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Conserved domains on  [gi|19922890|ref|NP_611895|]
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cytosolic 5'-nucleotidase IIIB [Drosophila melanogaster]

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 ...
22-303 0e+00

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: 503.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890    22 LTQDHCRMRDPAEVERIINEFVIGGPERMQIVSDFDYTITKQRTEDGGAVPSSFGIFNACQSLPENFKAETDKLYHKYRP 101
Cdd:TIGR01544   1 LTQDHCRMRDPTEVERIINEFVIGGAEKMQIISDFDYTLSRFRTEDGGRVPTSHGIFDACQSLPEEFKAKTDKLKHKYYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890   102 IEIDPHMPIAEKVQYMIEWWTKSGELTSGFPFDQSEIDQIASKYTHALRDRTHEFFADLQRLGIPTLVFSAGLGNSVVSV 181
Cdd:TIGR01544  81 IEIDPHLTIEEKVPYMIEWWTKSHELTVGFPFDKSEIDQIVSKSTHALKDGTEEFFADLQRHGIPTLIFSAGIGNSVESV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890   182 LRQANVLHPNVKVVSNFLQF-RDGLLDGFQQPMIHTFNKNETVLNETSEYYDLVHTRDHIIVMGDSIGDADMASGVPASS 260
Cdd:TIGR01544 161 LRQANVLHPNVKVVSNFLQFdEDGLLDGFQQPLIHTFNKNETVLNETTEYFDLVHTRDNIILLGDSIGDADMASGVPASS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 19922890   261 HIMKIGFLFDHVEANMKKYMDTFDIVLVDDQTMDVPRTLLSLI 303
Cdd:TIGR01544 241 HILKIGYLNDHVDANLKKYMDTYDIVLVDDQTLDVARTILSLI 283
 
Name Accession Description Interval E-value
HAD-SF-IE TIGR01544
haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a ...
22-303 0e+00

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: 503.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890    22 LTQDHCRMRDPAEVERIINEFVIGGPERMQIVSDFDYTITKQRTEDGGAVPSSFGIFNACQSLPENFKAETDKLYHKYRP 101
Cdd:TIGR01544   1 LTQDHCRMRDPTEVERIINEFVIGGAEKMQIISDFDYTLSRFRTEDGGRVPTSHGIFDACQSLPEEFKAKTDKLKHKYYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890   102 IEIDPHMPIAEKVQYMIEWWTKSGELTSGFPFDQSEIDQIASKYTHALRDRTHEFFADLQRLGIPTLVFSAGLGNSVVSV 181
Cdd:TIGR01544  81 IEIDPHLTIEEKVPYMIEWWTKSHELTVGFPFDKSEIDQIVSKSTHALKDGTEEFFADLQRHGIPTLIFSAGIGNSVESV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890   182 LRQANVLHPNVKVVSNFLQF-RDGLLDGFQQPMIHTFNKNETVLNETSEYYDLVHTRDHIIVMGDSIGDADMASGVPASS 260
Cdd:TIGR01544 161 LRQANVLHPNVKVVSNFLQFdEDGLLDGFQQPLIHTFNKNETVLNETTEYFDLVHTRDNIILLGDSIGDADMASGVPASS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 19922890   261 HIMKIGFLFDHVEANMKKYMDTFDIVLVDDQTMDVPRTLLSLI 303
Cdd:TIGR01544 241 HILKIGYLNDHVDANLKKYMDTYDIVLVDDQTLDVARTILSLI 283
UMPH-1 pfam05822
Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5 ...
58-304 1.33e-158

