPFK--------DRGGKEVSLYPDAQEILKELKERGILLAVASRNNEFDHaNEVLEKLD 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1008856398  81 IAQYFNFLEVAWNEKDEMVLEILKifvRKNKDTGKVFFVDDFGYNIEIVQANpelsHITCI 141
Cdd:cd07501    74 LKELFDAFEIYPGSKSSHFRKIAK---ELGIGFDSMVFFDDEPRNREEVSEG----GVTCI 127
 
Name Accession Description Interval E-value
HAD_MDP-1_like cd07501
eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to ...
 2-141 2.68e-12

eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to Bacillus cereus phosphonoacetaldehyde hydrolase and Streptomyces FkbH; This family includes eukaryotic magnesium-dependent phosphatase-1 (MDP-1) which is most likely a phosphotyrosine phosphatase catalyzing the dephosphorylation of tyrosine-phosphorylated proteins, Bacillus cereus phosphonoacetaldehyde hydrolase (phosphonatase)which catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor, and sequences annotated as FkbH including BafAIV an FkbH-like protein from Streptomyces griseus encoded in ORF12 of the bafilomycin synthesis gene cluster. 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: 319804 [Multi-domain]  Cd Length: 129  Bit Score: 60.05  E-value: 2.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008856398   2 LVIFDGDGTLWSGdVLAGYLTTPLHqidentveDHQGKRIQLKEGVIDVLRELRSRNIYVALASENRKLPV-IALLRRLQ 80
Cdd:cd07501     3 CLVFDLDYTLWPG-VVDEHGIPPFK--------DRGGKEVSLYPDAQEILKELKERGILLAVASRNNEFDHaNEVLEKLD 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1008856398  81 IAQYFNFLEVAWNEKDEMVLEILKifvRKNKDTGKVFFVDDFGYNIEIVQANpelsHITCI 141
Cdd:cd07501    74 LKELFDAFEIYPGSKSSHFRKIAK---ELGIGFDSMVFFDDEPRNREEVSEG----GVTCI 127
Acid_PPase pfam12689
Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD ...
 2-130 2.45e-10

Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD superfamily. It includes MDP-1 which is a eukaryotic magnesium-dependent acid phosphatase.


Pssm-ID: 372256  Cd Length: 169  Bit Score: 55.70  E-value: 2.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008856398   2 LVIFDGDGTLWSGDVLAgYLTTPLHQIDEN-TVEDHQGKRIQLKEGVIDVLRELRSRNIYVALASE-NRklPVIA--LLR 77
Cdd:pfam12689   5 LIVFDLDYTLWPFWVDT-HVSPPFKKVSNGsRVVDRRGEELSLYPDVPSILQELKTRGVTLAAASRtDA--PDWAreLLK 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1008856398  78 RLQI----------AQYFNFLEVAWNEKdemvleiLKIFVRKNKDTG----KVFFVDDFGYNIEIVQ 130
Cdd:pfam12689  82 LLHIndgpgdtvpaIDYFDDLEIYPGSK-------TKHFTKILKKSGipysDMLFFDDESRNIDVVS 141
HAD-SF-IIIC TIGR01681
HAD-superfamily phosphatase, subfamily IIIC; This model represents the IIIC subfamily of the ...
 1-130 6.28e-07

HAD-superfamily phosphatase, subfamily IIIC; This model represents the IIIC subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate nucleophile hydrolases. Subfamily III (also including IIIA - TIGR01662 and IIIB - pfam03767) contains sequences which do not contain either of the insert domains (between the 1st and 2nd conserved catalytic motifs, subfamily I - TIGR01493, TIGR01509, TIGR01549, TIGR01488, TIGR01494, TIGR01658, TIGR01544 and TIGR01545, or between the 2nd and 3rd, subfamily II - TIGR01460 and TIGR01484). Subfamily IIIC contains five relatively distantly related clades: a family of viral proteins (TIGR01684), a family of eukaryotic proteins called MDP-1 and a family of archaeal proteins most closely related to MDP-1 (TIGR01685), a family of bacteria including the Streptomyces FkbH protein (TIGR01686), and a small clade including the Pasteurella BcbF and EcbF proteins. The overall lack of species overlap among these clades may indicate a conserved function, but the degree of divergence between the clades and the differences in archetecture outside of the domain in some clades warns against such a conclusion. No member of this subfamily is characterized with respect to function, however the MDP-1 protein is a characterized phosphatase. All of the characterized enzymes within subfamily III are phosphatases, and all of the active site residues characteristic of HAD-superfamily phosphatases are present in subfamily IIIC.


