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Conserved domains on  [gi|219858312|gb|ACL38654|]
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HAD-superfamily hydrolase, subfamily IIA [Pseudarthrobacter chlorophenolicus A6]

Protein Classification

HAD-IIA family hydrolase( domain architecture ID 11576402)

haloacid dehalogenase (HAD)-IIA family hydrolase uses a nucleophilic aspartate in the phosphoryl transfer reaction; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 21-271 4.53e-123

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: 350.74  E-value: 4.53e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  21 ECWLTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLKDQV 100
Cdd:cd07530    1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSALATAQYLAEQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 101 RGSgsgnRAYTIGEAGLTTALHEAGFILTDQDPDFVVLGETRTYSFEAITTAIRLILAGARFIATNPDATGPSKDGPMPA 180
Cdd:cd07530   81 PGA----KVYVIGEEGLRTALHEAGLTLTDENPDYVVVGLDRDLTYEKLAEATLAIRNGAKFIATNPDLTLPTERGLLPG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 181 TGAIAALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLVLTGITQRDEIASYPF 260
Cdd:cd07530  157 NGSVVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVLTGVTTREDLAKPPY 236

                        250
                 ....*....|.
gi 219858312 261 RPNQVLNSVAD 271
Cdd:cd07530  237 RPTYIVPSLRE 247
 
Name Accession Description Interval E-value
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 21-271 4.53e-123

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: 350.74  E-value: 4.53e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  21 ECWLTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLKDQV 100
Cdd:cd07530    1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSALATAQYLAEQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 101 RGSgsgnRAYTIGEAGLTTALHEAGFILTDQDPDFVVLGETRTYSFEAITTAIRLILAGARFIATNPDATGPSKDGPMPA 180
Cdd:cd07530   81 PGA----KVYVIGEEGLRTALHEAGLTLTDENPDYVVVGLDRDLTYEKLAEATLAIRNGAKFIATNPDLTLPTERGLLPG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 181 TGAIAALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLVLTGITQRDEIASYPF 260
Cdd:cd07530  157 NGSVVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVLTGVTTREDLAKPPY 236

                        250
                 ....*....|.
gi 219858312 261 RPNQVLNSVAD 271
Cdd:cd07530  237 RPTYIVPSLRE 247
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
19-272 2.16e-120

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 344.40  E-value: 2.16e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  19 DIECWLTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLKD 98
Cdd:COG0647    7 RYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLAE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  99 QVRGSgsgnRAYTIGEAGLTTALHEAGFILT-DQDPDFVVLGETRTYSFEAITTAIRLILAGARFIATNPDATGPSKDGP 177
Cdd:COG0647   87 RHPGA----RVYVIGEEGLREELEEAGLTLVdDEEPDAVVVGLDRTFTYEKLAEALRAIRRGAPFIATNPDRTVPTEDGL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 178 MPATGAIAALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLVLTGITQRDEIAS 257
Cdd:COG0647  163 IPGAGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLTGVTTAEDLEA 242

                        250
                 ....*....|....*
gi 219858312 258 YPFRPNQVLNSVADL 272
Cdd:COG0647  243 APIRPDYVLDSLAEL 257
PRK10444 PRK10444
HAD-IIA family hydrolase;
26-272 5.96e-95

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 279.76  E-value: 5.96e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  26 DMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLKDQvrgsgS 105
Cdd:PRK10444   7 DIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQ-----E 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 106 GNRAYTIGEAGLTTALHEAGFILTDQDPDFVVLGETRTYSFEAITTAIRLILAGARFIATNPDATGPskdGPMPATGAIA 185
Cdd:PRK10444  82 GKKAYVIGEGALIHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDTHGR---GFYPACGALC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 186 ALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLVLTGITQRDEIASYPFRPNQV 265
Cdd:PRK10444 159 AGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSTLDDIDSMPFRPSWI 238


                 ....*..
gi 219858312 266 LNSVADL 272
Cdd:PRK10444 239 YPSVADI 245
HAD-SF-IIA-hyp2 TIGR01457
HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of ...
 23-271 2.63e-59

HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all gram positive (low-GC) bacteria. Sequences found in this model are annotated variously as related to NagD or 4-nitrophenyl phosphatase, and this hypothetical equivalog, of all of those within the Class IIA subfamily, is most closely related to the E. coli NagD enzyme and the PGP_euk equivalog (TIGR01452). However, there is presently no evidence that this hypothetical equivalog has the same function of either those. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 130524  Cd Length: 249  Bit Score: 188.91  E-value: 2.63e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312   23 WLTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLKDQvrg 102
Cdd:TIGR01457   4 YLIDLDGTMYNGTEKIEEACEFVRTLKKRGVPYLFVTNNSTRTPEQVADKLVSFDIPATEEQVFTTSMATAQYIAQQ--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  103 sGSGNRAYTIGEAGLTTALHEAGFILTDQDPDFVVLGETRTYSFEAITTAIRLILAGARFIATNPDATGPSKDGPMPATG 182
Cdd:TIGR01457  81 -KKDASVYVIGEEGLREAIKENGLTFGGENPDYVVVGLDRSITYEKFAVACLAIRNGARFISTNGDIAIPTERGLLPGNG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  183 AIAALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLVLTGITQRDEIASYPFRP 262
Cdd:TIGR01457 160 SLTSVLTVSTGVKPVFIGKPESIIMEQAMRVLGTDVEETLMVGDNYATDIMAGINAGIDTLLVHTGVTKREHMTDDMEKP 239