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: 442.57  E-value: 1.33e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890    58 YTITKQRTeDGGAVPSSFGIFNACQSLPENFKAETDKLYHKYRPIEIDPHMPIAEKVQYMIEWWTKSGELTSGFPFDQSE 137
Cdd:pfam05822   1 MTLSKFRV-NGERCPSSHGIFDNCKSIPEECRKKLRELYHKYYPIEIDPHMPIEEKVPYMVEWWTKSHALLIGQGLQKEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890   138 IDQIASKYTHALRDRTHEFFADLQRLGIPTLVFSAGLGNSVVSVLRQANVLHPNVKVVSNFLQF-RDGLLDGFQQPMIHT 216
Cdd:pfam05822  80 IAEVVAESDIMLRDGTHEFFDDLQQLNVPVLIFSAGLGDVLEEVLRQANVMHPNVKVVSNFMDFdDDGVLNGFKGPLIHT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890   217 FNKNETVLnETSEYYDLVHTRDHIIVMGDSIGDADMASGVPASSHIMKIGFLFDHVEANMKKYMDTFDIVLVDDQTMDVP 296
Cdd:pfam05822 160 FNKNETVL-DGTEYFDQLHTRDNIILLGDSLGDLGMADGVPSVEHILKIGFLNDKVEENLDKYMDAFDIVLVDDQTMDVP 238

                  ....*...
gi 19922890   297 RTLLSLIE 304
Cdd:pfam05822 239 NAILEMIL 246
HAD_5NT cd07504
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5 ...
31-304 2.04e-153

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: 430.58  E-value: 2.04e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890  31 DPAEVERIINEFVIGGPERMQIVSDFDYTITKQRTEDGGAvPSSFGIFNACQSLPENFKAETDKLYHKYRPIEIDPHMPI 110
Cdd:cd07504   1 DPTRVEEKICGLVKGGADKLQIISDFDMTLSRFRYNGGRC-PTCHNIFDNCKLLTEECRAKLVQLKEKYYPIEIDPHLTI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890 111 AEKVQYMIEWWTKSGELTSGFPFDQSEIDQIASKYTHALRDRTHEFFADLQRLGIPTLVFSAGLGNSVVSVLRQANVLHP 190
Cdd:cd07504  80 EEKVPYMEEWWTKSHELLIEQGFQKDAIDQIVAESDIALRDGYEEFFEKLQQHGIPVLIFSAGLGDIIEEVLRQAGVYHP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890 191 NVKVVSNFLQFRD-GLLDGFQQPMIHTFNKNETVLNETSEYYDLvHTRDHIIVMGDSIGDADMASGVPASSHIMKIGFLF 269
Cdd:cd07504 160 NVKVVSNFMDFDDnGVLTGFKGPLIHVFNKNESALKNTDYFKQL-KGRTNIILLGDSIGDLRMADGVPNVEHILKIGFLN 238
                       250       260       270
                ....*....|....*....|....*....|....*
gi 19922890 270 DHVEANMKKYMDTFDIVLVDDQTMDVPRTLLSLIE 304
Cdd:cd07504 239 DKVEELLEKYMDSYDIVLVNDETLDVPNSILQKIL 273
 
Name Accession Description Interval E-value
HAD-SF-IE TIGR01544
haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a ...
22-303 0e+00

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: 503.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890    22 LTQDHCRMRDPAEVERIINEFVIGGPERMQIVSDFDYTITKQRTEDGGAVPSSFGIFNACQSLPENFKAETDKLYHKYRP 101
Cdd:TIGR01544   1 LTQDHCRMRDPTEVERIINEFVIGGAEKMQIISDFDYTLSRFRTEDGGRVPTSHGIFDACQSLPEEFKAKTDKLKHKYYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890   102 IEIDPHMPIAEKVQYMIEWWTKSGELTSGFPFDQSEIDQIASKYTHALRDRTHEFFADLQRLGIPTLVFSAGLGNSVVSV 181
Cdd:TIGR01544  81 IEIDPHLTIEEKVPYMIEWWTKSHELTVGFPFDKSEIDQIVSKSTHALKDGTEEFFADLQRHGIPTLIFSAGIGNSVESV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890   182 LRQANVLHPNVKVVSNFLQF-RDGLLDGFQQPMIHTFNKNETVLNETSEYYDLVHTRDHIIVMGDSIGDADMASGVPASS 260
Cdd:TIGR01544 161 LRQANVLHPNVKVVSNFLQFdEDGLLDGFQQPLIHTFNKNETVLNETTEYFDLVHTRDNIILLGDSIGDADMASGVPASS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 19922890   261 HIMKIGFLFDHVEANMKKYMDTFDIVLVDDQTMDVPRTLLSLI 303
Cdd:TIGR01544 241 HILKIGYLNDHVDANLKKYMDTYDIVLVDDQTLDVARTILSLI 283
UMPH-1 pfam05822
Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5 ...
58-304 1.33e-158