Pssm-ID: 273752 [Multi-domain]  Cd Length: 128  Bit Score: 45.88  E-value: 6.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008856398   1 MLVIFDGDGTLWsgdvlagylTTPLHQIDENTVEDHQGKRIQlkegVIDVLRELRSRNIYVALASENRKLPVIALLRRLQ 80
Cdd:TIGR01681   1 KVIVFDLDNTLW---------TGENIVVGEDPIIDLEVTIKE----IRDKLQTLKKNGFLLALASYNDDPHVAYELLKIF 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1008856398  81 I--------AQYF-NFLEVAWNEKDEMVLEILKIFVRKNKdTGKVFFVDDFGYNIEIVQ 130
Cdd:TIGR01681  68 EdfgiifplAEYFdPLTIGYWLPKSPRLVEIALKLNGVLK-PKSILFVDDRPDNNEEVD 125
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
34-121 1.11e-06

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 46.46  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008856398  34 EDHQGKRIQLKEGVIDVLRELRSRNIYVALASENRKLPVIALLRRLQIAQYFNFL-----EVAWNEKDEMVLEILKifvR 108
Cdd:COG0546    76 EEELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIvggddVPPAKPKPEPLLEALE---R 152

                          90
                  ....*....|...
gi 1008856398 109 KNKDTGKVFFVDD 121
Cdd:COG0546   153 LGLDPEEVLMVGD 165
 
Name Accession Description Interval E-value
HAD_MDP-1_like cd07501
eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to ...
 2-141 2.68e-12

eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to Bacillus cereus phosphonoacetaldehyde hydrolase and Streptomyces FkbH; This family includes eukaryotic magnesium-dependent phosphatase-1 (MDP-1) which is most likely a phosphotyrosine phosphatase catalyzing the dephosphorylation of tyrosine-phosphorylated proteins, Bacillus cereus phosphonoacetaldehyde hydrolase (phosphonatase)which catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor, and sequences annotated as FkbH including BafAIV an FkbH-like protein from Streptomyces griseus encoded in ORF12 of the bafilomycin synthesis gene cluster. 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: 319804 [Multi-domain]  Cd Length: 129  Bit Score: 60.05  E-value: 2.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008856398   2 LVIFDGDGTLWSGdVLAGYLTTPLHqidentveDHQGKRIQLKEGVIDVLRELRSRNIYVALASENRKLPV-IALLRRLQ 80
Cdd:cd07501     3 CLVFDLDYTLWPG-VVDEHGIPPFK--------DRGGKEVSLYPDAQEILKELKERGILLAVASRNNEFDHaNEVLEKLD 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1008856398  81 IAQYFNFLEVAWNEKDEMVLEILKifvRKNKDTGKVFFVDDFGYNIEIVQANpelsHITCI 141
Cdd:cd07501    74 LKELFDAFEIYPGSKSSHFRKIAK---ELGIGFDSMVFFDDEPRNREEVSEG----GVTCI 127
Acid_PPase pfam12689
Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD ...
 2-130 2.45e-10

Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD superfamily. It includes MDP-1 which is a eukaryotic magnesium-dependent acid phosphatase.


Pssm-ID: 372256  Cd Length: 169  Bit Score: 55.70  E-value: 2.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008856398   2 LVIFDGDGTLWSGDVLAgYLTTPLHQIDEN-TVEDHQGKRIQLKEGVIDVLRELRSRNIYVALASE-NRklPVIA--LLR 77
Cdd:pfam12689   5 LIVFDLDYTLWPFWVDT-HVSPPFKKVSNGsRVVDRRGEELSLYPDVPSILQELKTRGVTLAAASRtDA--PDWAreLLK 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1008856398  78 RLQI----------AQYFNFLEVAWNEKdemvleiLKIFVRKNKDTG----KVFFVDDFGYNIEIVQ 130
Cdd:pfam12689  82 LLHIndgpgdtvpaIDYFDDLEIYPGSK-------TKHFTKILKKSGipysDMLFFDDESRNIDVVS 141
HAD-SF-IIIC TIGR01681
HAD-superfamily phosphatase, subfamily IIIC; This model represents the IIIC subfamily of the ...
 1-130 6.28e-07

