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Conserved domains on  [gi|1831510635|ref|NP_001367732|]
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Putative cytosolic 5'-nucleotidase 3 [Caenorhabditis elegans]

Protein Classification

HAD family hydrolase( domain architecture ID 10019287)

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-SF-IE TIGR01544
haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a ...
37-323 2.65e-173

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: 481.66  E-value: 2.65e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635  37 LGEEQILVADPTAVAAKLRKMVVGGAGKTVVISDFDYTLSRFANEQGERLSTTHGVFDDnVMRLKPELGQKFVDLKNKYY 116
Cdd:TIGR01544   1 LTQDHCRMRDPTEVERIINEFVIGGAEKMQIISDFDYTLSRFRTEDGGRVPTSHGIFDA-CQSLPEEFKAKTDKLKHKYY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 117 PIEFSPNLTMEEKIPHMEKWWGTSHSLIVNEKFSKNTIEDFVRQSRIVFKDGAEDFIEALDAHNIPLVIFSAGIGNIIEY 196
Cdd:TIGR01544  80 PIEIDPHLTIEEKVPYMIEWWTKSHELTVGFPFDKSEIDQIVSKSTHALKDGTEEFFADLQRHGIPTLIFSAGIGNSVES 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 197 FLQQKlGAIPRNTHFISNMILFDEDDNACAFSEPLIHTFCKNSSVIQKETSFFHDIAGRVNVILLGDSMGDIHMDVGVER 276
Cdd:TIGR01544 160 VLRQA-NVLHPNVKVVSNFLQFDEDGLLDGFQQPLIHTFNKNETVLNETTEYFDLVHTRDNIILLGDSIGDADMASGVPA 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1831510635 277 DGPTLKVGYYNGSLDDtaALQHYEEVYDIVLIHDPTLNVAQKIVDII 323
Cdd:TIGR01544 239 SSHILKIGYLNDHVDA--NLKKYMDTYDIVLVDDQTLDVARTILSLI 283
 
Name Accession Description Interval E-value
HAD-SF-IE TIGR01544
haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a ...
37-323 2.65e-173

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: 481.66  E-value: 2.65e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635  37 LGEEQILVADPTAVAAKLRKMVVGGAGKTVVISDFDYTLSRFANEQGERLSTTHGVFDDnVMRLKPELGQKFVDLKNKYY 116
Cdd:TIGR01544   1 LTQDHCRMRDPTEVERIINEFVIGGAEKMQIISDFDYTLSRFRTEDGGRVPTSHGIFDA-CQSLPEEFKAKTDKLKHKYY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 117 PIEFSPNLTMEEKIPHMEKWWGTSHSLIVNEKFSKNTIEDFVRQSRIVFKDGAEDFIEALDAHNIPLVIFSAGIGNIIEY 196
Cdd:TIGR01544  80 PIEIDPHLTIEEKVPYMIEWWTKSHELTVGFPFDKSEIDQIVSKSTHALKDGTEEFFADLQRHGIPTLIFSAGIGNSVES 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 197 FLQQKlGAIPRNTHFISNMILFDEDDNACAFSEPLIHTFCKNSSVIQKETSFFHDIAGRVNVILLGDSMGDIHMDVGVER 276
Cdd:TIGR01544 160 VLRQA-NVLHPNVKVVSNFLQFDEDGLLDGFQQPLIHTFNKNETVLNETTEYFDLVHTRDNIILLGDSIGDADMASGVPA 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1831510635 277 DGPTLKVGYYNGSLDDtaALQHYEEVYDIVLIHDPTLNVAQKIVDII 323
Cdd:TIGR01544 239 SSHILKIGYLNDHVDA--NLKKYMDTYDIVLVDDQTLDVARTILSLI 283
HAD_5NT cd07504
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5 ...
46-324 6.65e-144