                  ....*....
gi 219858312  263 NQVLNSVAD 271
Cdd:TIGR01457 240 THAIDSLAE 248
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 23-126 1.40e-31

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 112.56  E-value: 1.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312   23 WLTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLKDQVRG 102
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKERKFG 80

                          90       100
                  ....*....|....*....|....
gi 219858312  103 SgsgnRAYTIGEAGLTTALHEAGF 126
Cdd:pfam13344  81 K----KVLVIGSEGLREELEEAGF 100
 
Name Accession Description Interval E-value
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 21-271 4.53e-123

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: 350.74  E-value: 4.53e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  21 ECWLTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLKDQV 100
Cdd:cd07530    1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSALATAQYLAEQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 101 RGSgsgnRAYTIGEAGLTTALHEAGFILTDQDPDFVVLGETRTYSFEAITTAIRLILAGARFIATNPDATGPSKDGPMPA 180
Cdd:cd07530   81 PGA----KVYVIGEEGLRTALHEAGLTLTDENPDYVVVGLDRDLTYEKLAEATLAIRNGAKFIATNPDLTLPTERGLLPG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 181 TGAIAALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLVLTGITQRDEIASYPF 260
Cdd:cd07530  157 NGSVVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVLTGVTTREDLAKPPY 236

                        250
                 ....*....|.
gi 219858312 261 RPNQVLNSVAD 271
Cdd:cd07530  237 RPTYIVPSLRE 247
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
19-272 2.16e-120

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 344.40  E-value: 2.16e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  19 DIECWLTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLKD 98
Cdd:COG0647    7 RYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLAE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  99 QVRGSgsgnRAYTIGEAGLTTALHEAGFILT-DQDPDFVVLGETRTYSFEAITTAIRLILAGARFIATNPDATGPSKDGP 177
Cdd:COG0647   87 RHPGA----RVYVIGEEGLREELEEAGLTLVdDEEPDAVVVGLDRTFTYEKLAEALRAIRRGAPFIATNPDRTVPTEDGL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 178 MPATGAIAALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLVLTGITQRDEIAS 257
Cdd:COG0647  163 IPGAGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLTGVTTAEDLEA 242

                        250
                 ....*....|....*
gi 219858312 258 YPFRPNQVLNSVADL 272
Cdd:COG0647  243 APIRPDYVLDSLAEL 257
PRK10444 PRK10444
HAD-IIA family hydrolase;
26-272 5.96e-95

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 279.76  E-value: 5.96e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  26 DMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLKDQvrgsgS 105
Cdd:PRK10444   7 DIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQ-----E 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 106 GNRAYTIGEAGLTTALHEAGFILTDQDPDFVVLGETRTYSFEAITTAIRLILAGARFIATNPDATGPskdGPMPATGAIA 185
Cdd:PRK10444  82 GKKAYVIGEGALIHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDTHGR---GFYPACGALC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 186 ALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLVLTGITQRDEIASYPFRPNQV 265
Cdd:PRK10444 159 AGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSTLDDIDSMPFRPSWI 238


                 ....*..
gi 219858312 266 LNSVADL 272
Cdd:PRK10444 239 YPSVADI 245
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 24-271 5.63e-76

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: 232.26  E-value: 5.63e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  24 LTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLKDQVrgs 103
Cdd:cd07508    3 ISDCDGVLWHDERAIPGAAEFLEALKEAGKKIVFVSNNSSRSRQDYAEKFRKFGVDVPEDQIVTSAKATARFLRSRK--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 104 gSGNRAYTIGEAGLTTALHEAGF-------------------ILTDQDPDFVVLGETRTYSFEAITTAIRLILA-GARFI 163
Cdd:cd07508   80 -FGKKVYVLGEEGLKEELRAAGFriaggpskgietyaelvehLEDDENVDAVIVGSDFKLNFAKLRKACRYLRNpGCLFI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 164 ATNPDATGPSKD-GPMPATGAIAALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHT 242
Cdd:cd07508  159 ATAPDRIHPLKDgGPIPGTGAFAAAVEAATGRQPLVLGKPSPWLGELALEKFGIDPERVLFVGDRLATDVLFGKACGFQT 238

                        250       260       270
                 ....*....|....*....|....*....|..
gi 219858312 243 VLVLTGITQRDEIASYP---FRPNQVLNSVAD 271
Cdd:cd07508  239 LLVLTGVTTLEDLQAYIdheLVPDYYADSLAD 270
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 22-269 1.36e-65

