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Conserved domains on  [gi|24656330|ref|NP_728791|]
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uncharacterized protein Dmel_CG32487 [Drosophila melanogaster]

Protein Classification

HAD family hydrolase( domain architecture ID 11576405)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 26-311 2.56e-157

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: 440.97  E-value: 2.56e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330  26 QWLKTIDTIIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAKNEILSSVQTLAK 105
Cdd:cd07532   1 EWLANIDTVIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 106 FMKEKKFKKKCYVVGGQGIVDELKLVGIESLPLDHSSLQGFSMPDHIHSIYLDPNVGAVVVGSDKDFNTIKLTKACCYLR 185
Cdd:cd07532  81 YLKEKGFKKKVYVIGEEGIRKELEEAGIVSCGGDGEDEKDDSMGDFAHNLELDPDVGAVVVGRDEHFSYPKLMKACNYLR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 186 DSEVMFVATSRDAALPAAPGRMVPSAGVMVAAIQAASQRMPFTCGKPNPYMCIDLMQKGVIQPDRTLIIGDTMCTDILLG 265
Cdd:cd07532 161 NPDVLFLATNMDATFPGPVGRVIPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILFA 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 24656330 266 YKCGFQTLLVGTGVNSYQDAIEAQGSKAPLLYQQVPDLYMPKLSNL 311
Cdd:cd07532 241 NNCGFQSLLVGTGVNSLEDAEKIKKEGDPKKKDLVPDTYLPSLGHL 286
 
Name Accession Description Interval E-value
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 26-311 2.56e-157

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: 440.97  E-value: 2.56e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330  26 QWLKTIDTIIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAKNEILSSVQTLAK 105
Cdd:cd07532   1 EWLANIDTVIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 106 FMKEKKFKKKCYVVGGQGIVDELKLVGIESLPLDHSSLQGFSMPDHIHSIYLDPNVGAVVVGSDKDFNTIKLTKACCYLR 185
Cdd:cd07532  81 YLKEKGFKKKVYVIGEEGIRKELEEAGIVSCGGDGEDEKDDSMGDFAHNLELDPDVGAVVVGRDEHFSYPKLMKACNYLR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 186 DSEVMFVATSRDAALPAAPGRMVPSAGVMVAAIQAASQRMPFTCGKPNPYMCIDLMQKGVIQPDRTLIIGDTMCTDILLG 265
Cdd:cd07532 161 NPDVLFLATNMDATFPGPVGRVIPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILFA 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 24656330 266 YKCGFQTLLVGTGVNSYQDAIEAQGSKAPLLYQQVPDLYMPKLSNL 311
Cdd:cd07532 241 NNCGFQSLLVGTGVNSLEDAEKIKKEGDPKKKDLVPDTYLPSLGHL 286
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
 30-311 1.20e-72

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: 225.90  E-value: 1.20e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330    30 TIDTIIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAKNEILSSVQTLAKFM-K 108
Cdd:TIGR01452   1 TAQGFIFDCDGVLWLGERVVPGAPELLDRLARAGKQILFVTNNSTKSRAEYALKFARLGFNGLAEQLFSSALCAARLLrQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330   109 EKKFKKKCYVVGGQGIVDELKLVGIEsLPLDHSSLQGFSMPDHIHSIYLDPNVGAVVVGSDKDFNTIKLTKACCYLRDSE 188
Cdd:TIGR01452  81 PPDAGKAVYVIGEEGLRAELDAAGIR-LAGDPGEKKQDEADGFMYDIKLDERVGAVVVGYDEHFSYVKLMEACAHLREPG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330   189 VMFVATSRDAALPAAPGRMVPSAGVMVAAIQAASQRMPFTCGKPNPYMCIDLMQKGVIQPDRTLIIGDTMCTDILLGYKC 268
Cdd:TIGR01452 160 CLFVATNRDPWHPLSDGSRTPGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRLETDILFGHRC 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 24656330   269 GFQTLLVGTGVNSYQDAIEAQGSKAPLLyqqVPDLYMPKLSNL 311
Cdd:TIGR01452 240 GMTTVLVLSGVSQLEEAQEYLMAGQDDL---VPDYVVESLADL 279
PLN02645 PLN02645
phosphoglycolate phosphatase
 28-312 1.65e-54

