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Conserved domains on  [gi|85861235|ref|NP_001034291|]
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haloacid dehalogenase-like hydrolase domain-containing protein 2 isoform 2 [Mus musculus]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 8-132 3.09e-72

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 cd07509:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 248  Bit Score: 216.76  E-value: 3.09e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235   8 KAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIFTSLTAARNLIEQKQ 87
Cdd:cd07509   1 KAVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEKG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 85861235  88 VRPMLLVDDRALPEFTGVQTQDPNAVVIGLAPEHFHYQLLNQAFR 132
Cdd:cd07509  81 LRPHLLVDDDALEDFIGIDTSDPNAVVIGDAGEHFNYQTLNRAFR 125
 
Name Accession Description Interval E-value
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 8-132 3.09e-72

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. 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: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 216.76  E-value: 3.09e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235   8 KAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIFTSLTAARNLIEQKQ 87
Cdd:cd07509   1 KAVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEKG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 85861235  88 VRPMLLVDDRALPEFTGVQTQDPNAVVIGLAPEHFHYQLLNQAFR 132
Cdd:cd07509  81 LRPHLLVDDDALEDFIGIDTSDPNAVVIGDAGEHFNYQTLNRAFR 125
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 7-132 1.10e-61

HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of the IIA subfamily (TIGR01460) of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. One sequence (GP|10716807) has been annotated as a "phospholysine phosphohistidine inorganic pyrophosphatase," probably in reference to studies on similarly described (but unsequenced) enzymes from bovine and rat tissues. However, the supporting information for this annotation has never been published. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 162372 [Multi-domain]  Cd Length: 257  Bit Score: 190.07  E-value: 1.10e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235     7 LKAVLVDLNGTLHIEDA----AVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIFTSLTAARNL 82
Cdd:TIGR01458   1 VKGVLLDISGVLYISDAgggtAVPGSQEAVKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 85861235    83 IEQKQVRPMLLVDDRALPEFTGVQTQDPNAVVIGLAPEHFHYQLLNQAFR 132
Cdd:TIGR01458  81 LEEKQLRPMLLVDDRVLPDFDGIDTSDPNCVVMGLAPEHFSYQILNQAFR 130
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
8-137 3.34e-33

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 117.13  E-value: 3.34e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235   8 KAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIFTSLTAARNLIEQKQ 87
Cdd:COG0647   9 DAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLAERH 88

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 85861235  88 V--RPMLLVDDRALPEFTG-----VQTQDPNAVVIGLAPEhFHYQLLNQAFRRKQRG 137
Cdd:COG0647  89 PgaRVYVIGEEGLREELEEagltlVDDEEPDAVVVGLDRT-FTYEKLAEALRAIRRG 144
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 10-86 5.11e-22

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 84.05  E-value: 5.11e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 85861235    10 VLVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIFTSLTAARNLIEQK 86
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKER 77
PLN02645 PLN02645
phosphoglycolate phosphatase
 1-79 9.27e-09

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 52.41  E-value: 9.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235    1 MAARRALKAV---LVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIFTSLT 77
Cdd:PLN02645  19 ENADELIDSVetfIFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSF 98


                 ..
gi 85861235   78 AA 79
Cdd:PLN02645  99 AA 100
 
Name Accession Description Interval E-value
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 8-132 3.09e-72

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. 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: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 216.76  E-value: 3.09e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235   8 KAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIFTSLTAARNLIEQKQ 87
Cdd:cd07509   1 KAVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEKG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 85861235  88 VRPMLLVDDRALPEFTGVQTQDPNAVVIGLAPEHFHYQLLNQAFR 132
Cdd:cd07509  81 LRPHLLVDDDALEDFIGIDTSDPNAVVIGDAGEHFNYQTLNRAFR 125
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 7-132 1.10e-61

HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of the IIA subfamily (TIGR01460) of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. One sequence (GP|10716807) has been annotated as a "phospholysine phosphohistidine inorganic pyrophosphatase," probably in reference to studies on similarly described (but unsequenced) enzymes from bovine and rat tissues. However, the supporting information for this annotation has never been published. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 162372 [Multi-domain]  Cd Length: 257  Bit Score: 190.07  E-value: 1.10e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235     7 LKAVLVDLNGTLHIEDA----AVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIFTSLTAARNL 82
Cdd:TIGR01458   1 VKGVLLDISGVLYISDAgggtAVPGSQEAVKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 85861235    83 IEQKQVRPMLLVDDRALPEFTGVQTQDPNAVVIGLAPEHFHYQLLNQAFR 132
Cdd:TIGR01458  81 LEEKQLRPMLLVDDRVLPDFDGIDTSDPNCVVMGLAPEHFSYQILNQAFR 130
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
8-137 3.34e-33