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: 442.57  E-value: 1.33e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890    58 YTITKQRTeDGGAVPSSFGIFNACQSLPENFKAETDKLYHKYRPIEIDPHMPIAEKVQYMIEWWTKSGELTSGFPFDQSE 137
Cdd:pfam05822   1 MTLSKFRV-NGERCPSSHGIFDNCKSIPEECRKKLRELYHKYYPIEIDPHMPIEEKVPYMVEWWTKSHALLIGQGLQKEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890   138 IDQIASKYTHALRDRTHEFFADLQRLGIPTLVFSAGLGNSVVSVLRQANVLHPNVKVVSNFLQF-RDGLLDGFQQPMIHT 216
Cdd:pfam05822  80 IAEVVAESDIMLRDGTHEFFDDLQQLNVPVLIFSAGLGDVLEEVLRQANVMHPNVKVVSNFMDFdDDGVLNGFKGPLIHT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890   217 FNKNETVLnETSEYYDLVHTRDHIIVMGDSIGDADMASGVPASSHIMKIGFLFDHVEANMKKYMDTFDIVLVDDQTMDVP 296
Cdd:pfam05822 160 FNKNETVL-DGTEYFDQLHTRDNIILLGDSLGDLGMADGVPSVEHILKIGFLNDKVEENLDKYMDAFDIVLVDDQTMDVP 238

                  ....*...
gi 19922890   297 RTLLSLIE 304
Cdd:pfam05822 239 NAILEMIL 246
HAD_5NT cd07504
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5 ...
31-304 2.04e-153

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: 430.58  E-value: 2.04e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890  31 DPAEVERIINEFVIGGPERMQIVSDFDYTITKQRTEDGGAvPSSFGIFNACQSLPENFKAETDKLYHKYRPIEIDPHMPI 110
Cdd:cd07504   1 DPTRVEEKICGLVKGGADKLQIISDFDMTLSRFRYNGGRC-PTCHNIFDNCKLLTEECRAKLVQLKEKYYPIEIDPHLTI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890 111 AEKVQYMIEWWTKSGELTSGFPFDQSEIDQIASKYTHALRDRTHEFFADLQRLGIPTLVFSAGLGNSVVSVLRQANVLHP 190
Cdd:cd07504  80 EEKVPYMEEWWTKSHELLIEQGFQKDAIDQIVAESDIALRDGYEEFFEKLQQHGIPVLIFSAGLGDIIEEVLRQAGVYHP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922890 191 NVKVVSNFLQFRD-GLLDGFQQPMIHTFNKNETVLNETSEYYDLvHTRDHIIVMGDSIGDADMASGVPASSHIMKIGFLF 269
Cdd:cd07504 160 NVKVVSNFMDFDDnGVLTGFKGPLIHVFNKNESALKNTDYFKQL-KGRTNIILLGDSIGDLRMADGVPNVEHILKIGFLN 238
                       250       260       270
                ....*....|....*....|....*....|....*
gi 19922890 270 DHVEANMKKYMDTFDIVLVDDQTMDVPRTLLSLIE 304
Cdd:cd07504 239 DKVEELLEKYMDSYDIVLVNDETLDVPNSILQKIL 273
 
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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