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Conserved domains on  [gi|971059214|ref|NP_001305261|]
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phospholysine phosphohistidine inorganic pyrophosphate phosphatase isoform 4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD-SF-IIA-hyp3 super family cl31447
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 11-212 7.59e-118

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]


The actual alignment was detected with superfamily member TIGR01458:

Pssm-ID: 162372 [Multi-domain]  Cd Length: 257  Bit Score: 335.29  E-value: 7.59e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214   11 VRGVLLDISGVLYDSGAGGGTAIAGSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAACQI 90
Cdd:TIGR01458   1 VKGVLLDISGVLYISDAGGGTAVPGSQEAVKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214   91 LKEQGLRPYLLIHDGVRSEFDQIDTSNPNCVVIADAGESFSYQNMNNAFQVLMELEKPVLISLGKGRYYKETSGLMLDVG 170
Cdd:TIGR01458  81 LEEKQLRPMLLVDDRVLPDFDGIDTSDPNCVVMGLAPEHFSYQILNQAFRLLLDGAKPVLIAIGKGRYYKRKDGLALDVG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 971059214  171 PYMKALEYACGIKAEVVGKPSPEFFKSALQAIGVEAHQLLSV 212
Cdd:TIGR01458 161 PFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMI 202
 
Name Accession Description Interval E-value
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 11-212 7.59e-118

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: 335.29  E-value: 7.59e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214   11 VRGVLLDISGVLYDSGAGGGTAIAGSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAACQI 90
Cdd:TIGR01458   1 VKGVLLDISGVLYISDAGGGTAVPGSQEAVKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214   91 LKEQGLRPYLLIHDGVRSEFDQIDTSNPNCVVIADAGESFSYQNMNNAFQVLMELEKPVLISLGKGRYYKETSGLMLDVG 170
Cdd:TIGR01458  81 LEEKQLRPMLLVDDRVLPDFDGIDTSDPNCVVMGLAPEHFSYQILNQAFRLLLDGAKPVLIAIGKGRYYKRKDGLALDVG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 971059214  171 PYMKALEYACGIKAEVVGKPSPEFFKSALQAIGVEAHQLLSV 212
Cdd:TIGR01458 161 PFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMI 202
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 12-212 2.57e-105

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: 303.43  E-value: 2.57e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  12 RGVLLDISGVLYDSGAGGGTaiagSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAACQIL 91
Cdd:cd07509    1 KAVLLDLSGTLYISGAAIPG----AAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  92 KEQGLRPYLLIHDGVRSEFDQIDTSNPNCVVIADAGESFSYQNMNNAFQVLmeLEKPVLISLGKGRYYKETSGLMLDVGP 171
Cdd:cd07509   77 EEKGLRPHLLVDDDALEDFIGIDTSDPNAVVIGDAGEHFNYQTLNRAFRLL--LDGAPLIALHKGRYYKRKDGLALDPGA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 971059214 172 YMKALEYACGIKAEVVGKPSPEFFKSALQAIGVEAHQLLSV 212
Cdd:cd07509  155 FVTGLEYATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMI 195
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
8-210 2.69e-43

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 145.64  E-value: 2.69e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214   8 LAGVRGVLLDISGVLYDSGAGGGTaiagSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAA 87
Cdd:COG0647    5 ADRYDAFLLDLDGVLYRGDEPIPG----AVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  88 CQILKEQ--GLRPYLLIHDGVRSEFDQI-----DTSNPNCVVIADaGESFSYQNMNNAFQVLMEleKPVLISLGKGRYYK 160
Cdd:COG0647   81 AAYLAERhpGARVYVIGEEGLREELEEAgltlvDDEEPDAVVVGL-DRTFTYEKLAEALRAIRR--GAPFIATNPDRTVP 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 971059214 161 ETSGLMLDVGPYMKALEYACGIKAEVVGKPSPEFFKSALQAIGVEAHQLL 210
Cdd:COG0647  158 TEDGLIPGAGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVL 207
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 14-111 4.32e-15

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 67.88  E-value: 4.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214   14 VLLDISGVLYDSGAGGGTaiagSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAACQILKE 93
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPG----AAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKE 76