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 117.13  E-value: 3.34e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235   8 KAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIFTSLTAARNLIEQKQ 87
Cdd:COG0647   9 DAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLAERH 88

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 85861235  88 V--RPMLLVDDRALPEFTG-----VQTQDPNAVVIGLAPEhFHYQLLNQAFRRKQRG 137
Cdd:COG0647  89 PgaRVYVIGEEGLREELEEagltlVDDEEPDAVVVGLDRT-FTYEKLAEALRAIRRG 144
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 10-86 5.11e-22

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 84.05  E-value: 5.11e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 85861235    10 VLVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIFTSLTAARNLIEQK 86
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKER 77
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 8-137 1.40e-16

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and 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: 319832 [Multi-domain]  Cd Length: 247  Bit Score: 73.40  E-value: 1.40e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235   8 KAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIFTS-LTAARNLIEQK 86
Cdd:cd07530   1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSaLATAQYLAEQL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 85861235  87 QVRPMLLVDDRALPE------FTGVQTqDPNAVVIGLAPeHFHYQLLNQAFRRKQRG 137
Cdd:cd07530  81 PGAKVYVIGEEGLRTalheagLTLTDE-NPDYVVVGLDR-DLTYEKLAEATLAIRNG 135
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
 8-137 1.19e-14

UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar phosphatase; Bacillus subtilis AraL is a phosphatase displaying activity towards different sugar phosphate substrates; it is encoded by the arabinose metabolic operon araABDLMNPQ-abfA and may play a role in the dephosphorylation of substrates related to l-arabinose metabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and 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: 319833 [Multi-domain]  Cd Length: 252  Bit Score: 68.36  E-value: 1.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235   8 KAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIFTSLTA-ARNLIEQK 86
Cdd:cd07531   1 KGYIIDLDGTIGKGVTLIPGAVEGVKTLRRLGKKIIFLSNNSTRSRRILLERLRSFGIEVGEDEILVSSYVtARFLAREK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 85861235  87 QVRPMLLVDDRALPE---FTGVQTQDP---NAVVIGLAPEHFHYQLLNQAFRRKQRG 137
Cdd:cd07531  81 PNAKVFVTGEEGLIEelrLAGLEIVDKydeAEYVVVGSNRKITYELLTKAFRACLRG 137
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 10-137 4.49e-14

Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural subclass of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The classes 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. Class I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Class II consists of sequences in which the capping domain is found between the second and third motifs. Class III sequences have no capping domain in iether of these positions. The Class IIA capping domain is predicted by PSI-PRED to consist of a mixed alpha-beta fold with the basic pattern: Helix-Helix-Helix-Sheet-Helix-Loop-Sheet-Helix-Sheet-Helix. Presently, this subfamily encompasses a single equivalog model (TIGR01452) for the eukaryotic phosphoglycolate phosphatase, as well as four hypothetical equivalogs covering closely related sequences (TIGR01456 and TIGR01458 in eukaryotes, TIGR01457 in gram positive bacteria and TIGR01459 in gram negative bacteria). The Escherishia coli NagD gene and the Bacillus subtilus AraL gene are members of this subfamily but are not members of the any of the presently defined equivalogs within it. NagD is part of the NAG operon responsible for N-acetylglucosamine metabolism. The function of this gene is unknown. Genes from several organisms have been annotated as NagD, or NagD-like. However, without data on the presence of other members of this pathway, (such as in the case of Yersinia pestis) these assignments should not be given great weight. The AraL gene is similar: it is part of the L-arabinose operon, but the function is unknown. A gene from Halobacterium has been annotated as AraL, but no other Ara operon genes have been annotated. Many of the genes in this subfamily have been annotated as "pNPPase" "4-nitrophenyl phosphatase" or "NPPase". These all refer to the same activity versus a common lab test compound used to determine phosphatase activity. There is no evidence that this activity is physiologically relevant. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273637 [Multi-domain]  Cd Length: 236  Bit Score: 66.58  E-value: 4.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235    10 VLVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEF-EISEDEIFTSLTAARNLIEQKQV 88
Cdd:TIGR01460   1 FLFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLSSLLGvDVSPDQIITSGSVTKDLLRQRFE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 85861235    89 R-PMLLV--------------DDRALPEFTGVQTQDPNAVVIGLAPEHFHYQLLNQAFRRKQRG 137
Cdd:TIGR01460  81 GeKVYVIgvgelresleglgfRNDFFDDIDHLAIEKIPAAVIVGEPSDFSYDELAKAAYLLAEG 144
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 10-124 3.91e-11

UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium falciparum PNPase; Plasmodium falciparum para nitrophenyl phosphate phosphatase (PNPase) catalyzes the dephosphorylation of thiamine monophosphate to thiamine, other substrates on which its active are nucleotides, phosphorylated sugars, pyridoxal-5-phosphate, and paranitrophenyl phosphate. This subfamily belongs to the UmpH/NagD phosphatase family, and 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: 319834 [Multi-domain]  Cd Length: 286  Bit Score: 58.86  E-value: 3.91e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235  10 VLVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIFTSLTAARNLIEQKQVR 89
Cdd:cd07532   9 VIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIADYLKEKGFK 88

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 85861235  90 PMLLV-------------------------DDRALPEFTGVQTQDPN--AVVIGLaPEHFHY 124
Cdd:cd07532  89 KKVYVigeegirkeleeagivscggdgedeKDDSMGDFAHNLELDPDvgAVVVGR-DEHFSY 149
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 10-86 3.36e-10

haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this UmpH/NagD family include Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase , Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase, human PGP phosphoglycolate phosphatase, Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase, Bacillus AraL a putative sugar phosphatase, and Plasmodium falciparum para nitrophenyl phosphate phosphatase PNPase. 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: 319811 [Multi-domain]  Cd Length: 270  Bit Score: 56.22  E-value: 3.36e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85861235  10 VLVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIFTS-LTAARNLIEQK 86
Cdd:cd07508   2 VISDCDGVLWHDERAIPGAAEFLEALKEAGKKIVFVSNNSSRSRQDYAEKFRKFGVDVPEDQIVTSaKATARFLRSRK 79
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 10-132 2.07e-09

UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase; This subfamily includes the phosphoglycolate phosphatases (human PGP and Arabidopsis thaliana PGLP2) and p-nitrophenylphosphatases (Schizosaccharomyces pombe PHO2 and Saccharomyces PHO13p). It belongs to the UmpH/NagD phosphatase family, and 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: 319813 [Multi-domain]  Cd Length: 282  Bit Score: 54.32  E-value: 2.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235  10 VLVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFE-ISEDEIFTSLTAARNLIEQK-- 86
Cdd:cd07510   4 FLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTgLKEEEIFSSAYCAARYLRQRlp 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 85861235  87 -QVRPMLLV------------------------DDRALPEFTGVQTQDPN--AVVIGLAPeHFHYQLLNQAFR 132
Cdd:cd07510  84 gPADGKVYVlggeglraeleaagvahlggpddgLRRAAPKDWLLAGLDPDvgAVLVGLDE-HVNYLKLAKATQ 155
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 8-134 3.04e-09

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


Pssm-ID: 319827 [Multi-domain]  Cd Length: 253  Bit Score: 53.48  E-value: 3.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235   8 KAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKeSKKDLLERLKKLEFE-ISEDEIFTSLTAARNLIEQK 86
Cdd:cd07525   1 DAFLLDLWGVLHDGNEPYPGAVEALAALRAAGKTVVLVTNAPR-PAESVVRQLAKLGVPpSTYDAIITSGEVTRELLARE 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 85861235  87 QVRP---MLLVDDRALPEFTGVQ---TQDPNA----VVIGLAPEHF----HYQ-LLNQAFRRK 134
Cdd:cd07525  80 AGLGrkvYHLGPERDANVLEGLDvvaTDDAEKaefiLCTGLYDDETetpeDYRkLLKAAAARG 142
PLN02645 PLN02645
phosphoglycolate phosphatase
 1-79 9.27e-09

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 52.41  E-value: 9.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235    1 MAARRALKAV---LVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIFTSLT 77
Cdd:PLN02645  19 ENADELIDSVetfIFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSF 98


                 ..
gi 85861235   78 AA 79
Cdd:PLN02645  99 AA 100
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 11-116 4.05e-08

uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid dehalogenase-like superfamily; This uncharacterized subfamily belongs to the UmpH/NagD phosphatase family and 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: 319858 [Multi-domain]  Cd Length: 247  Bit Score: 50.51  E-value: 4.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235  11 LVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIFTSLTAARNLIEQKQVRP 90
Cdd:cd16422   3 IFDMDGTIYLGDDLIPGTLEFLERLHEKKRRYIFLTNNSSKNLADYVEKLNRLGIDAGLDRVFTSGEATIDHLKKEFIKP 82

                        90       100       110
                ....*....|....*....|....*....|..
gi 85861235  91 --MLLVDDRALPEFTG----VQTQDPNAVVIG 116
Cdd:cd16422  83 kiFLLGTKSLREEFEKagftLDGDDIDVVVLG 114
PRK10444 PRK10444
HAD-IIA family hydrolase;
7-146 6.09e-06