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: 204.98  E-value: 1.36e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  22 CWLTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLKDQvr 101
Cdd:cd16422    1 LFIFDMDGTIYLGDDLIPGTLEFLERLHEKKRRYIFLTNNSSKNLADYVEKLNRLGIDAGLDRVFTSGEATIDHLKKE-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 102 gsGSGNRAYTIGEAGLTTALHEAGFILTDQDPDFVVLGETRTYSFEAITTAIRLILAGARFIATNPDATGPSKDGPMPAT 181
Cdd:cd16422   79 --FIKPKIFLLGTKSLREEFEKAGFTLDGDDIDVVVLGFDTELTYEKLRTACLLLRRGIPYIATHPDINCPSEEGPIPDA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 182 GAIAALITKATGR-EPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLVLTGITQRDEIASYPF 260
Cdd:cd16422  157 GSIIALIETSTGRrPDLVIGKPNPIILDPVLEKFDYSKEETVMVGDRLYTDIVLGINAGVDSILVLSGETTREDLEDLER 236


                 ....*....
gi 219858312 261 RPNQVLNSV 269
Cdd:cd16422  237 KPTYVFDNV 245
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
 23-272 5.40e-61

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: 193.55  E-value: 5.40e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  23 WLTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLKDQVRG 102
Cdd:cd07531    3 YIIDLDGTIGKGVTLIPGAVEGVKTLRRLGKKIIFLSNNSTRSRRILLERLRSFGIEVGEDEILVSSYVTARFLAREKPN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 103 SgsgnRAYTIGEAGLTTALHEAGFILTDQ--DPDFVVLGETRTYSFEAITTAIRLILAGARFIATNPDATGPSKDGPMPA 180
Cdd:cd07531   83 A----KVFVTGEEGLIEELRLAGLEIVDKydEAEYVVVGSNRKITYELLTKAFRACLRGARYIATNPDRIFPAEDGPIPD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 181 TGAIAALITKATGREP-YIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLVLTGITQRDEIASYP 259
Cdd:cd07531  159 TAAIIGAIEWCTGREPeVVVGKPSEVMAREALDILGLDAKDCAIVGDQIDVDIAMGKAIGMETALVLTGVTTRENLDRHG 238

                        250
                 ....*....|...
gi 219858312 260 FRPNQVLNSVADL 272
Cdd:cd07531  239 YKPDYVLNSIKDL 251
HAD-SF-IIA-hyp2 TIGR01457
HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of ...
 23-271 2.63e-59

HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all gram positive (low-GC) bacteria. Sequences found in this model are annotated variously as related to NagD or 4-nitrophenyl phosphatase, and this hypothetical equivalog, of all of those within the Class IIA subfamily, is most closely related to the E. coli NagD enzyme and the PGP_euk equivalog (TIGR01452). However, there is presently no evidence that this hypothetical equivalog has the same function of either those. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 130524  Cd Length: 249  Bit Score: 188.91  E-value: 2.63e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312   23 WLTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLKDQvrg 102
Cdd:TIGR01457   4 YLIDLDGTMYNGTEKIEEACEFVRTLKKRGVPYLFVTNNSTRTPEQVADKLVSFDIPATEEQVFTTSMATAQYIAQQ--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  103 sGSGNRAYTIGEAGLTTALHEAGFILTDQDPDFVVLGETRTYSFEAITTAIRLILAGARFIATNPDATGPSKDGPMPATG 182
Cdd:TIGR01457  81 -KKDASVYVIGEEGLREAIKENGLTFGGENPDYVVVGLDRSITYEKFAVACLAIRNGARFISTNGDIAIPTERGLLPGNG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  183 AIAALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLVLTGITQRDEIASYPFRP 262
Cdd:TIGR01457 160 SLTSVLTVSTGVKPVFIGKPESIIMEQAMRVLGTDVEETLMVGDNYATDIMAGINAGIDTLLVHTGVTKREHMTDDMEKP 239


                  ....*....
gi 219858312  263 NQVLNSVAD 271
Cdd:TIGR01457 240 THAIDSLAE 248
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 20-272 3.82e-52

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: 171.80  E-value: 3.82e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  20 IECWLTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIP-EENIWTSALATAQFLKD 98
Cdd:cd07510    1 VDTFLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTGLkEEEIFSSAYCAARYLRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  99 QVRGSGSGnRAYTIGEAGLTTALHEAGF------------------ILTDQDPDF--VVLGETRTYSFEAITTAIRLIL- 157
Cdd:cd07510   81 RLPGPADG-KVYVLGGEGLRAELEAAGVahlggpddglrraapkdwLLAGLDPDVgaVLVGLDEHVNYLKLAKATQYLRd 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 158 AGARFIATNPDATGPSKDGP-MPATGAIAALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGM 236
Cdd:cd07510  160 PGCLFVATNRDPWHPLSDGSfIPGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDTDILFGQ 239

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 219858312 237 EAGLHTVLVLTGITQRDEIASY---PFRPNQVLNSVADL 272
Cdd:cd07510  240 NCGLKTLLVLTGVSTLEEALAKlsnDLVPDYYVESLADL 278
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 24-248 2.97e-51

