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Conserved domains on  [gi|157823059|ref|NP_001099509|]
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magnesium-dependent phosphatase 1 isoform 2 [Rattus norvegicus]

Protein Classification

magnesium-dependent phosphatase-1( domain architecture ID 10577417)

magnesium-dependent phosphatase-1 (MDP-1) may act as a tyrosine phosphatase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Acid_PPase pfam12689
Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD ...
 3-160 2.94e-86

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: 249.84  E-value: 2.94e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059    3 RLPKLAVFDLDYTLWPFWVDTHVDPPFHKSSDG-TVRDRRGQDIRLYPEVPEILGRLQSLGVPVAAASRTSEIEGANQLL 81
Cdd:pfam12689   1 PLPKLIVFDLDYTLWPFWVDTHVSPPFKKVSNGsRVVDRRGEELSLYPDVPSILQELKTRGVTLAAASRTDAPDWARELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059   82 ELFDLG----------KYFIQREIYPGSKVTHFERLRNKTGVPFSQMIFFDDENRNIIDVGKLGVTCIHIQDGMSLQMLT 151
Cdd:pfam12689  81 KLLHINdgpgdtvpaiDYFDDLEIYPGSKTKHFTKILKKSGIPYSDMLFFDDESRNIDVVSRLGVTFVLVPDGLTREEFE 160


                  ....*....
gi 157823059  152 QGLETFAKA 160
Cdd:pfam12689 161 RGLRKWRKR 169
 
Name Accession Description Interval E-value
Acid_PPase pfam12689
Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD ...
 3-160 2.94e-86

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: 249.84  E-value: 2.94e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059    3 RLPKLAVFDLDYTLWPFWVDTHVDPPFHKSSDG-TVRDRRGQDIRLYPEVPEILGRLQSLGVPVAAASRTSEIEGANQLL 81
Cdd:pfam12689   1 PLPKLIVFDLDYTLWPFWVDTHVSPPFKKVSNGsRVVDRRGEELSLYPDVPSILQELKTRGVTLAAASRTDAPDWARELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059   82 ELFDLG----------KYFIQREIYPGSKVTHFERLRNKTGVPFSQMIFFDDENRNIIDVGKLGVTCIHIQDGMSLQMLT 151
Cdd:pfam12689  81 KLLHINdgpgdtvpaiDYFDDLEIYPGSKTKHFTKILKKSGIPYSDMLFFDDESRNIDVVSRLGVTFVLVPDGLTREEFE 160


                  ....*....
gi 157823059  152 QGLETFAKA 160
Cdd:pfam12689 161 RGLRKWRKR 169
HAD_MDP-1_like cd07501
eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to ...
 5-141 9.23e-69

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: 204.50  E-value: 9.23e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059   5 PKLAVFDLDYTLWPFWVDTHVDPPFHkssdgtvrDRRGQDIRLYPEVPEILGRLQSLGVPVAAASRTSEIEGANQLLELF 84
Cdd:cd07501    1 PKCLVFDLDYTLWPGVVDEHGIPPFK--------DRGGKEVSLYPDAQEILKELKERGILLAVASRNNEFDHANEVLEKL 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157823059  85 DLGKYFIQREIYPGSKVTHFERLRNKTGVPFSQMIFFDDENRNIIDVGKLGVTCIHI 141
Cdd:cd07501   73 DLKELFDAFEIYPGSKSSHFRKIAKELGIGFDSMVFFDDEPRNREEVSEGGVTCILV 129
MDP-1 TIGR01685
magnesium-dependent phosphatase-1; This model represents two closely related clades of ...
 4-155 8.65e-32

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: 111.86  E-value: 8.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059    4 LPKLAVFDLDYTLWPFWVDTHVDPPF--HKSSDGTVRDRRGQDIRLYPEVPEILGRLQSLGVPVAAASRTSEIEGANQLL 81
Cdd:TIGR01685   1 LPRVIVFDLDGTLWDHYMISLLGGPFkpVKQNNSIIIDKSGTEVTLIKEVRDVLQTLKDAGTYLATASWNDVPEWAYEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059   82 ELFD---------LGKYF-IQREIYPGSKVTHFE----RLRNKTGV--PFSQMIFFDDENRNIIDVGKLGVTCIHIQDGM 145
Cdd:TIGR01685  81 GTFEityagktvpMHSLFdDRIEIYKPNKAKQLEmilqKVNKVDPSvlKPAQILFFDDRTDNVREVWGYGVTSCYCPSGM 160

                         170
                  ....*....|
gi 157823059  146 SLQMLTQGLE 155
Cdd:TIGR01685 161 DKGTFKKILE 170
COG4996 COG4996
Predicted phosphatase [General function prediction only];
4-141 1.28e-13