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: 406.70  E-value: 6.65e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635  46 DPTAVAAKLRKMVVGGAGKTVVISDFDYTLSRFANEQGERLsTTHGVFDDNVMrLKPELGQKFVDLKNKYYPIEFSPNLT 125
Cdd:cd07504     1 DPTRVEEKICGLVKGGADKLQIISDFDMTLSRFRYNGGRCP-TCHNIFDNCKL-LTEECRAKLVQLKEKYYPIEIDPHLT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 126 MEEKIPHMEKWWGTSHSLIVNEKFSKNTIEDFVRQSRIVFKDGAEDFIEALDAHNIPLVIFSAGIGNIIEYFLQQKLGAi 205
Cdd:cd07504    79 IEEKVPYMEEWWTKSHELLIEQGFQKDAIDQIVAESDIALRDGYEEFFEKLQQHGIPVLIFSAGLGDIIEEVLRQAGVY- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 206 PRNTHFISNMILFDEDDNACAFSEPLIHTFCKNSSVIqKETSFFHDIAGRVNVILLGDSMGDIHMDVGVERDGPTLKVGY 285
Cdd:cd07504   158 HPNVKVVSNFMDFDDNGVLTGFKGPLIHVFNKNESAL-KNTDYFKQLKGRTNIILLGDSIGDLRMADGVPNVEHILKIGF 236
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1831510635 286 YNGSLDdtAALQHYEEVYDIVLIHDPTLNVAQKIVDIIN 324
Cdd:cd07504   237 LNDKVE--ELLEKYMDSYDIVLVNDETLDVPNSILQKIL 273
UMPH-1 pfam05822
Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5 ...
73-323 8.82e-81

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: 245.73  E-value: 8.82e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635  73 YTLSRFANEqGERLSTTHGVFDdNVMRLKPELGQKFVDLKNKYYPIEFSPNLTMEEKIPHMEKWWGTSHSLIVNEKFSKN 152
Cdd:pfam05822   1 MTLSKFRVN-GERCPSSHGIFD-NCKSIPEECRKKLRELYHKYYPIEIDPHMPIEEKVPYMVEWWTKSHALLIGQGLQKE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 153 TIEDFVRQSRIVFKDGAEDFIEALDAHNIPLVIFSAGIGNIIEYFLQQKlGAIPRNTHFISNMILFDEDDNACAFSEPLI 232
Cdd:pfam05822  79 AIAEVVAESDIMLRDGTHEFFDDLQQLNVPVLIFSAGLGDVLEEVLRQA-NVMHPNVKVVSNFMDFDDDGVLNGFKGPLI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 233 HTFCKNSSVIqKETSFFHDIAGRVNVILLGDSMGDIHMDVGVERDGPTLKVGYYNGSLDdtAALQHYEEVYDIVLIHDPT 312
Cdd:pfam05822 158 HTFNKNETVL-DGTEYFDQLHTRDNIILLGDSLGDLGMADGVPSVEHILKIGFLNDKVE--ENLDKYMDAFDIVLVDDQT 234
                         250
                  ....*....|.
gi 1831510635 313 LNVAQKIVDII 323
Cdd:pfam05822 235 MDVPNAILEMI 245
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
124-207 1.94e-03

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 39.04  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 124 LTMEEKIPHMEKWWGTSHSL--IVNEKfsKNTIEDFVRQSRIVFKDGAEDFIEALDAHNIPLVIFSAGIGNIIEYFLqQK 201
Cdd:COG0637    46 RSREDILRYLLEEYGLDLPEeeLAARK--EELYRELLAEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVL-EA 122

                  ....*.
gi 1831510635 202 LGAIPR 207
Cdd:COG0637   123 AGLLDY 128
 
Name Accession Description Interval E-value
HAD-SF-IE TIGR01544
haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a ...
37-323 2.65e-173

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: 481.66  E-value: 2.65e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635  37 LGEEQILVADPTAVAAKLRKMVVGGAGKTVVISDFDYTLSRFANEQGERLSTTHGVFDDnVMRLKPELGQKFVDLKNKYY 116
Cdd:TIGR01544   1 LTQDHCRMRDPTEVERIINEFVIGGAEKMQIISDFDYTLSRFRTEDGGRVPTSHGIFDA-CQSLPEEFKAKTDKLKHKYY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 117 PIEFSPNLTMEEKIPHMEKWWGTSHSLIVNEKFSKNTIEDFVRQSRIVFKDGAEDFIEALDAHNIPLVIFSAGIGNIIEY 196
Cdd:TIGR01544  80 PIEIDPHLTIEEKVPYMIEWWTKSHELTVGFPFDKSEIDQIVSKSTHALKDGTEEFFADLQRHGIPTLIFSAGIGNSVES 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 197 FLQQKlGAIPRNTHFISNMILFDEDDNACAFSEPLIHTFCKNSSVIQKETSFFHDIAGRVNVILLGDSMGDIHMDVGVER 276
Cdd:TIGR01544 160 VLRQA-NVLHPNVKVVSNFLQFDEDGLLDGFQQPLIHTFNKNETVLNETTEYFDLVHTRDNIILLGDSIGDADMASGVPA 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1831510635 277 DGPTLKVGYYNGSLDDtaALQHYEEVYDIVLIHDPTLNVAQKIVDII 323
Cdd:TIGR01544 239 SSHILKIGYLNDHVDA--NLKKYMDTYDIVLVDDQTLDVARTILSLI 283
HAD_5NT cd07504
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5 ...
46-324 6.65e-144