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: 167.89  E-value: 2.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312   24 LTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRAS-GLEIPEENIWTSALATAQFLKDQVRg 102
Cdd:TIGR01460   2 LFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLSSLlGVDVSPDQIITSGSVTKDLLRQRFE- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  103 sgsGNRAYTIGEAGLTTALHEAGF----------ILTDQDPDFVVLGETRTYSFEAITTAIRLILAG-ARFIATNPDATG 171
Cdd:TIGR01460  81 ---GEKVYVIGVGELRESLEGLGFrndffddidhLAIEKIPAAVIVGEPSDFSYDELAKAAYLLAEGdVPFIAANRDDLV 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 219858312  172 PSKDG-PMPATGAIAALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTA-MIGDRMDTDIIAGMEAGLHTVLVLTG 248
Cdd:TIGR01460 158 RLGDGrFRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNLLQARPERRDvMVGDNLRTDILGAKNAGFDTLLVLTG 236
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
 20-272 6.01e-51

phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In mammals, PGP is found in many tissues, notably in red blood cells where P-glycolate is and important activator of the hydrolysis of 2,3-bisphosphoglycerate, a major modifier of the oxygen affinity of hemoglobin. Pyridoxal phosphate (PLP, Vitamin B6) phosphatase is involved in the degradation of PLP in mammals and is widely distributed in human tissues including erythrocyes. The enzymes described here are members of the Haloacid dehalogenase superfamily of hydrolase enzymes (pfam00702). Unlike the bacterial PGP equivalog (TIGR01449), which is a member of class (subfamily) I, these enzymes are members of class (subfamily) II. These two families have almost certainly arisen from convergent evolution (although these two ancestors may themselves have diverged from a more distant HAD superfamily progenitor). The primary seed sequence for this model comes from Chlamydomonas reinhardtii, a photosynthetic alga. The enzyme has been purified and characterized and these data are fully consistent with the assignment of function as a PGPase involved in photorespiration. The second seed, from Homo sapiens chromosome 22 has been characterized as a pyridoxal phosphatase. Biochemical characterization of partially purified PGP's from various tissues including red blood cells have been performed while one gene for PGP has been localized to chromosome 16p13.3. The sequence used here maps to chromosome 22. There is indeed a related gene on chromosome 16 (and it is expressed, since EST's are found) which shows 46% identity. The chromosome 16 gene is not in evidence in nraa but translated from the genomic sequence. The third seed, from C. elegans, is only supported by sequence similarity. This model is limited to eukaryotic species including S. pombe and S. cerevisiae, although several archaea score between the trusted and noise cutoffs. This model is closely related to a family of bacterial sequences including the E. coli NagD and B. subtilus AraL genes which are characterized by the ability to hydrolyze para-nitrophenylphosphate (pNPPases or NPPases). The chlamydomonas PGPase d


Pssm-ID: 273635 [Multi-domain]  Cd Length: 279  Bit Score: 168.50  E-value: 6.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312   20 IECWLTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLKdq 99
Cdd:TIGR01452   2 AQGFIFDCDGVLWLGERVVPGAPELLDRLARAGKQILFVTNNSTKSRAEYALKFARLGFNGLAEQLFSSALCAARLLR-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  100 vRGSGSGNRAYTIGEAGLTTALHEAG--------------------FILTDQDPDFVVLGETRTYSFEAITTAIRLIL-A 158
Cdd:TIGR01452  80 -QPPDAGKAVYVIGEEGLRAELDAAGirlagdpgekkqdeadgfmyDIKLDERVGAVVVGYDEHFSYVKLMEACAHLReP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  159 GARFIATNPDATGPSKDGP-MPATGAIAALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGME 237
Cdd:TIGR01452 159 GCLFVATNRDPWHPLSDGSrTPGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRLETDILFGHR 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 219858312  238 AGLHTVLVLTGITQRDEIASY------PFRPNQVLNSVADL 272
Cdd:TIGR01452 239 CGMTTVLVLSGVSQLEEAQEYlmagqdDLVPDYVVESLADL 279
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 18-255 8.31e-51

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: 168.25  E-value: 8.31e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  18 QDIECWLTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLK 97
Cdd:cd07532    4 ANIDTVIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIADYLK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  98 DqvrgSGSGNRAYTIGEAGLTTALHEAGF---------------------ILTDQDPDFVVLGETRTYSFEAITTAIRLI 156
Cdd:cd07532   84 E----KGFKKKVYVIGEEGIRKELEEAGIvscggdgedekddsmgdfahnLELDPDVGAVVVGRDEHFSYPKLMKACNYL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 157 L-AGARFIATNPDATGPSKDGP-MPATGAIAALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIA 234
Cdd:cd07532  160 RnPDVLFLATNMDATFPGPVGRvIPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILF 239

                        250       260
                 ....*....|....*....|.
gi 219858312 235 GMEAGLHTVLVLTGITQRDEI 255
Cdd:cd07532  240 ANNCGFQSLLVGTGVNSLEDA 260
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 24-271 1.00e-41

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: 143.57  E-value: 1.00e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  24 LTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLKdqvrgs 103
Cdd:cd07509    4 LLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLE------ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 104 GSGNRAYTIGEAGLTTALHEagfiLTDQDPDFVVLGET-RTYSFEAITTAIRLILAGARFIATNPDATGPSKDGPMPATG 182
Cdd:cd07509   78 EKGLRPHLLVDDDALEDFIG----IDTSDPNAVVIGDAgEHFNYQTLNRAFRLLLDGAPLIALHKGRYYKRKDGLALDPG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 183 AIAALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLVLTG-ITQRDEIASYPfR 261
Cdd:cd07509  154 AFVTGLEYATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVRTGkYRPSDEKKPNV-P 232

                        250
                 ....*....|
gi 219858312 262 PNQVLNSVAD 271
Cdd:cd07509  233 PDLTADSFAD 242
PLN02645 PLN02645
phosphoglycolate phosphatase
 18-272 1.11e-40

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 142.93  E-value: 1.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  18 QDIECWLTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLK 97
Cdd:PLN02645  26 DSVETFIFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSFAAAAYLK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  98 dqVRGSGSGNRAYTIGEAGLTTALHEAGF------------------ILTDQDPDF--VVLGETRTYSFEAI---TTAIR 154
Cdd:PLN02645 106 --SINFPKDKKVYVIGEEGILEELELAGFqylggpedgdkkielkpgFLMEHDKDVgaVVVGFDRYINYYKIqyaTLCIR 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 155 LIlAGARFIATNPDATGPSKDG-PMPATGAIAALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDII 233
Cdd:PLN02645 184 EN-PGCLFIATNRDAVTHLTDAqEWAGAGSMVGAIKGSTEREPLVVGKPSTFMMDYLANKFGIEKSQICMVGDRLDTDIL 262

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 219858312 234 AGMEAGLHTVLVLTGITQRDEI--ASYPFRPNQVLNSVADL 272
Cdd:PLN02645 263 FGQNGGCKTLLVLSGVTSESMLlsPENKIQPDFYTSKISDF 303
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 23-126 1.40e-31

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 112.56  E-value: 1.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312   23 WLTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLKDQVRG 102
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKERKFG 80

                          90       100
                  ....*....|....*....|....
gi 219858312  103 SgsgnRAYTIGEAGLTTALHEAGF 126
Cdd:pfam13344  81 K----KVLVIGSEGLREELEEAGF 100
Hydrolase_like pfam13242
HAD-hyrolase-like;
198-272 4.51e-30

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 108.09  E-value: 4.51e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219858312  198 IVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLVLTGITQRDEIASYPFRPNQVLNSVADL 272
Cdd:pfam13242   1 VCGKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTRPADLEKAPIRPDYVVDDLAEA 75
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 24-248 1.59e-25

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: 101.48  E-value: 1.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312   24 LTDMDGVLVHE----NQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLKDQ 99
Cdd:TIGR01458   5 LLDISGVLYISdaggGTAVPGSQEAVKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQLLEEK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  100 vrgsgsGNRAYTIGEAGlttALHEAGFILTdQDPDFVVLGET-RTYSFEAITTAIRLILAGAR--FIATNPDATGPSKDG 176
Cdd:TIGR01458  85 ------QLRPMLLVDDR---VLPDFDGIDT-SDPNCVVMGLApEHFSYQILNQAFRLLLDGAKpvLIAIGKGRYYKRKDG 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219858312  177 PMPATGAIAALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLVLTG 248
Cdd:TIGR01458 155 LALDVGPFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMIGDDCRDDVGGAQDCGMRGIQVRTG 226
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 22-254 1.32e-19

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: 85.46  E-value: 1.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  22 CWLTDMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPrDLAARLRASGLE-IPEENIWTSALATAQFLKdqv 100
Cdd:cd07525    2 AFLLDLWGVLHDGNEPYPGAVEALAALRAAGKTVVLVTNAPRPAE-SVVRQLAKLGVPpSTYDAIITSGEVTRELLA--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 101 RGSGSGNRAYTIGEAGLTTALHEAGFILTDQDP--DFVV---LGETRTYSFEAITTAIRLILA-GARFIATNPDATGPSK 174
Cdd:cd07525   78 REAGLGRKVYHLGPERDANVLEGLDVVATDDAEkaEFILctgLYDDETETPEDYRKLLKAAAArGLPLICANPDLVVPRG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 175 DGPMPATGAIAALITKATGREPYIvGKPNPMMFRSAMNQID--AHSETtAMIGDRMDTDIIAGMEAGLHTVLVLTGITQR 252
Cdd:cd07525  158 GKLIYCAGALAELYEELGGEVIYF-GKPHPPIYDLALARLGrpAKARI-LAVGDGLHTDILGANAAGLDSLFVTGGIHRR 235


                 ..
gi 219858312 253 DE 254
Cdd:cd07525  236 LA 237
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 196-245 2.12e-12

Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the uncharacterized protein Bacillus subtilis YqeG; 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: 319853 [Multi-domain]  Cd Length: 108  Bit Score: 62.29  E-value: 2.12e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 219858312 196 PYIV--GKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLV 245
Cdd:cd16416   57 PFVAraGKPRPRAFRRALKEMDLPPEQVAMVGDQLFTDILGGNRAGLYTILV 108
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
196-261 2.15e-12

Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];


Pssm-ID: 441782  Cd Length: 164  Bit Score: 63.61  E-value: 2.15e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219858312 196 PYIV--GKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLVlTGITQRDEIASYPFR 261
Cdd:COG2179   84 PYIAraKKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILV-KPLVDKEFWFTRINR 150
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
193-276 2.33e-12

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 64.56  E-value: 2.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 193 GREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRmDTDIIAGMEAGLHTVLVLTGITQRDEIASYPfrPNQVLNSVADL 272
Cdd:COG0546  132 GGDDVPPAKPKPEPLLEALERLGLDPEEVLMVGDS-PHDIEAARAAGVPFIGVTWGYGSAEELEAAG--ADYVIDSLAEL 208