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 44.01  E-value: 6.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235    7 LKAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIFTSLTAARNLIEQK 86
Cdd:PRK10444   1 IKNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQ 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85861235   87 QVRPMLLVDDRALPE------FTgVQTQDPNAVVIGlAPEHFHYQLLNQAFRRKQRGQE--EENSDSH 146
Cdd:PRK10444  81 EGKKAYVIGEGALIHelykagFT-ITDINPDFVIVG-ETRSYNWDMMHKAAYFVANGARfiATNPDTH 146
COG2503 COG2503
Predicted secreted acid phosphatase [General function prediction only];
23-112 6.51e-05

Predicted secreted acid phosphatase [General function prediction only];


Pssm-ID: 441997 [Multi-domain]  Cd Length: 269  Bit Score: 41.10  E-value: 6.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235  23 AAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEF-EISEDEIF-----TSLTAARNLIEQKQvRPMLLVDD 96
Cdd:COG2503 123 TAVPGAVEFLNYANSKGVTVFYISNRKAEEKAATLANLKALGFpVVDEDHLLlktdgSDKEARRQAVAKRY-RIVMLVGD 201

                        90
                ....*....|....*.
gi 85861235  97 RaLPEFTGVQTQDPNA 112
Cdd:COG2503 202 N-LGDFADAFDKKSNA 216
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 9-75 1.53e-04

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: 38.92  E-value: 1.53e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 85861235   9 AVLVDLNGTLHiedaavpgAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFeisEDEIFTS 75
Cdd:cd01427   1 AVLFDLDGTLL--------AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDL---FDGIIGS 56
HAD_CAP cd07534
molecular class C acid phosphatases, similar to Haemophilus influenzae e (P4) acid phosphatase; ...
 23-122 1.61e-04

molecular class C acid phosphatases, similar to Haemophilus influenzae e (P4) acid phosphatase; belongs to the haloacid dehalogenase-like hydrolase superfamily; Molecular class C acid phosphatases (CAPs) are nonspecific acid phosphatases with generally broad substrate specificity and optimum activity at neutral to acidic pH. Members include Haemophilus influenzae lipoprotein e (P4), Elizabethkingia meningosepticum OlpA, Helicobacter pylori HppA, Enterobacter sp. 4 acid phosphatase PhoI, and Streptococcus pyogenes M1 GAS LppC. Lipoprotein e (P4) exhibits phosphomonoesterase activity with aryl phosphate substrates including nicotinamide mononucleotide (NMN), tyrosine phosphate, phenyl phosphate, p-nitrophenyl phosphate, and 4-methylumbelliferyl phosphate. The role of P4 in NAD+ uptake appears to be the dephosphorylation of NMN to nicotinamide riboside, which is then taken up by the organism. Elizabethkingia meningosepticum OlpA is a broad-spectrum nucleotidase with preference for 5'-nucleotides, it efficiently hydrolyzes nucleotide monophosphates, with a strong preference for 5'-nucleotides and for 3'-AMP; OlpA can also hydrolyze sugar phosphates and beta-glycerol phosphate, although with a lower efficiency. Helicobacter pylori HppA is also a 5' nucleotidase. 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: 319836 [Multi-domain]  Cd Length: 196  Bit Score: 40.01  E-value: 1.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235  23 AAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERLKKLEFEISEDEIF-----TSLTAARNLIEQKQVRPMLLVDDR 97
Cdd:cd07534  74 KPIPGAVDFLNYANAKGVTIFYVSNRDQKLKAATLKNLKRLGFPQASDDHLllktdKSSKESRRQLVKEKYNIVLLFGDN 153

                        90       100
                ....*....|....*....|....*...
gi 85861235  98 aLPEFTGVQTQDPNA---VVIGLAPEHF 122
Cdd:cd07534 154 -LGDFGDFTYKKENEdrrALVEKNAEEF 180
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 9-90 6.99e-04

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to the uncharacterized human CECR5 (cat eye syndrome critical region protein 5); 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: 319814  Cd Length: 136  Bit Score: 37.37  E-value: 6.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861235   9 AVLVDLNGTLHIEDAAVPGAQEALKRLRATSVMVRFVTNTTKESKKDLLERL-KKLEFEISEDEI-----------FTSL 76
Cdd:cd07511   2 GFAFDIDGVLVRGKKPIPGAPKALKFLNDNKIPFIFLTNGGGFPESKRADFLsKLLGVEVSPDQViqshspgkpteLTYD 81

                        90
                ....*....|....
gi 85861235  77 TAARNLIEQKQVRP 90
Cdd:cd07511  82 FAEHVLQRQAKRLG 95
 
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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