HAD-superfamily phosphatase, subfamily IIIC; This model represents the IIIC subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate nucleophile hydrolases. Subfamily III (also including IIIA - TIGR01662 and IIIB - pfam03767) contains sequences which do not contain either of the insert domains (between the 1st and 2nd conserved catalytic motifs, subfamily I - TIGR01493, TIGR01509, TIGR01549, TIGR01488, TIGR01494, TIGR01658, TIGR01544 and TIGR01545, or between the 2nd and 3rd, subfamily II - TIGR01460 and TIGR01484). Subfamily IIIC contains five relatively distantly related clades: a family of viral proteins (TIGR01684), a family of eukaryotic proteins called MDP-1 and a family of archaeal proteins most closely related to MDP-1 (TIGR01685), a family of bacteria including the Streptomyces FkbH protein (TIGR01686), and a small clade including the Pasteurella BcbF and EcbF proteins. The overall lack of species overlap among these clades may indicate a conserved function, but the degree of divergence between the clades and the differences in archetecture outside of the domain in some clades warns against such a conclusion. No member of this subfamily is characterized with respect to function, however the MDP-1 protein is a characterized phosphatase. All of the characterized enzymes within subfamily III are phosphatases, and all of the active site residues characteristic of HAD-superfamily phosphatases are present in subfamily IIIC.


Pssm-ID: 273752 [Multi-domain]  Cd Length: 128  Bit Score: 45.88  E-value: 6.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008856398   1 MLVIFDGDGTLWsgdvlagylTTPLHQIDENTVEDHQGKRIQlkegVIDVLRELRSRNIYVALASENRKLPVIALLRRLQ 80
Cdd:TIGR01681   1 KVIVFDLDNTLW---------TGENIVVGEDPIIDLEVTIKE----IRDKLQTLKKNGFLLALASYNDDPHVAYELLKIF 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1008856398  81 I--------AQYF-NFLEVAWNEKDEMVLEILKIFVRKNKdTGKVFFVDDFGYNIEIVQ 130
Cdd:TIGR01681  68 EdfgiifplAEYFdPLTIGYWLPKSPRLVEIALKLNGVLK-PKSILFVDDRPDNNEEVD 125
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 3-88 6.62e-07

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: 46.48  E-value: 6.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008856398   3 VIFDGDGTLWSGDVLAGYLTT----------PLHQIDENTVedhqgkrIQLKEGVIDVLRELRSRNIYVALASENRKLPV 72
Cdd:cd16423     2 VIFDFDGVIVDTEPLWYEAWQellnerrnelIKRQFSEKTD-------LPPIEGVKELLEFLKEKGIKLAVASSSPRRWI 74

                          90
                  ....*....|....*.
gi 1008856398  73 IALLRRLQIAQYFNFL 88
Cdd:cd16423    75 EPHLERLGLLDYFEVI 90
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
34-121 1.11e-06

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 46.46  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008856398  34 EDHQGKRIQLKEGVIDVLRELRSRNIYVALASENRKLPVIALLRRLQIAQYFNFL-----EVAWNEKDEMVLEILKifvR 108
Cdd:COG0546    76 EEELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIvggddVPPAKPKPEPLLEALE---R 152

                          90
                  ....*....|...
gi 1008856398 109 KNKDTGKVFFVDD 121
Cdd:COG0546   153 LGLDPEEVLMVGD 165
FkbH TIGR01686
FkbH-like domain; This model describes a domain of a family of proteins of unknown overall ...
 3-140 1.20e-06

FkbH-like domain; This model describes a domain of a family of proteins of unknown overall function. One of these, however, is a modular polyketide synthase 4800 amino acids in length from Streptomyces avermilitis in which this domain is the C-terminal segment. By contrast, the FkbH protein from Streptomyces hygroscopicus aparently contains only this domain. The remaining members of the family all contain an additional N-terminal domain of between 200 and 275 amino acids which show less than 20% identity to one another. It seems likely then that these proteins are involved in disparate functions, probably the biosynthesis of different natural products. For instance, the FkbH gene is found in a gene cluster believed to be responsible for the biosynthesis of unususal "PKS extender units" in the ascomycin pathway. This domain is composed of two parts, the first of which is a member of subfamily IIIC (TIGR01681) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. All of the characterized enzymes within subfamily III are phosphatases, and all of the active site residues characteristic of HAD-superfamily phosphatases are present in this domain. The C-terminal portion of this domain is unique to this family (by BLAST).