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 180.29  E-value: 1.65e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330   28 LKTIDTIIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAKNEILSSVQTLAK-- 105
Cdd:PLN02645  25 IDSVETFIFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSFAAAAyl 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330  106 FMKEKKFKKKCYVVGGQGIVDELKLVGIESL--PLDHS---SLQGFSMPDHihsiylDPNVGAVVVGSDKDFNTIKLTKA 180
Cdd:PLN02645 105 KSINFPKDKKVYVIGEEGILEELELAGFQYLggPEDGDkkiELKPGFLMEH------DKDVGAVVVGFDRYINYYKIQYA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330  181 C-CYLRDSEVMFVATSRDAALPAAPGRMVPSAGVMVAAIQAASQRMPFTCGKPNPYMCIDLMQKGVIQPDRTLIIGDTMC 259
Cdd:PLN02645 179 TlCIRENPGCLFIATNRDAVTHLTDAQEWAGAGSMVGAIKGSTEREPLVVGKPSTFMMDYLANKFGIEKSQICMVGDRLD 258

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 24656330  260 TDILLGYKCGFQTLLVGTGVNSyQDAIEAQGSKApllyqqVPDLYMPKLSNLL 312
Cdd:PLN02645 259 TDILFGQNGGCKTLLVLSGVTS-ESMLLSPENKI------QPDFYTSKISDFL 304
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
28-312 4.59e-52

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 172.22  E-value: 4.59e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330  28 LKTIDTIIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAKNEILSSVQTLAKFM 107
Cdd:COG0647   5 ADRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 108 KEKKFKKKCYVVGGQGIVDELKLVGIEslpldhsslqgfsmpdhihsIYLDPNVGAVVVGSDKDFNTIKLTKACCYLRDs 187
Cdd:COG0647  85 AERHPGARVYVIGEEGLREELEEAGLT--------------------LVDDEEPDAVVVGLDRTFTYEKLAEALRAIRR- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 188 EVMFVATSRDAALPaAPGRMVPSAGVMVAAIQAASQRMPFTCGKPNPYM---CIDLMQkgvIQPDRTLIIGDTMCTDILL 264
Cdd:COG0647 144 GAPFIATNPDRTVP-TEDGLIPGAGALAAALEAATGGEPLVVGKPSPPIyelALERLG---VDPERVLMVGDRLDTDILG 219

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 24656330 265 GYKCGFQTLLVGTGVNSYQDAIEAqgskapllyQQVPDLYMPKLSNLL 312
Cdd:COG0647 220 ANAAGLDTLLVLTGVTTAEDLEAA---------PIRPDYVLDSLAELL 258
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 34-134 1.02e-27

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 103.70  E-value: 1.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330    34 IIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAKNEILSSVQTLAKFMKEKKFK 113
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKERKFG 80

                          90       100
                  ....*....|....*....|.
gi 24656330   114 KKCYVVGGQGIVDELKLVGIE 134
Cdd:pfam13344  81 KKVLVIGSEGLREELEEAGFE 101
 
Name Accession Description Interval E-value
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 26-311 2.56e-157

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: 440.97  E-value: 2.56e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330  26 QWLKTIDTIIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAKNEILSSVQTLAK 105
Cdd:cd07532   1 EWLANIDTVIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 106 FMKEKKFKKKCYVVGGQGIVDELKLVGIESLPLDHSSLQGFSMPDHIHSIYLDPNVGAVVVGSDKDFNTIKLTKACCYLR 185
Cdd:cd07532  81 YLKEKGFKKKVYVIGEEGIRKELEEAGIVSCGGDGEDEKDDSMGDFAHNLELDPDVGAVVVGRDEHFSYPKLMKACNYLR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 186 DSEVMFVATSRDAALPAAPGRMVPSAGVMVAAIQAASQRMPFTCGKPNPYMCIDLMQKGVIQPDRTLIIGDTMCTDILLG 265
Cdd:cd07532 161 NPDVLFLATNMDATFPGPVGRVIPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILFA 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 24656330 266 YKCGFQTLLVGTGVNSYQDAIEAQGSKAPLLYQQVPDLYMPKLSNL 311
Cdd:cd07532 241 NNCGFQSLLVGTGVNSLEDAEKIKKEGDPKKKDLVPDTYLPSLGHL 286
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
 30-311 1.20e-72