Predicted phosphatase [General function prediction only];


Pssm-ID: 444020  Cd Length: 165  Bit Score: 64.63  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059   4 LPKLAVFDLDYTLWpfwvdTHVD-----PPFHKSSDGTVRDRRGQDIRLYPEVPEILGRLQSLGVPVAAASRTSEiEGAN 78
Cdd:COG4996    2 MIKLLVLDLDGTLW-----DHHNiselkPPFKRISENSIVDSYGREVRLFPDVREFLEWAKERGAILSTASWNVP-DKAL 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157823059  79 QLLELFDLGKYF--IQREIYPG-----SKVthFERLRNKT-GVPFSQMIFFDDENRNIIDVGK-LG-VTCIHI 141
Cdd:COG4996   76 EALEALGLDEYFdyPVIEPHPYkflmlEEI--LRRLKERGiKIKPDEIVYVDDRRIHFGNIWLyVGdVKFIEM 146
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 45-143 2.37e-04

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 39.64  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059  45 IRLYPEVPEILGRLQSLGVPVAAASRTS------------EIEGANQLLELF-DLGKYFIQREIYpgskvthfERLRNKT 111
Cdd:PRK09456  83 VALRPEVIAIMHKLREQGHRVVVLSNTNrlhttfwpeeypEVRAAADHIYLSqDLGMRKPEARIY--------QHVLQAE 154

                         90       100       110
                 ....*....|....*....|....*....|..
gi 157823059 112 GVPFSQMIFFDDENRNIIDVGKLGVTCIHIQD 143
Cdd:PRK09456 155 GFSAADAVFFDDNADNIEAANALGITSILVTD 186
 
Name Accession Description Interval E-value
Acid_PPase pfam12689
Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD ...
 3-160 2.94e-86

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: 249.84  E-value: 2.94e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059    3 RLPKLAVFDLDYTLWPFWVDTHVDPPFHKSSDG-TVRDRRGQDIRLYPEVPEILGRLQSLGVPVAAASRTSEIEGANQLL 81
Cdd:pfam12689   1 PLPKLIVFDLDYTLWPFWVDTHVSPPFKKVSNGsRVVDRRGEELSLYPDVPSILQELKTRGVTLAAASRTDAPDWARELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059   82 ELFDLG----------KYFIQREIYPGSKVTHFERLRNKTGVPFSQMIFFDDENRNIIDVGKLGVTCIHIQDGMSLQMLT 151
Cdd:pfam12689  81 KLLHINdgpgdtvpaiDYFDDLEIYPGSKTKHFTKILKKSGIPYSDMLFFDDESRNIDVVSRLGVTFVLVPDGLTREEFE 160


                  ....*....
gi 157823059  152 QGLETFAKA 160
Cdd:pfam12689 161 RGLRKWRKR 169
HAD_MDP-1_like cd07501
eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to ...
 5-141 9.23e-69

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: 204.50  E-value: 9.23e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059   5 PKLAVFDLDYTLWPFWVDTHVDPPFHkssdgtvrDRRGQDIRLYPEVPEILGRLQSLGVPVAAASRTSEIEGANQLLELF 84
Cdd:cd07501    1 PKCLVFDLDYTLWPGVVDEHGIPPFK--------DRGGKEVSLYPDAQEILKELKERGILLAVASRNNEFDHANEVLEKL 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157823059  85 DLGKYFIQREIYPGSKVTHFERLRNKTGVPFSQMIFFDDENRNIIDVGKLGVTCIHI 141
Cdd:cd07501   73 DLKELFDAFEIYPGSKSSHFRKIAKELGIGFDSMVFFDDEPRNREEVSEGGVTCILV 129
MDP-1 TIGR01685
magnesium-dependent phosphatase-1; This model represents two closely related clades of ...
 4-155 8.65e-32

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: 111.86  E-value: 8.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059    4 LPKLAVFDLDYTLWPFWVDTHVDPPF--HKSSDGTVRDRRGQDIRLYPEVPEILGRLQSLGVPVAAASRTSEIEGANQLL 81
Cdd:TIGR01685   1 LPRVIVFDLDGTLWDHYMISLLGGPFkpVKQNNSIIIDKSGTEVTLIKEVRDVLQTLKDAGTYLATASWNDVPEWAYEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059   82 ELFD---------LGKYF-IQREIYPGSKVTHFE----RLRNKTGV--PFSQMIFFDDENRNIIDVGKLGVTCIHIQDGM 145
Cdd:TIGR01685  81 GTFEityagktvpMHSLFdDRIEIYKPNKAKQLEmilqKVNKVDPSvlKPAQILFFDDRTDNVREVWGYGVTSCYCPSGM 160