Pssm-ID: 273757 [Multi-domain]  Cd Length: 320  Bit Score: 46.77  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008856398   3 VIFDGDGTLWSGDVLagylttplhQIDENTVeDHQGKRIQLKEgvidVLRELRSRNIYVALASENRKLPVIALLRR---- 78
Cdd:TIGR01686   6 LVLDLDNTLWGGVLG---------EDGIDNL-NLSPLHKTLQE----KIKTLKKQGFLLALASKNDEDDAKKVFERrkdf 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1008856398  79 LQIAQYFNFLEVAWNEKDEMVLEILKIFvrkNKDTGKVFFVDDFGYNIEIVQAnpELSHITC 140
Cdd:TIGR01686  72 ILQAEDFDARSINWGPKSESLRKIAKKL---NLGTDSFLFIDDNPAERANVKI--TLPVKTL 128
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 3-85 1.65e-06

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: 44.91  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008856398   3 VIFDGDGTLwsgdvlagYLTTPLH--------QIDENTVEDHQGKRIQLKEGVIDVLRELRSRNIYVALASENRKLPVIA 74
Cdd:cd07505     2 VIFDMDGVL--------IDTEPLHrqawqlleRKNALLLELIASEGLKLKPGVVELLDALKAAGIPVAVATSSSRRNVEL 73

                          90
                  ....*....|.
gi 1008856398  75 LLRRLQIAQYF 85
Cdd:cd07505    74 LLLELGLLRGY 84
MDP-1 TIGR01685
magnesium-dependent phosphatase-1; This model represents two closely related clades of ...
 1-104 1.26e-05

magnesium-dependent phosphatase-1; This model represents two closely related clades of sequences from eukaryotes and archaea. The mouse enzyme has been characterized as a phosphatase and has been positively identified as a member of the haloacid dehalogenase (HAD) superfamily by site-directed mutagenesis of the active site residues.


Pssm-ID: 273756  Cd Length: 174  Bit Score: 43.30  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008856398   1 MLVIFDGDGTLWSG-DVLAGYLTTPLHQIDENTVEDHQGKRIQLKEGVIDVLRELRSRNIYVALASENrKLPVIA--LLR 77
Cdd:TIGR01685   3 RVIVFDLDGTLWDHyMISLLGGPFKPVKQNNSIIIDKSGTEVTLIKEVRDVLQTLKDAGTYLATASWN-DVPEWAyeILG 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1008856398  78 RLQI---------AQYFN-FLEVAWNEKDEMVLEILK 104
Cdd:TIGR01685  82 TFEItyagktvpmHSLFDdRIEIYKPNKAKQLEMILQ 118
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
3-88 3.66e-05

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 42.12  E-value: 3.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008856398   3 VIFDGDGTL---------------------WSGDVLAGYLTTPLHQI---------------------DENTVEDHQGKR 40
Cdd:COG0637     5 VIFDMDGTLvdseplharawreafaelgidLTEEEYRRLMGRSREDIlrylleeygldlpeeelaarkEELYRELLAEEG 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1008856398  41 IQLKEGVIDVLRELRSRNIYVALASENRKLPVIALLRRLQIAQYFNFL 88
Cdd:COG0637    85 LPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVI 132
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 24-87 1.31e-04

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: 40.35  E-value: 1.31e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1008856398  24 PLHQIDENTVEDhqgkriqLKEGVIDVLRELRSRNIYVALASENRKLPVIalLRRLQIAQYFNF 87
Cdd:cd02598    38 YVELIEELTPVD-------VLPGIASLLVDLKAKGIKIALASASKNAPKI--LEKLGLAEYFDA 92
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
39-91 8.55e-03

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 34.87  E-value: 8.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1008856398  39 KRIQLKEGVIDVLRELRSRNIYVALASENRKLPVIALLRRLQIAQYFNFLEVA 91
Cdd:pfam13419  76 KLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGG 128
 
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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