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: 225.90  E-value: 1.20e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330    30 TIDTIIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAKNEILSSVQTLAKFM-K 108
Cdd:TIGR01452   1 TAQGFIFDCDGVLWLGERVVPGAPELLDRLARAGKQILFVTNNSTKSRAEYALKFARLGFNGLAEQLFSSALCAARLLrQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330   109 EKKFKKKCYVVGGQGIVDELKLVGIEsLPLDHSSLQGFSMPDHIHSIYLDPNVGAVVVGSDKDFNTIKLTKACCYLRDSE 188
Cdd:TIGR01452  81 PPDAGKAVYVIGEEGLRAELDAAGIR-LAGDPGEKKQDEADGFMYDIKLDERVGAVVVGYDEHFSYVKLMEACAHLREPG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330   189 VMFVATSRDAALPAAPGRMVPSAGVMVAAIQAASQRMPFTCGKPNPYMCIDLMQKGVIQPDRTLIIGDTMCTDILLGYKC 268
Cdd:TIGR01452 160 CLFVATNRDPWHPLSDGSRTPGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRLETDILFGHRC 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 24656330   269 GFQTLLVGTGVNSYQDAIEAQGSKAPLLyqqVPDLYMPKLSNL 311
Cdd:TIGR01452 240 GMTTVLVLSGVSQLEEAQEYLMAGQDDL---VPDYVVESLADL 279
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 31-315 2.58e-72

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: 224.96  E-value: 2.58e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330  31 IDTIIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAK-NEILSSVQTLAK---F 106
Cdd:cd07510   1 VDTFLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTGLKeEEIFSSAYCAARylrQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 107 MKEKKFKKKCYVVGGQGIVDELKLVGIESLPLDHSSLQGFSMPDHIHsIYLDPNVGAVVVGSDKDFNTIKLTKACCYLRD 186
Cdd:cd07510  81 RLPGPADGKVYVLGGEGLRAELEAAGVAHLGGPDDGLRRAAPKDWLL-AGLDPDVGAVLVGLDEHVNYLKLAKATQYLRD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 187 SEVMFVATSRDAALPAAPGRMVPSAGVMVAAIQAASQRMPFTCGKPNPYMCIDLMQKGVIQPDRTLIIGDTMCTDILLGY 266
Cdd:cd07510 160 PGCLFVATNRDPWHPLSDGSFIPGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDTDILFGQ 239

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 24656330 267 KCGFQTLLVGTGVNSYQDAIEAQGSKApllyqqVPDLYMPKLSNLLPFL 315
Cdd:cd07510 240 NCGLKTLLVLTGVSTLEEALAKLSNDL------VPDYYVESLADLLELL 282
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 34-308 2.92e-71

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: 221.85  E-value: 2.92e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330  34 IIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAKNEILSSVQTLAKFMKEKKFK 113
Cdd:cd07508   2 VISDCDGVLWHDERAIPGAAEFLEALKEAGKKIVFVSNNSSRSRQDYAEKFRKFGVDVPEDQIVTSAKATARFLRSRKFG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 114 KKCYVVGGQGIVDELKLVGIESLplDHSSLQGFSMPDHIHSIYLDPNVGAVVVGSDKDFNTIKLTKACCYLRDSEVMFVA 193
Cdd:cd07508  82 KKVYVLGEEGLKEELRAAGFRIA--GGPSKGIETYAELVEHLEDDENVDAVIVGSDFKLNFAKLRKACRYLRNPGCLFIA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 194 TSRDAALPAAPGRMVPSAGVMVAAIQAASQRMPFTCGKPNPYMCIDLMQKGVIQPDRTLIIGDTMCTDILLGYKCGFQTL 273
Cdd:cd07508 160 TAPDRIHPLKDGGPIPGTGAFAAAVEAATGRQPLVLGKPSPWLGELALEKFGIDPERVLFVGDRLATDVLFGKACGFQTL 239

                       250       260       270
                ....*....|....*....|....*....|....*
gi 24656330 274 LVGTGVNSYQDAieaqgsKAPLLYQQVPDLYMPKL 308
Cdd:cd07508 240 LVLTGVTTLEDL------QAYIDHELVPDYYADSL 268
PLN02645 PLN02645
phosphoglycolate phosphatase
 28-312 1.65e-54