                         170
                  ....*....|
gi 157823059  146 SLQMLTQGLE 155
Cdd:TIGR01685 161 DKGTFKKILE 170
COG4996 COG4996
Predicted phosphatase [General function prediction only];
4-141 1.28e-13

Predicted phosphatase [General function prediction only];


Pssm-ID: 444020  Cd Length: 165  Bit Score: 64.63  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059   4 LPKLAVFDLDYTLWpfwvdTHVD-----PPFHKSSDGTVRDRRGQDIRLYPEVPEILGRLQSLGVPVAAASRTSEiEGAN 78
Cdd:COG4996    2 MIKLLVLDLDGTLW-----DHHNiselkPPFKRISENSIVDSYGREVRLFPDVREFLEWAKERGAILSTASWNVP-DKAL 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157823059  79 QLLELFDLGKYF--IQREIYPG-----SKVthFERLRNKT-GVPFSQMIFFDDENRNIIDVGK-LG-VTCIHI 141
Cdd:COG4996   76 EALEALGLDEYFdyPVIEPHPYkflmlEEI--LRRLKERGiKIKPDEIVYVDDRRIHFGNIWLyVGdVKFIEM 146
HAD-SF-IIIC TIGR01681
HAD-superfamily phosphatase, subfamily IIIC; This model represents the IIIC subfamily of the ...
 6-135 2.69e-09

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: 52.43  E-value: 2.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059    6 KLAVFDLDYTLWpfwvdTHVDPPFHKSSDGTVRDRrgqdirlYPEVPEILGRLQSLGVPVAAASRTSEIEGANQLLELF- 84
Cdd:TIGR01681   1 KVIVFDLDNTLW-----TGENIVVGEDPIIDLEVT-------IKEIRDKLQTLKKNGFLLALASYNDDPHVAYELLKIFe 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059   85 DLGKYFIQREIY---------PGSKVTHFERLRNKTGVPFSQMIFFDDENRNIIDVGKLG 135
Cdd:TIGR01681  69 DFGIIFPLAEYFdpltigywlPKSPRLVEIALKLNGVLKPKSILFVDDRPDNNEEVDYYL 128
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
38-141 2.00e-07

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 48.77  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059  38 RDRRGQDIRLYPEVPEILGRLQSLGVPVAAASRTSEiEGANQLLELFDLGKYF--IQ-REIYPGSK--VTHFERLRNKTG 112
Cdd:COG0546   76 EEELLDETRLFPGVRELLEALKARGIKLAVVTNKPR-EFAERLLEALGLDDYFdaIVgGDDVPPAKpkPEPLLEALERLG 154

                         90       100
                 ....*....|....*....|....*....
gi 157823059 113 VPFSQMIFFDDENRNIIDVGKLGVTCIHI 141
Cdd:COG0546  155 LDPEEVLMVGDSPHDIEAARAAGVPFIGV 183
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 38-144 4.42e-07

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: 47.72  E-value: 4.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059  38 RDRRGQDIRLYPEVPEILGRLQSLGVPVAAASRTSEiEGANQLLELFDLGKYFiqREIYPGSKVTH-------FERLRNK 110
Cdd:COG1011   85 LAALPELVEPYPDALELLEALKARGYRLALLTNGSA-ELQEAKLRRLGLDDLF--DAVVSSEEVGVrkpdpeiFELALER 161

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 157823059 111 TGVPFSQMIFFDDENRNIIDVGK-LGVTCIHIQDG 144
Cdd:COG1011  162 LGVPPEEALFVGDSPETDVAGARaAGMRTVWVNRS 196
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 7-141 2.40e-06

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: 43.92  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059   7 LAVFDLDYTLWpfwvdthvdppfhkssdgtvrdrrgqdirlypeVPEILGRLQSLGVPVAAASRTSEIEgANQLLELFDL 86
Cdd:cd01427    1 AVLFDLDGTLL---------------------------------AVELLKRLRAAGIKLAIVTNRSREA-LRALLEKLGL 46

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059  87 GKYFIQ-----REIYPGSKVTHFERLRNKTGVPFSQMIFFDDENRNIIDVGKLGVTCIHI 141
Cdd:cd01427   47 GDLFDGiigsdGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAGGRTVAV 106
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 40-141 1.40e-04

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 40.10  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059   40 RRGQDIRLYPEVPEILGRLQSLGVPVAAASRTSEIEGANQL-LELFDLGKYFIQREIYPGSKVTH--FERLRNKTGVPFS 116
Cdd:TIGR01509  74 EEEAKLKPLPGVRALLEALRARGKKLALLTNSPRAHKLVLAlLGLRDLFDVVIDSSDVGLGKPDPdiYLQALKALGLEPS 153

