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Conserved domains on  [gi|1045559357|ref|NP_001316547|]
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ectonucleotide pyrophosphatase/phosphodiesterase family member 5 isoform 2 [Mus musculus]

Protein Classification

nucleotide pyrophosphatase/phosphodiesterase family protein( domain architecture ID 12025720)

nucleotide pyrophosphatase/phosphodiesterase family protein catalyzes the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and/or nucleotide sugars; belongs to the alkaline phosphatase superfamily

CATH:  3.40.720.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
17-273 6.61e-77

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


:

Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 241.94  E-value: 6.61e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357  17 ENHGIVANDMFDPILNKSFSLEHMDIYDSKFWEEAtPIWITNQRAGHASGAAMWPGADVKIHD---SFPTYYL-PYNESV 92
Cdd:pfam01663  58 GSHGIVGNTFYDPKTGEYLVFVISDPEDPRWWQGE-PIWDTAAKAGVRAAALFWPGSEVDYSTyygTPPRYLKdDYNNSV 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357  93 SFEDRVAKII--EWFT------AKDPINLGFLYWEEPDDTGHDVGPDSPLMGSVISDVDHKLGYLIKMLKRAKLWNNVNL 164
Cdd:pfam01663 137 PFEDRVDTAVlqTWLDlpfadvAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNV 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357 165 IVTSDHGMTQCSKQRVIELDRYLDKE-HYTLIDHSPVAAILPK--------EGKFDEVYDALAGA--------HPNLTVY 227
Cdd:pfam01663 217 IVVSDHGMTPVSDDKVIFLNDYLREKgLLHLVDGGPVVAIYPKarelghvpPGEVEEVYAELKEKllglriqdGEHLAVY 296
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1045559357 228 KKEEIPERWHYkhNDRVQPIVAVADEGWYILQNKSDDFLL---GNHGYD 273
Cdd:pfam01663 297 LKEEIPGRLHY--NPRIPDLVLVADPGWYITGKDGGDKEAaihGTHGYD 343
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
17-273 6.61e-77

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 241.94  E-value: 6.61e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357  17 ENHGIVANDMFDPILNKSFSLEHMDIYDSKFWEEAtPIWITNQRAGHASGAAMWPGADVKIHD---SFPTYYL-PYNESV 92
Cdd:pfam01663  58 GSHGIVGNTFYDPKTGEYLVFVISDPEDPRWWQGE-PIWDTAAKAGVRAAALFWPGSEVDYSTyygTPPRYLKdDYNNSV 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357  93 SFEDRVAKII--EWFT------AKDPINLGFLYWEEPDDTGHDVGPDSPLMGSVISDVDHKLGYLIKMLKRAKLWNNVNL 164
Cdd:pfam01663 137 PFEDRVDTAVlqTWLDlpfadvAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNV 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357 165 IVTSDHGMTQCSKQRVIELDRYLDKE-HYTLIDHSPVAAILPK--------EGKFDEVYDALAGA--------HPNLTVY 227
Cdd:pfam01663 217 IVVSDHGMTPVSDDKVIFLNDYLREKgLLHLVDGGPVVAIYPKarelghvpPGEVEEVYAELKEKllglriqdGEHLAVY 296
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1045559357 228 KKEEIPERWHYkhNDRVQPIVAVADEGWYILQNKSDDFLL---GNHGYD 273
Cdd:pfam01663 297 LKEEIPGRLHY--NPRIPDLVLVADPGWYITGKDGGDKEAaihGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
17-313 4.30e-72

Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 226.70  E-value: 4.30e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357  17 ENHGIVANDMFDPILNKSFSleHMDIYDSKFWEEATPIWITNQRAGHASGAAMWPGADVKIHDSFPT------YYLPYNE 90
Cdd:cd16018    60 ESHGIVGNYFYDPKTNEEFS--DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTpiplggYWQPYND 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357  91 SVSFEDRVAKIIEWFTAKDPiNLGFLYWEEPDDTGHDVGPDSPLMGSVISDVDHKLGYLIKMLKRAKLWNNVNLIVTSDH 170
Cdd:cd16018   138 SFPFEERVDTILEWLDLERP-DLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDH 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357 171 GMTQcskqrvieldryldkehytlidhspvaailpkegkfdevydalagahpnltvykkeeiperwhykhndrvqpivav 250
Cdd:cd16018   217 GMTD---------------------------------------------------------------------------- 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045559357 251 adegwyilqnksddflLGNHGYDNALAEMHPIFLAHGPAFRKNFTKEAMNSTDLYSLLCHLLN 313
Cdd:cd16018   221 ----------------VGTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
19-314 1.66e-51