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: 406.70  E-value: 6.65e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635  46 DPTAVAAKLRKMVVGGAGKTVVISDFDYTLSRFANEQGERLsTTHGVFDDNVMrLKPELGQKFVDLKNKYYPIEFSPNLT 125
Cdd:cd07504     1 DPTRVEEKICGLVKGGADKLQIISDFDMTLSRFRYNGGRCP-TCHNIFDNCKL-LTEECRAKLVQLKEKYYPIEIDPHLT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 126 MEEKIPHMEKWWGTSHSLIVNEKFSKNTIEDFVRQSRIVFKDGAEDFIEALDAHNIPLVIFSAGIGNIIEYFLQQKLGAi 205
Cdd:cd07504    79 IEEKVPYMEEWWTKSHELLIEQGFQKDAIDQIVAESDIALRDGYEEFFEKLQQHGIPVLIFSAGLGDIIEEVLRQAGVY- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 206 PRNTHFISNMILFDEDDNACAFSEPLIHTFCKNSSVIqKETSFFHDIAGRVNVILLGDSMGDIHMDVGVERDGPTLKVGY 285
Cdd:cd07504   158 HPNVKVVSNFMDFDDNGVLTGFKGPLIHVFNKNESAL-KNTDYFKQLKGRTNIILLGDSIGDLRMADGVPNVEHILKIGF 236
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1831510635 286 YNGSLDdtAALQHYEEVYDIVLIHDPTLNVAQKIVDIIN 324
Cdd:cd07504   237 LNDKVE--ELLEKYMDSYDIVLVNDETLDVPNSILQKIL 273
UMPH-1 pfam05822
Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5 ...
73-323 8.82e-81

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: 245.73  E-value: 8.82e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635  73 YTLSRFANEqGERLSTTHGVFDdNVMRLKPELGQKFVDLKNKYYPIEFSPNLTMEEKIPHMEKWWGTSHSLIVNEKFSKN 152
Cdd:pfam05822   1 MTLSKFRVN-GERCPSSHGIFD-NCKSIPEECRKKLRELYHKYYPIEIDPHMPIEEKVPYMVEWWTKSHALLIGQGLQKE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 153 TIEDFVRQSRIVFKDGAEDFIEALDAHNIPLVIFSAGIGNIIEYFLQQKlGAIPRNTHFISNMILFDEDDNACAFSEPLI 232
Cdd:pfam05822  79 AIAEVVAESDIMLRDGTHEFFDDLQQLNVPVLIFSAGLGDVLEEVLRQA-NVMHPNVKVVSNFMDFDDDGVLNGFKGPLI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 233 HTFCKNSSVIqKETSFFHDIAGRVNVILLGDSMGDIHMDVGVERDGPTLKVGYYNGSLDdtAALQHYEEVYDIVLIHDPT 312
Cdd:pfam05822 158 HTFNKNETVL-DGTEYFDQLHTRDNIILLGDSLGDLGMADGVPSVEHILKIGFLNDKVE--ENLDKYMDAFDIVLVDDQT 234
                         250
                  ....*....|.
gi 1831510635 313 LNVAQKIVDII 323
Cdd:pfam05822 235 MDVPNAILEMI 245
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
148-268 2.50e-05

phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine 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: 319801 [Multi-domain]  Cd Length: 202  Bit Score: 44.58  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 148 KFSKNTIEDFVRQSRIVFKDGAEDFIEALDAHNIPLVIFSAGIGNIIEYFLQQkLGaIPRnTHFISNMILFDEDDNACAF 227
Cdd:cd04309    56 NPTKEQVDEFLEEHPPRLTPGVEELVSRLKARGVEVYLISGGFRELIEPVASQ-LG-IPL-ENVFANRLLFDFNGEYAGF 132
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1831510635 228 --SEPLIHTFCKnSSVIQKETSFFHDiagrVNVILLGDSMGDI 268
Cdd:cd04309   133 deTQPTSRSGGK-AKVIEQLKEKHHY----KRVIMIGDGATDL 170
HAD pfam12710
haloacid dehalogenase-like hydrolase;
157-270 9.02e-05

