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Conserved domains on  [gi|1720367261|ref|XP_030102120|]
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7-methylguanosine phosphate-specific 5'-nucleotidase isoform X8 [Mus musculus]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
1-188 1.59e-120

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member pfam05822:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 246  Bit Score: 341.26  E-value: 1.59e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261   1 MVQWWSKAHSLLCQQRIQKVQIAQVVGESTAMLREGYKTFFDTLYQNNIPLFIFSAGIGDILEEIIRQMKVFHPNIHIVS 80
Cdd:pfam05822  59 MVEWWTKSHALLIGQGLQKEAIAEVVAESDIMLRDGTHEFFDDLQQLNVPVLIFSAGLGDVLEEVLRQANVMHPNVKVVS 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261  81 NYMDFSEDGFLKGFKGQLIHTYNKNSSVCENSSYFQQLQNKTNIILLGDSIGDLTMADGVPGVQNILKIGFLNDKVEERR 160
Cdd:pfam05822 139 NFMDFDDDGVLNGFKGPLIHTFNKNETVLDGTEYFDQLHTRDNIILLGDSLGDLGMADGVPSVEHILKIGFLNDKVEENL 218
                         170       180
                  ....*....|....*....|....*...
gi 1720367261 161 ERYMDSYDIVLEKDETLDVVNGLLRHIL 188
Cdd:pfam05822 219 DKYMDAFDIVLVDDQTMDVPNAILEMIL 246
 
Name Accession Description Interval E-value
UMPH-1 pfam05822
Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5 ...
1-188 1.59e-120

Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5'-nucleotidase proteins. P5'N-1, also known as uridine monophosphate hydrolase-1 (UMPH-1), is a member of a large functional group of enzymes, characterized by the ability to dephosphorylate nucleic acids. P5'N-1 catalyzes the dephosphorylation of pyrimidine nucleoside monophosphates to the corresponding nucleosides. Deficiencies in this proteins function can lead to several different disorders in humans.


Pssm-ID: 310424 [Multi-domain]  Cd Length: 246  Bit Score: 341.26  E-value: 1.59e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261   1 MVQWWSKAHSLLCQQRIQKVQIAQVVGESTAMLREGYKTFFDTLYQNNIPLFIFSAGIGDILEEIIRQMKVFHPNIHIVS 80
Cdd:pfam05822  59 MVEWWTKSHALLIGQGLQKEAIAEVVAESDIMLRDGTHEFFDDLQQLNVPVLIFSAGLGDVLEEVLRQANVMHPNVKVVS 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261  81 NYMDFSEDGFLKGFKGQLIHTYNKNSSVCENSSYFQQLQNKTNIILLGDSIGDLTMADGVPGVQNILKIGFLNDKVEERR 160
Cdd:pfam05822 139 NFMDFDDDGVLNGFKGPLIHTFNKNETVLDGTEYFDQLHTRDNIILLGDSLGDLGMADGVPSVEHILKIGFLNDKVEENL 218
                         170       180
                  ....*....|....*....|....*...
gi 1720367261 161 ERYMDSYDIVLEKDETLDVVNGLLRHIL 188
Cdd:pfam05822 219 DKYMDAFDIVLVDDQTMDVPNAILEMIL 246
HAD_5NT cd07504
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5 ...
1-188 1.98e-115

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5'-nucleotidases dephosphorylate nucleoside 5prime-monophosphates. This family includes human 5'-nucleotidase, cytosolic IIIA (cN-IIIA, previously called cN-III; NT5C3A) the main pyrimidine 5'-nucleotidase in erythrocytes which dephosphorylates the pyrimidine nucleotides CMP, UMP, TMP, and the purine 7-methylguanosine monophosphate (m7GM), and possesses phosphotransferase activity. It also includes human 5'-nucleotidase, cytosolic IIIB (cN-IIIB; NT5C3B) which has a strong preference for m7GMP, dephosphorylates CMP and UMP and, with significantly lower efficiency, GMP and AMP, and can also act as a phosphotransferase. 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: 319807 [Multi-domain]  Cd Length: 273  Bit Score: 329.27  E-value: 1.98e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261   1 MVQWWSKAHSLLCQQRIQKVQIAQVVGESTAMLREGYKTFFDTLYQNNIPLFIFSAGIGDILEEIIRQMKVFHPNIHIVS 80
Cdd:cd07504    86 MEEWWTKSHELLIEQGFQKDAIDQIVAESDIALRDGYEEFFEKLQQHGIPVLIFSAGLGDIIEEVLRQAGVYHPNVKVVS 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261  81 NYMDFSEDGFLKGFKGQLIHTYNKNSSVCENSSYFQQLQNKTNIILLGDSIGDLTMADGVPGVQNILKIGFLNDKVEERR 160
Cdd:cd07504   166 NFMDFDDNGVLTGFKGPLIHVFNKNESALKNTDYFKQLKGRTNIILLGDSIGDLRMADGVPNVEHILKIGFLNDKVEELL 245
                         170       180
                  ....*....|....*....|....*...
gi 1720367261 161 ERYMDSYDIVLEKDETLDVVNGLLRHIL 188
Cdd:cd07504   246 EKYMDSYDIVLVNDETLDVPNSILQKIL 273
HAD-SF-IE TIGR01544
haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a ...
1-187 4.89e-84

haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a small group of metazoan sequences. The sequences from mouse are annotated as Pyrimidine 5'-nucleotidases, aparrently in reference to HSPC233, the human homolog. However, no such annotation can currently be found for this gene. This group of sequences was found during searches for members of the haloacid dehalogenase (HAD) superfamily. All of the conserved catalytic motifs are found. The placement of the variable domain between motifs 1 and 2 indicates membership in subfamily I of the superfamily, but these sequences are sufficiently different from any of the branches (IA, TIGR01493, TIGR01509, TIGR01549; IB, TIGR01488; IC, TIGR01494; ID, TIGR01658; IF TIGR01545) of that subfamily as to constitute a separate branch to now be called IE. Considering that the closest identifiable hit outside of the noise range is to a phosphoserine phosphatase, this group may be considered to be most closely allied to subfamily IB.


Pssm-ID: 273683 [Multi-domain]  Cd Length: 283  Bit Score: 250.16  E-value: 4.89e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261   1 MVQWWSKAHSLLCQQRIQKVQIAQVVGESTAMLREGYKTFFDTLYQNNIPLFIFSAGIGDILEEIIRQMKVFHPNIHIVS 80
Cdd:TIGR01544  96 MIEWWTKSHELTVGFPFDKSEIDQIVSKSTHALKDGTEEFFADLQRHGIPTLIFSAGIGNSVESVLRQANVLHPNVKVVS 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261  81 NYMDFSEDGFLKGFKGQLIHTYNKNSSVC-ENSSYFQQLQNKTNIILLGDSIGDLTMADGVPGVQNILKIGFLNDKVEER 159
Cdd:TIGR01544 176 NFLQFDEDGLLDGFQQPLIHTFNKNETVLnETTEYFDLVHTRDNIILLGDSIGDADMASGVPASSHILKIGYLNDHVDAN 255
                         170       180
                  ....*....|....*....|....*...
gi 1720367261 160 RERYMDSYDIVLEKDETLDVVNGLLRHI 187
Cdd:TIGR01544 256 LKKYMDTYDIVLVDDQTLDVARTILSLI 283
mtnX PRK09552
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase; Reviewed
29-180 4.33e-07

2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase; Reviewed


Pssm-ID: 236562  Cd Length: 219  Bit Score: 48.44  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261  29 STAMLREGYKTFFDTLYQNNIPLFIFSAGIgD-----ILEEIIrqmkvfhPNIHIVSNYMDFSedgflkgfkGQLIH--- 100
Cdd:PRK09552   71 ETAEIREGFHEFVQFVKENNIPFYVVSGGM-DffvypLLQGLI-------PKEQIYCNGSDFS---------GEYITitw 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261 101 -----TYNKNSSVCENSSYFQQLQNKTN-IILLGDSIGDLT---MADGVpgvqniLKIGFLNDKVEERRERYM---DSYD 168
Cdd:PRK09552  134 phpcdEHCQNHCGCCKPSLIRKLSDTNDfHIVIGDSITDLEaakQADKV------FARDFLITKCEELGIPYTpfeTFHD 207
                         170
                  ....*....|..
gi 1720367261 169 IVLEKDETLDVV 180
Cdd:PRK09552  208 VQTELKHLLEVK 219
 
Name Accession Description Interval E-value
UMPH-1 pfam05822
Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5 ...
1-188 1.59e-120

Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5'-nucleotidase proteins. P5'N-1, also known as uridine monophosphate hydrolase-1 (UMPH-1), is a member of a large functional group of enzymes, characterized by the ability to dephosphorylate nucleic acids. P5'N-1 catalyzes the dephosphorylation of pyrimidine nucleoside monophosphates to the corresponding nucleosides. Deficiencies in this proteins function can lead to several different disorders in humans.