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 176.86  E-value: 1.66e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357  19 HGIVANDMFDPILNKSFSL--EHMDIYDSKFWEEATPIWITNQRAGHASGAAMWPG----------ADVKIHDSFPTYYL 86
Cdd:COG1524    84 HGIVGNGWYDPELGRVVNSlsWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFWPSfegsglidaaRPYPYDGRKPLLGN 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357  87 PYNESVSFEDrVAKIIEwftAKDPiNLGFLYWEEPDDTGHDVGPDSPLMGSVISDVDHKLGYLIKMLKRAKLWNNVNLIV 166
Cdd:COG1524   164 PAADRWIAAA-ALELLR---EGRP-DLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIV 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357 167 TSDHGMTQCSKQrvIELDRyLDKEHYTLIDHSPVAAILPKEGKFDEVYDALAGAhpnLTVYKKEEIpERWHYKHNdRVQP 246
Cdd:COG1524   239 TADHGMVDVPPD--IDLNR-LRLAGLLAVRAGESAHLYLKDGADAEVRALLGLP---ARVLTREEL-AAGHFGPH-RIGD 310
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1045559357 247 IVAVADEGWYIlqnksDDFLLGNHGYDNAlAEMHPIFLAHGPAFRKNFtkeamNSTDLYSLLCHLLNL 314
Cdd:COG1524   311 LVLVAKPGWAL-----DAPLKGSHGGLPD-EEMRVPLLASGPGFRPGV-----RNVDVAPTIARLLGL 367
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
17-273 6.61e-77

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 241.94  E-value: 6.61e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357  17 ENHGIVANDMFDPILNKSFSLEHMDIYDSKFWEEAtPIWITNQRAGHASGAAMWPGADVKIHD---SFPTYYL-PYNESV 92
Cdd:pfam01663  58 GSHGIVGNTFYDPKTGEYLVFVISDPEDPRWWQGE-PIWDTAAKAGVRAAALFWPGSEVDYSTyygTPPRYLKdDYNNSV 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357  93 SFEDRVAKII--EWFT------AKDPINLGFLYWEEPDDTGHDVGPDSPLMGSVISDVDHKLGYLIKMLKRAKLWNNVNL 164
Cdd:pfam01663 137 PFEDRVDTAVlqTWLDlpfadvAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNV 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357 165 IVTSDHGMTQCSKQRVIELDRYLDKE-HYTLIDHSPVAAILPK--------EGKFDEVYDALAGA--------HPNLTVY 227
Cdd:pfam01663 217 IVVSDHGMTPVSDDKVIFLNDYLREKgLLHLVDGGPVVAIYPKarelghvpPGEVEEVYAELKEKllglriqdGEHLAVY 296
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1045559357 228 KKEEIPERWHYkhNDRVQPIVAVADEGWYILQNKSDDFLL---GNHGYD 273
Cdd:pfam01663 297 LKEEIPGRLHY--NPRIPDLVLVADPGWYITGKDGGDKEAaihGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
17-313 4.30e-72

Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 226.70  E-value: 4.30e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357  17 ENHGIVANDMFDPILNKSFSleHMDIYDSKFWEEATPIWITNQRAGHASGAAMWPGADVKIHDSFPT------YYLPYNE 90
Cdd:cd16018    60 ESHGIVGNYFYDPKTNEEFS--DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTpiplggYWQPYND 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357  91 SVSFEDRVAKIIEWFTAKDPiNLGFLYWEEPDDTGHDVGPDSPLMGSVISDVDHKLGYLIKMLKRAKLWNNVNLIVTSDH 170
Cdd:cd16018   138 SFPFEERVDTILEWLDLERP-DLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDH 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357 171 GMTQcskqrvieldryldkehytlidhspvaailpkegkfdevydalagahpnltvykkeeiperwhykhndrvqpivav 250
Cdd:cd16018   217 GMTD---------------------------------------------------------------------------- 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045559357 251 adegwyilqnksddflLGNHGYDNALAEMHPIFLAHGPAFRKNFTKEAMNSTDLYSLLCHLLN 313
Cdd:cd16018   221 ----------------VGTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
19-314 1.66e-51