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 180.29  E-value: 1.65e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330   28 LKTIDTIIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAKNEILSSVQTLAK-- 105
Cdd:PLN02645  25 IDSVETFIFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSFAAAAyl 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330  106 FMKEKKFKKKCYVVGGQGIVDELKLVGIESL--PLDHS---SLQGFSMPDHihsiylDPNVGAVVVGSDKDFNTIKLTKA 180
Cdd:PLN02645 105 KSINFPKDKKVYVIGEEGILEELELAGFQYLggPEDGDkkiELKPGFLMEH------DKDVGAVVVGFDRYINYYKIQYA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330  181 C-CYLRDSEVMFVATSRDAALPAAPGRMVPSAGVMVAAIQAASQRMPFTCGKPNPYMCIDLMQKGVIQPDRTLIIGDTMC 259
Cdd:PLN02645 179 TlCIRENPGCLFIATNRDAVTHLTDAQEWAGAGSMVGAIKGSTEREPLVVGKPSTFMMDYLANKFGIEKSQICMVGDRLD 258

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 24656330  260 TDILLGYKCGFQTLLVGTGVNSyQDAIEAQGSKApllyqqVPDLYMPKLSNLL 312
Cdd:PLN02645 259 TDILFGQNGGCKTLLVLSGVTS-ESMLLSPENKI------QPDFYTSKISDFL 304
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
28-312 4.59e-52

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 172.22  E-value: 4.59e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330  28 LKTIDTIIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAKNEILSSVQTLAKFM 107
Cdd:COG0647   5 ADRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 108 KEKKFKKKCYVVGGQGIVDELKLVGIEslpldhsslqgfsmpdhihsIYLDPNVGAVVVGSDKDFNTIKLTKACCYLRDs 187
Cdd:COG0647  85 AERHPGARVYVIGEEGLREELEEAGLT--------------------LVDDEEPDAVVVGLDRTFTYEKLAEALRAIRR- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 188 EVMFVATSRDAALPaAPGRMVPSAGVMVAAIQAASQRMPFTCGKPNPYM---CIDLMQkgvIQPDRTLIIGDTMCTDILL 264
Cdd:COG0647 144 GAPFIATNPDRTVP-TEDGLIPGAGALAAALEAATGGEPLVVGKPSPPIyelALERLG---VDPERVLMVGDRLDTDILG 219

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 24656330 265 GYKCGFQTLLVGTGVNSYQDAIEAqgskapllyQQVPDLYMPKLSNLL 312
Cdd:COG0647 220 ANAAGLDTLLVLTGVTTAEDLEAA---------PIRPDYVLDSLAELL 258
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 32-287 1.40e-39

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: 139.26  E-value: 1.40e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330  32 DTIIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAKNEILSSVQTLAKFMKEKK 111
Cdd:cd07530   1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSALATAQYLAEQL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 112 FKKKCYVVGGQGIVDELKLVGieslpldhsslqgFSMPDHihsiyldpNVGAVVVGSDKDFNTIKLTKACCYLRDSeVMF 191
Cdd:cd07530  81 PGAKVYVIGEEGLRTALHEAG-------------LTLTDE--------NPDYVVVGLDRDLTYEKLAEATLAIRNG-AKF 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 192 VATSRDAALPAAPGRmVPSAGVMVAAIQAASQRMPFTCGKPNPYMCIDLMQKGVIQPDRTLIIGDTMCTDILLGYKCGFQ 271
Cdd:cd07530 139 IATNPDLTLPTERGL-LPGNGSVVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGID 217

                       250
                ....*....|....*.
gi 24656330 272 TLLVGTGVNSYQDAIE 287
Cdd:cd07530 218 TLLVLTGVTTREDLAK 233
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 34-278 2.37e-38

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: 135.92  E-value: 2.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330    34 IIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFL-VAKNEILSSVQTLAKFMKEKKF 112
Cdd:TIGR01460   1 FLFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLSSLLGVdVSPDQIITSGSVTKDLLRQRFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330   113 KKKCYVVGGQGIVDELKLVGIEslpldhsslqgFSMPDHIHSIYLDPNVGAVVVGSDKDFNTIKLTKACCYLRDSEVMFV 192
Cdd:TIGR01460  81 GEKVYVIGVGELRESLEGLGFR-----------NDFFDDIDHLAIEKIPAAVIVGEPSDFSYDELAKAAYLLAEGDVPFI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330   193 ATSRDAALPAAPGRMVPSAGVMVAAIQAASQRMPFTCGKPNPY---MCIDLMQkgvIQPDRT-LIIGDTMCTDILLGYKC 268
Cdd:TIGR01460 150 AANRDDLVRLGDGRFRPGAGAIAAGIKELSGREPTVVGKPSPAiyrAALNLLQ---ARPERRdVMVGDNLRTDILGAKNA 226