                          90       100
                  ....*....|....*....|
gi 971059214   94 Q--GLRPYLLIHDGVRSEFD 111
Cdd:pfam13344  77 RkfGKKVLVIGSEGLREELE 96
PLN02645 PLN02645
phosphoglycolate phosphatase
 38-212 1.34e-04

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 41.62  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  38 EAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAACQILKEQGLRP----YLLIHDGVRSEFDQI 113
Cdd:PLN02645  51 ETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSFAAAAYLKSINFPKdkkvYVIGEEGILEELELA 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214 114 DTsnpNCVviadAGESFSYQNMNNAFQVLMELEKPV-LISLGKGR---YYK---------ETSGLM-----LD-VGPYMK 174
Cdd:PLN02645 131 GF---QYL----GGPEDGDKKIELKPGFLMEHDKDVgAVVVGFDRyinYYKiqyatlcirENPGCLfiatnRDaVTHLTD 203

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 971059214 175 ALEYA----------CGIKAE--VVGKPSPEFFKSALQAIGVEAHQLLSV 212
Cdd:PLN02645 204 AQEWAgagsmvgaikGSTEREplVVGKPSTFMMDYLANKFGIEKSQICMV 253
 
Name Accession Description Interval E-value
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 11-212 7.59e-118

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: 335.29  E-value: 7.59e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214   11 VRGVLLDISGVLYDSGAGGGTAIAGSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAACQI 90
Cdd:TIGR01458   1 VKGVLLDISGVLYISDAGGGTAVPGSQEAVKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214   91 LKEQGLRPYLLIHDGVRSEFDQIDTSNPNCVVIADAGESFSYQNMNNAFQVLMELEKPVLISLGKGRYYKETSGLMLDVG 170
Cdd:TIGR01458  81 LEEKQLRPMLLVDDRVLPDFDGIDTSDPNCVVMGLAPEHFSYQILNQAFRLLLDGAKPVLIAIGKGRYYKRKDGLALDVG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 971059214  171 PYMKALEYACGIKAEVVGKPSPEFFKSALQAIGVEAHQLLSV 212
Cdd:TIGR01458 161 PFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMI 202
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 12-212 2.57e-105

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: 303.43  E-value: 2.57e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  12 RGVLLDISGVLYDSGAGGGTaiagSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAACQIL 91
Cdd:cd07509    1 KAVLLDLSGTLYISGAAIPG----AAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  92 KEQGLRPYLLIHDGVRSEFDQIDTSNPNCVVIADAGESFSYQNMNNAFQVLmeLEKPVLISLGKGRYYKETSGLMLDVGP 171
Cdd:cd07509   77 EEKGLRPHLLVDDDALEDFIGIDTSDPNAVVIGDAGEHFNYQTLNRAFRLL--LDGAPLIALHKGRYYKRKDGLALDPGA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 971059214 172 YMKALEYACGIKAEVVGKPSPEFFKSALQAIGVEAHQLLSV 212
Cdd:cd07509  155 FVTGLEYATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMI 195
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
8-210 2.69e-43

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 145.64  E-value: 2.69e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214   8 LAGVRGVLLDISGVLYDSGAGGGTaiagSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAA 87
Cdd:COG0647    5 ADRYDAFLLDLDGVLYRGDEPIPG----AVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  88 CQILKEQ--GLRPYLLIHDGVRSEFDQI-----DTSNPNCVVIADaGESFSYQNMNNAFQVLMEleKPVLISLGKGRYYK 160
Cdd:COG0647   81 AAYLAERhpGARVYVIGEEGLREELEEAgltlvDDEEPDAVVVGL-DRTFTYEKLAEALRAIRR--GAPFIATNPDRTVP 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 971059214 161 ETSGLMLDVGPYMKALEYACGIKAEVVGKPSPEFFKSALQAIGVEAHQLL 210
Cdd:COG0647  158 TEDGLIPGAGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVL 207
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 14-203 8.16e-20