Pssm-ID: 310424 [Multi-domain]  Cd Length: 246  Bit Score: 341.26  E-value: 1.59e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261   1 MVQWWSKAHSLLCQQRIQKVQIAQVVGESTAMLREGYKTFFDTLYQNNIPLFIFSAGIGDILEEIIRQMKVFHPNIHIVS 80
Cdd:pfam05822  59 MVEWWTKSHALLIGQGLQKEAIAEVVAESDIMLRDGTHEFFDDLQQLNVPVLIFSAGLGDVLEEVLRQANVMHPNVKVVS 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261  81 NYMDFSEDGFLKGFKGQLIHTYNKNSSVCENSSYFQQLQNKTNIILLGDSIGDLTMADGVPGVQNILKIGFLNDKVEERR 160
Cdd:pfam05822 139 NFMDFDDDGVLNGFKGPLIHTFNKNETVLDGTEYFDQLHTRDNIILLGDSLGDLGMADGVPSVEHILKIGFLNDKVEENL 218
                         170       180
                  ....*....|....*....|....*...
gi 1720367261 161 ERYMDSYDIVLEKDETLDVVNGLLRHIL 188
Cdd:pfam05822 219 DKYMDAFDIVLVDDQTMDVPNAILEMIL 246
HAD_5NT cd07504
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5 ...
1-188 1.98e-115

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5'-nucleotidases dephosphorylate nucleoside 5prime-monophosphates. This family includes human 5'-nucleotidase, cytosolic IIIA (cN-IIIA, previously called cN-III; NT5C3A) the main pyrimidine 5'-nucleotidase in erythrocytes which dephosphorylates the pyrimidine nucleotides CMP, UMP, TMP, and the purine 7-methylguanosine monophosphate (m7GM), and possesses phosphotransferase activity. It also includes human 5'-nucleotidase, cytosolic IIIB (cN-IIIB; NT5C3B) which has a strong preference for m7GMP, dephosphorylates CMP and UMP and, with significantly lower efficiency, GMP and AMP, and can also act as a phosphotransferase. 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: 319807 [Multi-domain]  Cd Length: 273  Bit Score: 329.27  E-value: 1.98e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261   1 MVQWWSKAHSLLCQQRIQKVQIAQVVGESTAMLREGYKTFFDTLYQNNIPLFIFSAGIGDILEEIIRQMKVFHPNIHIVS 80
Cdd:cd07504    86 MEEWWTKSHELLIEQGFQKDAIDQIVAESDIALRDGYEEFFEKLQQHGIPVLIFSAGLGDIIEEVLRQAGVYHPNVKVVS 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261  81 NYMDFSEDGFLKGFKGQLIHTYNKNSSVCENSSYFQQLQNKTNIILLGDSIGDLTMADGVPGVQNILKIGFLNDKVEERR 160
Cdd:cd07504   166 NFMDFDDNGVLTGFKGPLIHVFNKNESALKNTDYFKQLKGRTNIILLGDSIGDLRMADGVPNVEHILKIGFLNDKVEELL 245
                         170       180
                  ....*....|....*....|....*...
gi 1720367261 161 ERYMDSYDIVLEKDETLDVVNGLLRHIL 188
Cdd:cd07504   246 EKYMDSYDIVLVNDETLDVPNSILQKIL 273
HAD-SF-IE TIGR01544
haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a ...
1-187 4.89e-84

haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a small group of metazoan sequences. The sequences from mouse are annotated as Pyrimidine 5'-nucleotidases, aparrently in reference to HSPC233, the human homolog. However, no such annotation can currently be found for this gene. This group of sequences was found during searches for members of the haloacid dehalogenase (HAD) superfamily. All of the conserved catalytic motifs are found. The placement of the variable domain between motifs 1 and 2 indicates membership in subfamily I of the superfamily, but these sequences are sufficiently different from any of the branches (IA, TIGR01493, TIGR01509, TIGR01549; IB, TIGR01488; IC, TIGR01494; ID, TIGR01658; IF TIGR01545) of that subfamily as to constitute a separate branch to now be called IE. Considering that the closest identifiable hit outside of the noise range is to a phosphoserine phosphatase, this group may be considered to be most closely allied to subfamily IB.


Pssm-ID: 273683 [Multi-domain]  Cd Length: 283  Bit Score: 250.16  E-value: 4.89e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261   1 MVQWWSKAHSLLCQQRIQKVQIAQVVGESTAMLREGYKTFFDTLYQNNIPLFIFSAGIGDILEEIIRQMKVFHPNIHIVS 80
Cdd:TIGR01544  96 MIEWWTKSHELTVGFPFDKSEIDQIVSKSTHALKDGTEEFFADLQRHGIPTLIFSAGIGNSVESVLRQANVLHPNVKVVS 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261  81 NYMDFSEDGFLKGFKGQLIHTYNKNSSVC-ENSSYFQQLQNKTNIILLGDSIGDLTMADGVPGVQNILKIGFLNDKVEER 159
Cdd:TIGR01544 176 NFLQFDEDGLLDGFQQPLIHTFNKNETVLnETTEYFDLVHTRDNIILLGDSIGDADMASGVPASSHILKIGYLNDHVDAN 255
                         170       180
                  ....*....|....*....|....*...
gi 1720367261 160 RERYMDSYDIVLEKDETLDVVNGLLRHI 187
Cdd:TIGR01544 256 LKKYMDTYDIVLVDDQTLDVARTILSLI 283
HAD_Pase cd07524
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like ...
28-175 2.05e-10

phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like superfamily; Bacillus subtilis recycles two toxic byproducts of polyamine metabolism, methylthioadenosine and methylthioribose, into methionine by a salvage pathway. The sixth reaction in this pathway is catalyzed by B. subtilis MtnX: the dephosphorylation of 2- hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HKMTP- 1-P) into 1,2-dihydroxy-3-keto-5-methylthiopentene. The hydrolysis of HK-MTP-1-P is a two-step mechanism involving the formation of a transiently phosphorylated aspartyl intermediate. 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: 319826 [Multi-domain]  Cd Length: 211  Bit Score: 57.73  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261  28 ESTAMLREGYKTFFDTLYQNNIPLFIFSAGIGDILEEIIRQMKVfhPNIHIVSNYMDFSedgflkgfkGQLIHTYNKNSS 107
Cdd:cd07524    68 EKTAKIRPGFKEFVAFCQEHGIPFIIVSGGMDFFIEPLLEGLVI--EKIAIYCNGSDFS---------GEQIHIDWPHEC 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261 108 VCEN------SSYFQQLQNKTN-IILLGDSIGDLTMA---DGVpgvqniLKIGFLNDKVEERRERYM---DSYDIVLEKD 174
Cdd:cd07524   137 DCTNgcgcckSSIIRKYSKPRPfIIVIGDSVTDLEAAkeaDLV------FARDGLILKCEEENLPYPpfeTFTDIDIHLQ 210

                  .
gi 1720367261 175 E 175
Cdd:cd07524   211 L 211
mtnX PRK09552
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase; Reviewed
29-180 4.33e-07

2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase; Reviewed


Pssm-ID: 236562  Cd Length: 219  Bit Score: 48.44  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261  29 STAMLREGYKTFFDTLYQNNIPLFIFSAGIgD-----ILEEIIrqmkvfhPNIHIVSNYMDFSedgflkgfkGQLIH--- 100
Cdd:PRK09552   71 ETAEIREGFHEFVQFVKENNIPFYVVSGGM-DffvypLLQGLI-------PKEQIYCNGSDFS---------GEYITitw 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261 101 -----TYNKNSSVCENSSYFQQLQNKTN-IILLGDSIGDLT---MADGVpgvqniLKIGFLNDKVEERRERYM---DSYD 168
Cdd:PRK09552  134 phpcdEHCQNHCGCCKPSLIRKLSDTNDfHIVIGDSITDLEaakQADKV------FARDFLITKCEELGIPYTpfeTFHD 207
                         170
                  ....*....|..
gi 1720367261 169 IVLEKDETLDVV 180
Cdd:PRK09552  208 VQTELKHLLEVK 219
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
11-137 1.45e-04

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 40.80  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261  11 LLCQQRIQKVQIAQVVGESTAMLREGYKTFFDTLYQNNIPLFIFSAGIGDILEEIIRQMkvfhpNIH-IVSNYMDFSEDG 89
Cdd:TIGR01488  52 LALLHRSRSEEVAKEFLARQVALRPGARELISWLKERGIDTVIVSGGFDFFVEPVAEKL-----GIDdVFANRLEFDDNG 126
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1720367261  90 FLKGFKGQLIHTYNKNsSVCENSSYFQQLQ-NKTNIILLGDSIGDLTMA 137
Cdd:TIGR01488 127 LLTGPIEGQVNPEGEC-KGKVLKELLEESKiTLKKIIAVGDSVNDLPML 174
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
38-137 2.95e-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: 35.83  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367261  38 KTFFDTLYQNNIPLFIFSAGIGDILEEIIRQMKVFHPNIHIVSnymdfSEDGFlkgfkgqlihtYNKNSSVCENSSYFQQ 117
Cdd:cd01427    13 VELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIG-----SDGGG-----------TPKPKPKPLLLLLLKL 76
                          90       100
                  ....*....|....*....|
gi 1720367261 118 LQNKTNIILLGDSIGDLTMA 137
Cdd:cd01427    77 GVDPEEVLFVGDSENDIEAA 96
 
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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