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 176.86  E-value: 1.66e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357  19 HGIVANDMFDPILNKSFSL--EHMDIYDSKFWEEATPIWITNQRAGHASGAAMWPG----------ADVKIHDSFPTYYL 86
Cdd:COG1524    84 HGIVGNGWYDPELGRVVNSlsWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFWPSfegsglidaaRPYPYDGRKPLLGN 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357  87 PYNESVSFEDrVAKIIEwftAKDPiNLGFLYWEEPDDTGHDVGPDSPLMGSVISDVDHKLGYLIKMLKRAKLWNNVNLIV 166
Cdd:COG1524   164 PAADRWIAAA-ALELLR---EGRP-DLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIV 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357 167 TSDHGMTQCSKQrvIELDRyLDKEHYTLIDHSPVAAILPKEGKFDEVYDALAGAhpnLTVYKKEEIpERWHYKHNdRVQP 246
Cdd:COG1524   239 TADHGMVDVPPD--IDLNR-LRLAGLLAVRAGESAHLYLKDGADAEVRALLGLP---ARVLTREEL-AAGHFGPH-RIGD 310
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1045559357 247 IVAVADEGWYIlqnksDDFLLGNHGYDNAlAEMHPIFLAHGPAFRKNFtkeamNSTDLYSLLCHLLNL 314
Cdd:COG1524   311 LVLVAKPGWAL-----DAPLKGSHGGLPD-EEMRVPLLASGPGFRPGV-----RNVDVAPTIARLLGL 367
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
98-206 9.80e-12

alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.


Pssm-ID: 293732 [Multi-domain]  Cd Length: 237  Bit Score: 64.36  E-value: 9.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357  98 VAKIIEWFTAKDPiNLGFLYWEEPDDTGHDVGPDSPLMGSVISDVDHKLGYLIKMLKRAKLWNNVNLIVTSDHGMTQCSK 177
Cdd:cd00016   108 LLKAIDETSKEKP-FVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGH 186
                          90       100
                  ....*....|....*....|....*....
gi 1045559357 178 QRVIELDRYLDKEHYTliDHSPVAAILPK 206
Cdd:cd00016   187 GGDPKADGKADKSHTG--MRVPFIAYGPG 213
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
139-171 8.35e-05

Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.


Pssm-ID: 293752 [Multi-domain]  Cd Length: 449  Bit Score: 44.56  E-value: 8.35e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1045559357 139 ISDVDHKLGYLIKMLKRAKLWNNVNLIVTSDHG 171
Cdd:cd16028   244 IAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHG 276
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
139-172 1.34e-03

N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.


Pssm-ID: 293751 [Multi-domain]  Cd Length: 373  Bit Score: 40.57  E-value: 1.34e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1045559357 139 ISDVDHKLGYLIKMLKRAKLWNNVNLIVTSDHGM 172
Cdd:cd16027   195 IERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM 228
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
139-171 2.33e-03

choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.


Pssm-ID: 293756 [Multi-domain]  Cd Length: 327  Bit Score: 39.87  E-value: 2.33e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1045559357 139 ISDVDHKLGYLIKMLKRAKLWNNVNLIVTSDHG 171
Cdd:cd16032   170 VSYVDDKVGQLLDTLERTGLADDTIVIFTSDHG 202
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
139-171 2.57e-03

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 39.45  E-value: 2.57e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1045559357 139 ISDVDHKLGYLIKMLKRAKLWNNVNLIVTSDHG 171
Cdd:cd16148   169 VRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHG 201
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
122-173 1.00e-02

GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293748 [Multi-domain]  Cd Length: 274  Bit Score: 37.54  E-value: 1.00e-02
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045559357 122 DDTGHDVGPDSPLMG-------SVISDVDHKLgylikmlkRAKLWNNVNLIV-TSDHGMT 173
Cdd:cd16024   156 DHIGHLEGPKSPLMPpklkemdDVIKRIYESL--------EEQSSNNPTLLVvCGDHGMT 207
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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