                          90       100
                  ....*....|....*....|....*
gi 157823059  117 QMIFFDDENRNIIDVGKLGVTCIHI 141
Cdd:TIGR01509 154 ECVFVDDSPAGIEAAKAAGMHTVGV 178
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 45-143 2.37e-04

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 39.64  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059  45 IRLYPEVPEILGRLQSLGVPVAAASRTS------------EIEGANQLLELF-DLGKYFIQREIYpgskvthfERLRNKT 111
Cdd:PRK09456  83 VALRPEVIAIMHKLREQGHRVVVLSNTNrlhttfwpeeypEVRAAADHIYLSqDLGMRKPEARIY--------QHVLQAE 154

                         90       100       110
                 ....*....|....*....|....*....|..
gi 157823059 112 GVPFSQMIFFDDENRNIIDVGKLGVTCIHIQD 143
Cdd:PRK09456 155 GFSAADAVFFDDNADNIEAANALGITSILVTD 186
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 32-147 5.01e-04

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: 38.86  E-value: 5.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059  32 SSDGTVRDRRGQDIRLYPEVPEILGRLQSLGVPVAAASRTSEIEGANQLLELFDLGKYFiqREIYPGSKVTH-------F 104
Cdd:cd02603   70 LSAELFEELVLAAVDPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDLF--DGVVESCRLGVrkpdpeiY 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 157823059 105 ERLRNKTGVPFSQMIFFDDENRNIIDVGKLGVTCIHIQDGMSL 147
Cdd:cd02603  148 QLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAEDA 190
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
4-139 5.02e-04

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 38.72  E-value: 5.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059    4 LPKLAVFDLDYTLWPFWVDTHVDPPFHKSsdgtvrdrrgqdIRLYPEVPEILGRLQSLGVPVA-AASRTSEIegANQLLE 82
Cdd:pfam13419  49 FRYLGVSEDEEEKIEFYLRKYNEELHDKL------------VKPYPGIKELLEELKEQGYKLGiVTSKSREN--VEEFLK 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157823059   83 LFDLGKYFiqREIYPGSKVTH-------FERLRNKTGVPFSQMIFFDDENRNIIDVGKLGVTCI 139
Cdd:pfam13419 115 QLGLEDYF--DVIVGGDDVEGkkpdpdpILKALEQLGLKPEEVIYVGDSPRDIEAAKNAGIKVI 176
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 8-123 1.25e-03

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: 37.21  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059   8 AVFDLDYTLwpfwVDTHvdpPFH--------KSSDGTVRDRRGQDIRLYPEVPEILGRLQSLGVPVAAASRTSEIEGANQ 79
Cdd:cd07505    2 VIFDMDGVL----IDTE---PLHrqawqlleRKNALLLELIASEGLKLKPGVVELLDALKAAGIPVAVATSSSRRNVELL 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157823059  80 LLELFDLGKYFIQreIYPGSKVTH-------FERLRNKTGVPFSQMIFFDD 123
Cdd:cd07505   75 LLELGLLRGYFDV--IVSGDDVERgkpapdiYLLAAERLGVDPERCLVFED 123
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 40-139 1.49e-03

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: 37.34  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823059  40 RRGQDIRLYPEVPEILGRLQSLGVPVAAASRTSE-----IEGANQLLELFDlgkYFIQREIYpgSKVTHFERLRNKTGVP 114
Cdd:cd04303   73 EAAPELALFPGVEDMLRALHARGVRLAVVSSNSEenirrVLGPEELISLFA---VIEGSSLF--GKAKKIRRVLRRTKIT 147

                         90       100
                 ....*....|....*....|....*
gi 157823059 115 FSQMIFFDDENRNIIDVGKLGVTCI 139
Cdd:cd04303  148 AAQVIYVGDETRDIEAARKVGLAFA 172
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 46-90 1.68e-03

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: 37.21  E-value: 1.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 157823059  46 RLYPEVPEILGRLQSLGVPVAAASRTSEIEgANQLLELFDLGKYF 90
Cdd:cd16417   87 HLYPGVKEGLAALKAQGYPLACVTNKPERF-VAPLLEALGISDYF 130
PTZ00445 PTZ00445
p36-lilke protein; Provisional
 97-147 2.03e-03

p36-lilke protein; Provisional


Pssm-ID: 240421  Cd Length: 219  Bit Score: 36.99  E-value: 2.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157823059  97 PGSKVTHFERLRNKTGVPFSQMIFFDDENRNIIDVGKLGVTCIHI--QDGMSL 147
Cdd:PTZ00445 160 PLDKSYHLKQVCSDFNVNPDEILFIDDDMNNCKNALKEGYIALHVtgNEGFSF 212
 
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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