                 ....
gi 219858312 273 KNQL 276
Cdd:COG0546  209 LALL 212
HAD-SF-IIA-hyp4 TIGR01459
HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the ...
 18-247 5.95e-12

HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all gram negative and primarily alpha proteobacteria. Only one sequence hase been annotated as other than "hypothetical." That one, from Brucella, is annotated as related to NagD, but only by sequence similarity and should be treated with some skepticism. (See comments for Class IIA subfamily model)


Pssm-ID: 130526 [Multi-domain]  Cd Length: 242  Bit Score: 63.76  E-value: 5.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312   18 QDIECWLTDMDGVLVHENQAVPGAAELIQRwVDTSKRFLVLTNNSIFTPRDLAARLRASGLEIPEENIWTSALATAQFLK 97
Cdd:TIGR01459   6 NDYDVFLLDLWGVIIDGNHTYPGAVQNLNK-IIAQGKPVYFVSNSPRNIFSLHKTLKSLGINADLPEMIISSGEIAVQMI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312   98 DQVRGSGSGNRA--YTIGE--------AGLTTALHEAGfiltdQDPDFVVLGETRTYSFEAITTAIRLILAGAR---FIA 164
Cdd:TIGR01459  85 LESKKRFDIRNGiiYLLGHlendiinlMQCYTTDDENK-----ANASLITIYRSENEKLDLDEFDELFAPIVARkipNIC 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  165 TNPDATGPSKDGPMPATGAIAALITKATGREPYiVGKPNPMMFRSAMNQIDA-HSETTAMIGDRMDTDIIAGMEAGLHTV 243
Cdd:TIGR01459 160 ANPDRGINQHGIYRYGAGYYAELIKQLGGKVIY-SGKPYPAIFHKALKECSNiPKNRMLMVGDSFYTDILGANRLGIDTA 238


                  ....
gi 219858312  244 LVLT 247
Cdd:TIGR01459 239 LVLT 242
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 20-276 1.09e-09

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: 56.96  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  20 IECWLTDMDGVLVHENQAVPGAAELIQRWVdtskrflvltnNSIFTPRDLAARLRAsgleipeeniwtsalATAQFLKDQ 99
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERL-----------GLLDEAEELAEAYRA---------------IEYALWRRY 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 100 VRGSGSGnraytigEAGLTTALHEAGFILTDQDPDfvVLGETRTYSFEAITTAIRLI--LAGARF---IATNpdatgpsk 174
Cdd:COG1011   55 ERGEITF-------AELLRRLLEELGLDLAEELAE--AFLAALPELVEPYPDALELLeaLKARGYrlaLLTN-------- 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 175 dgpmpATGAIAALITKATGREPYI----------VGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVL 244
Cdd:COG1011  118 -----GSAELQEAKLRRLGLDDLFdavvsseevgVRKPDPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVW 192

                        250       260       270
                 ....*....|....*....|....*....|..
gi 219858312 245 vltgITQRDEIASYPFRPNQVLNSVADLKNQL 276
Cdd:COG1011  193 ----VNRSGEPAPAEPRPDYVISDLAELLELL 220
CTE7 TIGR02253
HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and ...
 199-272 1.02e-08

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


Pssm-ID: 274057 [Multi-domain]  Cd Length: 221  Bit Score: 54.33  E-value: 1.02e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219858312  199 VGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLVLTGITQRDEIASYPfRPNQVLNSVADL 272
Cdd:TIGR02253 148 VEKPHPKIFYAALKRLGVKPEEAVMVGDRLDKDIKGAKNAGMKTVWINQGKSSKMEDDVYP-YPDYEISSLREL 220
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 201-276 4.10e-08

Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 440011 [Multi-domain]  Cd Length: 176  Bit Score: 51.64  E-value: 4.10e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 219858312 201 KPNPMMFRSAMN--QID-AHSettAMIGDRMdTDIIAGMEAGLHTVLVLTGITQRDEIASypfRPNQVLNSVADLKNQL 276
Cdd:COG0241  102 KPKPGMLLQAAErlGIDlSNS---YMIGDRL-SDLQAAKAAGCKGILVLTGKGAEELAEA---LPDTVADDLAEAVDYL 173
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 199-243 1.67e-07

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 48.69  E-value: 1.67e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 219858312 199 VGKPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTV 243
Cdd:cd04305   62 VQKPNPEIFDYALNQLGVKPEETLMVGDSLESDILGAKNAGIKTV 106
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 201-274 1.88e-07

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 50.36  E-value: 1.88e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219858312 201 KPNPMMFRSAMNQIDAHSETTAMIGDRmDTDIIAGMEAGLHTVLVLTGITQRDEIASYPfrPNQVLNSVADLKN 274
Cdd:cd02616  136 KPDPEPVLKALELLGAEPEEALMVGDS-PHDILAGKNAGVKTVGVTWGYKGREYLKAFN--PDFIIDKMSDLLT 206
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
201-276 3.11e-07