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 42.52  E-value: 9.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 157 FVRQSRIVFKDGAEDFIEALDAHNIPLVIFSAGIGNIIEYFLqQKLGAIprntHFISNMILFDED--DNACAFSEPLIHT 234
Cdd:pfam12710  77 VAEVALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVL-AELGFD----EVLATELEVDDGrfTGELRLIGPPCAG 151
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1831510635 235 FCKNSSViqKETSFFHDI-AGRVNVILLGDSMGDIHM 270
Cdd:pfam12710 152 EGKVRRL--RAWLAARGLgLDLADSVAYGDSPSDLPM 186
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
124-207 1.94e-03

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 39.04  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 124 LTMEEKIPHMEKWWGTSHSL--IVNEKfsKNTIEDFVRQSRIVFKDGAEDFIEALDAHNIPLVIFSAGIGNIIEYFLqQK 201
Cdd:COG0637    46 RSREDILRYLLEEYGLDLPEeeLAARK--EELYRELLAEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVL-EA 122

                  ....*.
gi 1831510635 202 LGAIPR 207
Cdd:COG0637   123 AGLLDY 128
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
66-270 2.35e-03

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: 38.49  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635  66 VVISDFDYTLSRFanEQGERLSTTHGVFDDNVMRLKPELGQKFvdlknkyypIEFSPNLTMEEKIPHMekwwgtshsliv 145
Cdd:TIGR01488   1 LAIFDFDGTLTRQ--DSLIDLLAKLLGTNDEVIELTRLAPSGR---------ISFEDALGRRLALLHR------------ 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 146 neKFSKNTIEDFVRQSRIVfKDGAEDFIEALDAHNIPLVIFSAGIGNIIEYFLqQKLGaIPRNthfISNMILFDEDDN-A 224
Cdd:TIGR01488  58 --SRSEEVAKEFLARQVAL-RPGARELISWLKERGIDTVIVSGGFDFFVEPVA-EKLG-IDDV---FANRLEFDDNGLlT 129
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1831510635 225 CAFSEPLIHTFCKNSSVIQK---ETSFfhdiaGRVNVILLGDSMGDIHM 270
Cdd:TIGR01488 130 GPIEGQVNPEGECKGKVLKElleESKI-----TLKKIIAVGDSVNDLPM 173
HAD_Pase cd07524
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like ...
150-270 4.35e-03

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: 37.70  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635 150 SKNTIEDFVRQsRIVFKDGAEDFIEALDAHNIPLVIFSAGIGNIIEYFLQQKLGAiprNTHFISNMILFDED------DN 223
Cdd:cd07524    59 LKDEIIEFLEK-TAKIRPGFKEFVAFCQEHGIPFIIVSGGMDFFIEPLLEGLVIE---KIAIYCNGSDFSGEqihidwPH 134
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1831510635 224 ACAFSEPLIHtfCKnSSVIQKETSFfhdiagRVNVILLGDSMGDIHM 270
Cdd:cd07524   135 ECDCTNGCGC--CK-SSIIRKYSKP------RPFIIVIGDSVTDLEA 172
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
66-189 5.50e-03

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; 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, (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 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the 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 related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 37.40  E-value: 5.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510635  66 VVISDFDYTLsrfaneqgerLSTTHGVFDDNVMRLKPELGQkfvDLKNKYYpiefspnLTMEEKIP-HMEKWWGTSHSLI 144
Cdd:TIGR01509   1 AILFDLDGVL----------VDTEFAIAKLINREELGLVPD---ELGVSAV-------GRLELALRrFKAQYGRTISPED 60
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1831510635 145 VNEKFSKNTIEDFVRQSRIVFKDGAEDFIEALDAHNIPLVIFSAG 189
Cdd:TIGR01509  61 AQLLYKQLFYEQIEEEAKLKPLPGVRALLEALRARGKKLALLTNS 105
 
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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