                         250
                  ....*....|
gi 24656330   269 GFQTLLVGTG 278
Cdd:TIGR01460 227 GFDTLLVLTG 236
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 34-134 1.02e-27

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 103.70  E-value: 1.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330    34 IIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAKNEILSSVQTLAKFMKEKKFK 113
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKERKFG 80

                          90       100
                  ....*....|....*....|.
gi 24656330   114 KKCYVVGGQGIVDELKLVGIE 134
Cdd:pfam13344  81 KKVLVIGSEGLREELEEAGFE 101
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
 32-303 7.68e-27

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: 106.11  E-value: 7.68e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330  32 DTIIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAKNEILSSVQTLAKFMKEKK 111
Cdd:cd07531   1 KGYIIDLDGTIGKGVTLIPGAVEGVKTLRRLGKKIIFLSNNSTRSRRILLERLRSFGIEVGEDEILVSSYVTARFLAREK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 112 FKKKCYVVGGQGIVDELKLVGIESLpldhsslqgfSMPDHIHsiyldpnvgAVVVGSDKDFNTIKLTKACCYLRDSeVMF 191
Cdd:cd07531  81 PNAKVFVTGEEGLIEELRLAGLEIV----------DKYDEAE---------YVVVGSNRKITYELLTKAFRACLRG-ARY 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 192 VATSRDAALPaAPGRMVPSAGVMVAAIQAASQRMP-FTCGKPNPYMCIDLMQKGVIQPDRTLIIGDTMCTDILLGYKCGF 270
Cdd:cd07531 141 IATNPDRIFP-AEDGPIPDTAAIIGAIEWCTGREPeVVVGKPSEVMAREALDILGLDAKDCAIVGDQIDVDIAMGKAIGM 219

                       250       260       270
                ....*....|....*....|....*....|...
gi 24656330 271 QTLLVGTGVnSYQDAIEAQGSKAPLLYQQVPDL 303
Cdd:cd07531 220 ETALVLTGV-TTRENLDRHGYKPDYVLNSIKDL 251
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 35-278 1.82e-21

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: 91.34  E-value: 1.82e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330  35 IFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAKNEILSSVQTLAKFMKEKKFKK 114
Cdd:cd16422   3 IFDMDGTIYLGDDLIPGTLEFLERLHEKKRRYIFLTNNSSKNLADYVEKLNRLGIDAGLDRVFTSGEATIDHLKKEFIKP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 115 KCYVVGGQGIVDELKLVGIEslpLDhsslqgfsmpdhihsiylDPNVGAVVVGSDKDFNTIKLTKACCYLRDSeVMFVAT 194
Cdd:cd16422  83 KIFLLGTKSLREEFEKAGFT---LD------------------GDDIDVVVLGFDTELTYEKLRTACLLLRRG-IPYIAT 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 195 SRDAALPAaPGRMVPSAGVMVAAIQAASQRMPFTC-GKPNPYMCIDLMQKGVIQPDRTLIIGDTMCTDILLGYKCGFQTL 273
Cdd:cd16422 141 HPDINCPS-EEGPIPDAGSIIALIETSTGRRPDLViGKPNPIILDPVLEKFDYSKEETVMVGDRLYTDIVLGINAGVDSI 219


                ....*
gi 24656330 274 LVGTG 278
Cdd:cd16422 220 LVLSG 224
HAD-SF-IIA-hyp2 TIGR01457
HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of ...
 35-279 1.37e-19