D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 49.43  E-value: 3.11e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219858312 201 KPNPMMFRSAMNQIDAHSETTAMIGDRMDtDIIAGMEAGLHTVLVLTGITQRDEiASYPFRPNQVLNSVADLKNQL 276
Cdd:PRK08942 103 KPKPGMLLSIAERLNIDLAGSPMVGDSLR-DLQAAAAAGVTPVLVRTGKGVTTL-AEGAAPGTWVLDSLADLPQAL 176
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 190-272 1.23e-06

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 48.10  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 190 KATGREPY---IVG-------KPNPMMFRSAMNQIDAHSETTAMIGDRMDtDIIAGMEAGLHTVLVLTGITQRDEIASYp 259
Cdd:PRK13288 117 KLTGLDEFfdvVITlddvehaKPDPEPVLKALELLGAKPEEALMVGDNHH-DILAGKNAGTKTAGVAWTIKGREYLEQY- 194

                         90
                 ....*....|...
gi 219858312 260 fRPNQVLNSVADL 272
Cdd:PRK13288 195 -KPDFMLDKMSDL 206
YqeG_hyp_ppase TIGR01668
HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins ...
 180-249 2.07e-06

HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. This family consists of sequences from fungi, plants, cyanobacteria, gram-positive bacteria and Deinococcus. There is presently no characterization of any sequence in this family.


Pssm-ID: 273744  Cd Length: 170  Bit Score: 47.01  E-value: 2.07e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219858312  180 ATGAIAALITKATGRePYIVG--KPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLVLTGI 249
Cdd:TIGR01668  69 AGEQRAKAVEKALGI-PVLPHavKPPGCAFRRAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVEPLV 139
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 26-239 2.87e-06

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 46.81  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312   26 DMDGVLVHENqavPGAAELIQRWVDTskrflvltnnsifTPRDLAARLRASGLEIPEENIWTSALA-TAQFLKDQvrgSG 104
Cdd:pfam00702   7 DLDGTLTDGE---PVVTEAIAELASE-------------HPLAKAIVAAAEDLPIPVEDFTARLLLgKRDWLEEL---DI 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  105 SGNRAYTIGEAGLTTALHEAGFILTDQDPDFVVLGetrtysfeAITTAIRLILAGAR-FIATNPDATGPSKDgpMPATGa 183
Cdd:pfam00702  68 LRGLVETLEAEGLTVVLVELLGVIALADELKLYPG--------AAEALKALKERGIKvAILTGDNPEAAEAL--LRLLG- 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 219858312  184 IAALITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRMDtDIIAGMEAG 239
Cdd:pfam00702 137 LDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVN-DIPAAKAAG 191
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 201-247 2.07e-05

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 43.16  E-value: 2.07e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 219858312  201 KPNPMMFRSA---MNQIDAhsETTAMIGDRMDTDIIAGMEAGLHTVLVLT 247
Cdd:TIGR01662  88 KPKPGMFLEAlkrFNEIDP--EESVYVGDQDLTDLQAAKRVGLATILVAP 135
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
187-245 4.78e-05

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 42.96  E-value: 4.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 219858312  187 LITKATGREPYIVGKPNPMMFRSAMNQIDAHSETTAMIGDRmDTDIIAGMEAGLHTVLV 245
Cdd:pfam13419 121 YFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYVGDS-PRDIEAAKNAGIKVIAV 178
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 26-85 5.33e-05

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: 41.99  E-value: 5.33e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219858312  26 DMDGVLVHENQAVPGAAELIQRWVDTSKRFLVLTNNSIFTPRDLAARLRAS-GLEIPEENI 85
Cdd:cd07511    6 DIDGVLVRGKKPIPGAPKALKFLNDNKIPFIFLTNGGGFPESKRADFLSKLlGVEVSPDQV 66
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 201-245 1.33e-04

histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. 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: 319806 [Multi-domain]  Cd Length: 142  Bit Score: 40.98  E-value: 1.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 219858312 201 KPNPMMFRSAMNQIDAHSETTAMIGDRmDTDIIAGMEAGLHTVLV 245
Cdd:cd07503   99 KPKPGMLLDAAKELGIDLARSFVIGDR-LSDIQAARNAGCKGILV 142
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
 177-271 6.38e-04

HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all eukaryotes. One sequence (GP|13344995) is called "Cat Eye Syndrome critical region protein 5" (CECR5). This gene has been cloned from a pericentromere region of human chromosome 22 believed to be the location of the gene or genes responsible for Cat Eye Syndrome. This is one of a number of candidate genes. The Schizosaccharomyces pombe sequence (EGAD|138276) is annotated as "phosphatidyl synthase," however this is due entirely to a C-terminal region of the protein (outside the region of similarity of this model) which is highly homologous to a family of CDP-alcohol phosphatidyltransferases. (Thus, the annotation of GP|4226073 from C. elegans as similar to phosphatidyl synthase, is a mistake as this gene does not contain the C-terminal portion). The physical connection of the phosphatidyl synthase and the HAD-superfamily hydrolase domain in S. pombe may, however, be an important clue to the substrate for the hydrolases in this equivalog.