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: 83.92  E-value: 8.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214   14 VLLDISGVLYDSGAGGGTaiagSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRL-GFDISEQEVTAPAPAACQILK 92
Cdd:TIGR01460   1 FLFDIDGVLWLGHKPIPG----AAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLSSLlGVDVSPDQIITSGSVTKDLLR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214   93 E--QGLRPYLLIHDGVRSE----------FDQIDTSNPN---CVVIADAGESFSYQNMNNAFQVLMELEKPVLIS----- 152
Cdd:TIGR01460  77 QrfEGEKVYVIGVGELRESleglgfrndfFDDIDHLAIEkipAAVIVGEPSDFSYDELAKAAYLLAEGDVPFIAAnrddl 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 971059214  153 --LGKGRYYketsglmLDVGPYMKALEYACGIKAEVVGKPSPEFFKSALQAIG 203
Cdd:TIGR01460 157 vrLGDGRFR-------PGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNLLQ 202
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 12-212 1.90e-18

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: 80.33  E-value: 1.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  12 RGVLLDISGVLYdsgaGGGTAIAGSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAACQIL 91
Cdd:cd07530    1 KGYLIDLDGTVY----RGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSALATAQYL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  92 KEQ--GLRPYLLIHDGVRSEFDQ----IDTSNPNCVVIAdAGESFSYQNMNNAfqVLMELEKPVLISLGKGRYYKETSGL 165
Cdd:cd07530   77 AEQlpGAKVYVIGEEGLRTALHEagltLTDENPDYVVVG-LDRDLTYEKLAEA--TLAIRNGAKFIATNPDLTLPTERGL 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 971059214 166 MLDVGPYMKALEYACGIKAEVVGKPSPEFFKSALQAIGVEAHQLLSV 212
Cdd:cd07530  154 LPGNGSVVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMV 200
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
 13-212 6.03e-17

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: 76.45  E-value: 6.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  13 GVLLDISGVLYDSGAGGGTaiagSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAACQILK 92
Cdd:cd07531    2 GYIIDLDGTIGKGVTLIPG----AVEGVKTLRRLGKKIIFLSNNSTRSRRILLERLRSFGIEVGEDEILVSSYVTARFLA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  93 EQ--GLRPYLLIHDGVRSE-----FDQIDTSNPNCVVIADAGESFSYQNMNNAFQVLMELEKpvLISLGKGRYYKETSGL 165
Cdd:cd07531   78 REkpNAKVFVTGEEGLIEElrlagLEIVDKYDEAEYVVVGSNRKITYELLTKAFRACLRGAR--YIATNPDRIFPAEDGP 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 971059214 166 MLDVGPYMKALEYACGIKAE-VVGKPSPEFFKSALQAIGVEAHQLLSV 212
Cdd:cd07531  156 IPDTAAIIGAIEWCTGREPEvVVGKPSEVMAREALDILGLDAKDCAIV 203
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 14-111 4.32e-15

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 67.88  E-value: 4.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214   14 VLLDISGVLYDSGAGGGTaiagSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAACQILKE 93
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPG----AAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKE 76

                          90       100
                  ....*....|....*....|
gi 971059214   94 Q--GLRPYLLIHDGVRSEFD 111
Cdd:pfam13344  77 RkfGKKVLVIGSEGLREELE 96
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 13-212 4.62e-14

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: 68.93  E-value: 4.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  13 GVLLDISGVLYDSGAGGGTaiagSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAACQILK 92
Cdd:cd07508    1 LVISDCDGVLWHDERAIPG----AAEFLEALKEAGKKIVFVSNNSSRSRQDYAEKFRKFGVDVPEDQIVTSAKATARFLR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  93 EQ--GLRPYLLIHDGVRSEF----------------------DQIDTSNPNCVVIADAGESFSYQNMNNAFQVLMELEKp 148
Cdd:cd07508   77 SRkfGKKVYVLGEEGLKEELraagfriaggpskgietyaelvEHLEDDENVDAVIVGSDFKLNFAKLRKACRYLRNPGC- 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 971059214 149 VLISLGKGRYYK-ETSGLMLDVGPYMKALEYACGIKAEVVGKPSPEFFKSALQAIGVEAHQLLSV 212
Cdd:cd07508  156 LFIATAPDRIHPlKDGGPIPGTGAFAAAVEAATGRQPLVLGKPSPWLGELALEKFGIDPERVLFV 220
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 8-198 9.12e-13