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: 86.06  E-value: 1.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330    35 IFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAKNEILSSVQTLAKFMKEKKFKK 114
Cdd:TIGR01457   5 LIDLDGTMYNGTEKIEEACEFVRTLKKRGVPYLFVTNNSTRTPEQVADKLVSFDIPATEEQVFTTSMATAQYIAQQKKDA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330   115 KCYVVGGQGIVDELKLVGIeslpldhssLQGFSMPDHihsiyldpnvgaVVVGSDKDFNTIKLTKACCYLRDSeVMFVAT 194
Cdd:TIGR01457  85 SVYVIGEEGLREAIKENGL---------TFGGENPDY------------VVVGLDRSITYEKFAVACLAIRNG-ARFIST 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330   195 SRDAALPAAPGRMvPSAGVMVAAIQAASQRMPFTCGKPNPYMCIDLMQKGVIQPDRTLIIGDTMCTDILLGYKCGFQTLL 274
Cdd:TIGR01457 143 NGDIAIPTERGLL-PGNGSLTSVLTVSTGVKPVFIGKPESIIMEQAMRVLGTDVEETLMVGDNYATDIMAGINAGIDTLL 221


                  ....*
gi 24656330   275 VGTGV 279
Cdd:TIGR01457 222 VHTGV 226
PRK10444 PRK10444
HAD-IIA family hydrolase;
152-303 7.64e-18

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 81.38  E-value: 7.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330  152 IHSIY------LDPNVGAVVVGSDKDFNTIKLTKACcYLRDSEVMFVATSRDAALPAapgrMVPSAGVMVAAIQAASQRM 225
Cdd:PRK10444  94 IHELYkagftiTDINPDFVIVGETRSYNWDMMHKAA-YFVANGARFIATNPDTHGRG----FYPACGALCAGIEKISGRK 168

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24656330  226 PFTCGKPNPYMCIDLMQKGVIQPDRTLIIGDTMCTDILLGYKCGFQTLLVGTGVNSYQDaIEAQGSKAPLLYQQVPDL 303
Cdd:PRK10444 169 PFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSTLDD-IDSMPFRPSWIYPSVADI 245
Hydrolase_like pfam13242
HAD-hyrolase-like;
229-281 8.57e-13

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 62.63  E-value: 8.57e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24656330   229 CGKPNPYMCIDLMQKGVIQPDRTLIIGDTMCTDILLGYKCGFQTLLVGTGVNS 281
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTR 54
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 34-297 2.68e-12

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: 65.38  E-value: 2.68e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330  34 IIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGICKYAQEMGFLVAKNEILSSvqTLAKFMKEKKFK 113
Cdd:cd07509   3 VLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTS--LTAARQYLEEKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 114 KKCYVVggqgivdelklvgieslpLDHSSLQGFSMPDHIhsiylDPNvgAVVVGS-DKDFNTIKLTKACCYLRDSEVMfV 192
Cdd:cd07509  81 LRPHLL------------------VDDDALEDFIGIDTS-----DPN--AVVIGDaGEHFNYQTLNRAFRLLLDGAPL-I 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 193 ATSRDAALPAAPGRMVpSAGVMVAAIQAASQRMPFTCGKPNPYMCIDLMQKGVIQPDRTLIIGDTMCTDILLGYKCGFQT 272
Cdd:cd07509 135 ALHKGRYYKRKDGLAL-DPGAFVTGLEYATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRG 213

                       250       260
                ....*....|....*....|....*
gi 24656330 273 LLVGTGvnSYQDAIEAQGSKAPLLY 297
Cdd:cd07509 214 ILVRTG--KYRPSDEKKPNVPPDLT 236
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 32-306 8.38e-11

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: 61.19  E-value: 8.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330  32 DTIIFDGNGVLWSHGKVLENAAETFNALRAMGKKAFICTNnSVTSVEGICKYAQEMGFL-VAKNEILSSVQ-TLAKFMKE 109
Cdd:cd07525   1 DAFLLDLWGVLHDGNEPYPGAVEALAALRAAGKTVVLVTN-APRPAESVVRQLAKLGVPpSTYDAIITSGEvTRELLARE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 110 KKFKKKCYVVGGqgivdELKLVGIESLPLDHSSlqgfsmpdhihsiylDPNVGAVVV---GSDKDFNTIK-LTKACCYLR 185
Cdd:cd07525  80 AGLGRKVYHLGP-----ERDANVLEGLDVVATD---------------DAEKAEFILctgLYDDETETPEdYRKLLKAAA 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 186 DSEVMFVATSRDAALPAaPGRMVPSAGVMVAAIQAASQRMPFTcGKPNPyMCIDLMQK--GVIQPDRTLIIGDTMCTDIL 263
Cdd:cd07525 140 ARGLPLICANPDLVVPR-GGKLIYCAGALAELYEELGGEVIYF-GKPHP-PIYDLALArlGRPAKARILAVGDGLHTDIL 216