Pssm-ID: 200106 [Multi-domain]  Cd Length: 321  Bit Score: 40.63  E-value: 6.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312  177 PMPATG------AIAALITKATGR--EPYIVGKPNPMMFRSA-------------MNQIDAHSETTAMIGDRMDTDIIAG 235
Cdd:TIGR01456 201 KLNRFGqgafrlLLERIYLELNGKplQYYTLGKPTKLTYDFAedvlidwekrlsgTKPSTSPFHALYMVGDNPASDIIGA 280

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 219858312  236 MEAGLHTVLVLTGI-TQRDEIASYPfrPNQVLNSVAD 271
Cdd:TIGR01456 281 QNYGWFSCLVKTGVyNGGDDLKECK--PTLIVNDVFD 315
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 197-245 7.38e-04

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 38.81  E-value: 7.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 219858312 197 YIVG--KPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVLV 245
Cdd:cd16415   56 YEVGyeKPDPRIFQKALERLGVSPEEALHVGDDLKNDYLGARAVGWHALLV 106
PRK09449 PRK09449
dUMP phosphatase; Provisional
 199-242 1.28e-03

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 39.11  E-value: 1.28e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 219858312 199 VGKPNPMMFRSAMNQIDAHS-ETTAMIGDRMDTDIIAGMEAGLHT 242
Cdd:PRK09449 148 VAKPDVAIFDYALEQMGNPDrSRVLMVGDNLHSDILGGINAGIDT 192
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 208-273 1.44e-03

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 39.11  E-value: 1.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219858312 208 RSAMNQIDAHSETTAMIGDRMdTDIIAGMEAGLHTVLVLTGITQRDEIASYPfrPNQVLNSVADLK 273
Cdd:cd04302  144 RYALDTLGIAPEQAVMIGDRK-HDIIGARANGIDSIGVLYGYGSEDELEEAG--ATYIVETPAELL 206
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
180-272 1.57e-03

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 38.65  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219858312 180 ATGAIAALIT---KATGREPY---IV-------GKPNPMMFRSAMNQIDAHSETTAMIGDRmDTDIIAGMEAGLHTVLVL 246
Cdd:COG0637  108 ATSSPRENAEavlEAAGLLDYfdvIVtgddvarGKPDPDIYLLAAERLGVDPEECVVFEDS-PAGIRAAKAAGMRVVGVP 186

                         90       100
                 ....*....|....*....|....*.
gi 219858312 247 TGITQRDEIAsypfRPNQVLNSVADL 272
Cdd:COG0637  187 DGGTAEEELA----GADLVVDDLAEL 208
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 188-244 2.18e-03

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


Pssm-ID: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 38.13  E-value: 2.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 219858312 188 ITKATGREPYIVG----------KPNPMMFRSAMNQIDAHSETTAMIGDRmDTDIIAGMEAGLHTVL 244
Cdd:cd07523  107 ILKKDGIASYFTEivtsdngfprKPNPEAINYLLNKYQLNPEETVMIGDR-ELDIEAGHNAGISTIL 172
DREG-2 TIGR02252
REG-2-like, HAD superfamily (subfamily IA) hydrolase; This family of proteins includes ...
 197-244 2.26e-03

REG-2-like, HAD superfamily (subfamily IA) hydrolase; This family of proteins includes uncharacterized sequences from eukaryotes, cyanobacteria and Leptospira as well as the DREG-2 protein from Drosophila melanogaster which has been identified as a rhythmically (diurnally) regulated gene. This family is a member 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. This family is a member of subfamily 1A in which the cap domain consists of a predicted alpha helical bundle found in between the first and second catalytic motifs. A distinctive feature of this family is a conserved tandem pair of tryptophan residues in the cap domain. The most divergent sequences included within the scope of this model are from plants and have "FW" at this position instead. Most likely, these sequences, like the vast majority of HAD sequences, represent phosphatase enzymes.


Pssm-ID: 274056 [Multi-domain]  Cd Length: 203  Bit Score: 38.42  E-value: 2.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 219858312  197 YIVG--KPNPMMFRSAMNQIDAHSETTAMIGDRMDTDIIAGMEAGLHTVL 244
Cdd:TIGR02252 154 YEVGaeKPDPKIFQEALERAGISPEEALHIGDSLRNDYQGARAAGWRALL 203
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 200-239 3.01e-03

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 37.38  E-value: 3.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 219858312  200 GKPNPMMFRSAMNQIDAhSETTAMIGDRmDTDIIAGMEAG 239
Cdd:TIGR01549 127 SKPEPEIFLAALESLGV-PPEVLHVGDN-LNDIEGARNAG 164
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
201-272 3.71e-03

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 37.87  E-value: 3.71e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219858312 201 KPNPMMFRSAMNQIDAHSETTAMIGDRMdTDIIAGMEAGLHTVLVLTGITQRDEIASYPfrPNQVLNSVADL 272
Cdd:PRK13222 149 KPDPAPLLLACEKLGLDPEEMLFVGDSR-NDIQAARAAGCPSVGVTYGYNYGEPIALSE--PDVVIDHFAEL 217
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 200-272 8.15e-03

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 36.61  E-value: 8.15e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219858312 200 GKPNPMMFRSAMNQIDAHSETTAMIGDRMdTDIIAGMEAGLHTVLVLTGITQRDEIASYPfrPNQVLNSVADL 272
Cdd:cd07533  138 SKPHPEMLREILAELGVDPSRAVMVGDTA-YDMQMAANAGAHAVGVAWGYHSLEDLRSAG--ADAVVDHFSEL 207
 
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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