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: 65.40  E-value: 9.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214   8 LAGVRGVLLDISGVLYdsgaGGGTAIAGSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAA 87
Cdd:cd07532    3 LANIDTVIFDADGVLW----TGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  88 CQILKEQGLRPYLLI--HDGVRSEFDQ-------------IDTS------------NPNCVVIA-DagESFSYQNMNNAF 139
Cdd:cd07532   79 ADYLKEKGFKKKVYVigEEGIRKELEEagivscggdgedeKDDSmgdfahnleldpDVGAVVVGrD--EHFSYPKLMKAC 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 971059214 140 QVLMElekPVLISLGKGR--YYKETSGLML-DVGPYMKALEYACGIKAEVVGKPSP---EFFKSA 198
Cdd:cd07532  157 NYLRN---PDVLFLATNMdaTFPGPVGRVIpGAGAMVAAIEAVSGRKPLVLGKPNPqilNFLMKS 218
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 11-212 1.16e-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: 56.63  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  11 VRGVLLDISGVLYDSGAGGGTaiagSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQE-------VTA- 82
Cdd:cd07510    1 VDTFLFDCDGVLWNGEKAIPG----APETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTGLKEEeifssayCAAr 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  83 --------PAPAACQILKEQGLRPYL----LIHDGVRSEFDQIDTSNPNCV---------VIADAGESFSYQNMNNAFQV 141
Cdd:cd07510   77 ylrqrlpgPADGKVYVLGGEGLRAELeaagVAHLGGPDDGLRRAAPKDWLLagldpdvgaVLVGLDEHVNYLKLAKATQY 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971059214 142 LmelEKPVLISLGKGR--YYKETSGLML-DVGPYMKALEYACGIKAEVVGKPSPEFFKSALQAIGVEAHQLLSV 212
Cdd:cd07510  157 L---RDPGCLFVATNRdpWHPLSDGSFIpGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMV 227
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 36-212 2.30e-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: 52.44  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  36 SVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAACQILKEQGLRP--YLLIHDGVRSEFDQ- 112
Cdd:cd16422   20 TLEFLERLHEKKRRYIFLTNNSSKNLADYVEKLNRLGIDAGLDRVFTSGEATIDHLKKEFIKPkiFLLGTKSLREEFEKa 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214 113 ---IDTSNPNCVVIA-DAgeSFSYQNMNNAfqvlmelekpvLISLGKGRYYKETS---------GLMLDVGPYMKALEYA 179
Cdd:cd16422  100 gftLDGDDIDVVVLGfDT--ELTYEKLRTA-----------CLLLRRGIPYIATHpdincpseeGPIPDAGSIIALIETS 166

                        170       180       190
                 ....*....|....*....|....*....|....
gi 971059214 180 CGIKAEVV-GKPSPEFFKSALQAIGVEAHQLLSV 212
Cdd:cd16422  167 TGRRPDLViGKPNPIILDPVLEKFDYSKEETVMV 200
PLN02645 PLN02645
phosphoglycolate phosphatase
 38-212 1.34e-04

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 41.62  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214  38 EAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAACQILKEQGLRP----YLLIHDGVRSEFDQI 113
Cdd:PLN02645  51 ETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSFAAAAYLKSINFPKdkkvYVIGEEGILEELELA 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971059214 114 DTsnpNCVviadAGESFSYQNMNNAFQVLMELEKPV-LISLGKGR---YYK---------ETSGLM-----LD-VGPYMK 174
Cdd:PLN02645 131 GF---QYL----GGPEDGDKKIELKPGFLMEHDKDVgAVVVGFDRyinYYKiqyatlcirENPGCLfiatnRDaVTHLTD 203

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 971059214 175 ALEYA----------CGIKAE--VVGKPSPEFFKSALQAIGVEAHQLLSV 212
Cdd:PLN02645 204 AQEWAgagsmvgaikGSTEREplVVGKPSTFMMDYLANKFGIEKSQICMV 253
 
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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