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 24656330 264 LGYKCGFQTLLVGTGVNSYQDAIEAqgskapLLYQQVPDLYMP 306
Cdd:cd07525 217 GANAAGLDSLFVTGGIHRRLAAEAG------IKSQIVPDFVIP 253
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
230-317 1.62e-06

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 48.00  E-value: 1.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330 230 GKPNPYMCIDLMQKGVIQPDRTLIIGDTMcTDILLGYKCGFQTLLVGTGVNSYQDAIEAQgskapllyqqvPDLYMPKLS 309
Cdd:COG0546 139 AKPKPEPLLEALERLGLDPEEVLMVGDSP-HDIEAARAAGVPFIGVTWGYGSAEELEAAG-----------ADYVIDSLA 206


                ....*...
gi 24656330 310 NLLPFLSS 317
Cdd:COG0546 207 ELLALLAE 214
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 229-278 3.60e-05

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: 43.55  E-value: 3.60e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24656330 229 CGKPNPYMCIDLMQKGVIQPDRTLIIGDTMcTDILLGYKCGFQTLLVGTG 278
Cdd:COG0241 100 CRKPKPGMLLQAAERLGIDLSNSYMIGDRL-SDLQAAKAAGCKGILVLTG 148
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 229-275 5.39e-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: 42.39  E-value: 5.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 24656330   229 CGKPNPYMCIDLMQK-GVIQPDRTLIIGDTMCTDILLGYKCGFQTLLV 275
Cdd:TIGR01662  86 CRKPKPGMFLEALKRfNEIDPEESVYVGDQDLTDLQAAKRVGLATILV 133
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 229-275 3.82e-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: 39.82  E-value: 3.82e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 24656330 229 CGKPNPYMCIDLMQKGVIQPDRTLIIGDTMcTDILLGYKCGFQTLLV 275
Cdd:cd07503  97 CRKPKPGMLLDAAKELGIDLARSFVIGDRL-SDIQAARNAGCKGILV 142
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 230-275 4.16e-04

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: 39.17  E-value: 4.16e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 24656330 230 GKPNPYMCIDLMQKGVIQPDRTLIIGDTMCTDILLGYKCGFQTLLV 275
Cdd:cd16416  63 GKPRPRAFRRALKEMDLPPEQVAMVGDQLFTDILGGNRAGLYTILV 108
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 2-84 1.02e-03

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: 39.49  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656330     2 NLALNKTFQKRGCQILGLNKYGIQQWLKTIDTIIfdgngVLWSHGKVLENAAETFNALRAMGKKAFICTNNSVTSVEGIC 81
Cdd:pfam00702  58 KRDWLEELDILRGLVETLEAEGLTVVLVELLGVI-----ALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALL 132


                  ...
gi 24656330    82 KYA 84
Cdd:pfam00702 133 RLL 135
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
230-275 3.78e-03

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


Pssm-ID: 441782  Cd Length: 164  Bit Score: 37.42  E-value: 3.78e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 24656330 230 GKPNP---YMCIDLMQkgvIQPDRTLIIGDTMCTDILLGYKCGFQTLLV 275
Cdd:COG2179  90 KKPLPrgfRKALKLMG---LPPEETAVVGDQLFTDVLGGNRAGLYTILV 135
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 34-78 8.85e-03

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 35.45  E-value: 8.85e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24656330  34 IIFDGNGVLWshgkvlenAAETFNALRAMGKKAFICTNNSVTSVE 78
Cdd:cd01427   2 VLFDLDGTLL--------AVELLKRLRAAGIKLAIVTNRSREALR 38
HAD-SF-IIA-hyp4 TIGR01459
HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the ...
 230-277 9.06e-03

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: 37.18  E-value: 9.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 24656330   230 GKPNPYMC-IDLMQKGVIQPDRTLIIGDTMCTDILLGYKCGFQTLLVGT 277
Cdd:TIGR01459 194 GKPYPAIFhKALKECSNIPKNRMLMVGDSFYTDILGANRLGIDTALVLT 242
 
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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