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Conserved domains on  [gi|1248065062|ref|WP_096569003|]
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MULTISPECIES: alkaline phosphatase family protein [Campylobacter]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 11445914)

alkaline phosphatase family protein catalyzes the hydrolysis of phosphate monoesters or diesters, similar to ectonucleotide pyrophosphatases/phosphodiesterases (ENPPs), which hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates

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

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
2-255 1.46e-38

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


:

Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 138.34  E-value: 1.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062   2 MSKVILVVLDGLNYKS-ASINMGYLNALCKENLgKFYSLECELPSMSRPLYECLLTGVKPVLSGIINN------------ 68
Cdd:COG1524    23 AKKVVLILVDGLRADLlERAHAPNLAALAARGV-YARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNgwydpelgrvvn 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062  69 KLSFS----------KQASIFDLCKEQGLKagCAAYHWVFelYNKKEFIpflhrhiedeNLTLPY---GHFYYEDDY-LD 134
Cdd:COG1524   102 SLSWVedgfgsnsllPVPTIFERARAAGLT--TAAVFWPS--FEGSGLI----------DAARPYpydGRKPLLGNPaAD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062 135 SHLFADGEHLRNKYDLDFTLIHSMNIDDTGHKFGSHSCEYANKTKKVDTLISEyLLIWLE-----QGINVIITSDHGMTE 209
Cdd:COG1524   168 RWIAAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGR-LLDALKarglyEGTLVIVTADHGMVD 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062 210 GK------------------------------------------------------------------------------ 211
Cdd:COG1524   247 VPpdidlnrlrlagllavragesahlylkdgadaevrallglparvltreelaaghfgphrigdlvlvakpgwaldaplk 326
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1248065062 212 -SHGGLSEDEILVPFFTFGSAFsyeNAKIKQDEICGSVCEILGLK 255
Cdd:COG1524   327 gSHGGLPDEEMRVPLLASGPGF---RPGVRNVDVAPTIARLLGLP 368
 
Name Accession Description Interval E-value
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
2-255 1.46e-38

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 138.34  E-value: 1.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062   2 MSKVILVVLDGLNYKS-ASINMGYLNALCKENLgKFYSLECELPSMSRPLYECLLTGVKPVLSGIINN------------ 68
Cdd:COG1524    23 AKKVVLILVDGLRADLlERAHAPNLAALAARGV-YARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNgwydpelgrvvn 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062  69 KLSFS----------KQASIFDLCKEQGLKagCAAYHWVFelYNKKEFIpflhrhiedeNLTLPY---GHFYYEDDY-LD 134
Cdd:COG1524   102 SLSWVedgfgsnsllPVPTIFERARAAGLT--TAAVFWPS--FEGSGLI----------DAARPYpydGRKPLLGNPaAD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062 135 SHLFADGEHLRNKYDLDFTLIHSMNIDDTGHKFGSHSCEYANKTKKVDTLISEyLLIWLE-----QGINVIITSDHGMTE 209
Cdd:COG1524   168 RWIAAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGR-LLDALKarglyEGTLVIVTADHGMVD 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062 210 GK------------------------------------------------------------------------------ 211
Cdd:COG1524   247 VPpdidlnrlrlagllavragesahlylkdgadaevrallglparvltreelaaghfgphrigdlvlvakpgwaldaplk 326
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1248065062 212 -SHGGLSEDEILVPFFTFGSAFsyeNAKIKQDEICGSVCEILGLK 255
Cdd:COG1524   327 gSHGGLPDEEMRVPLLASGPGF---RPGVRNVDVAPTIARLLGLP 368
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
3-253 6.89e-21

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: 88.80  E-value: 6.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062   3 SKVILVVLDGL--NYKSASINMGYLNALcKENLGKFYSLECELPSMSRPLYECLLTGVKPVLSGIINN-------KLSFS 73
Cdd:cd16018     1 PPLIVISIDGFrwDYLDRAGLTPNLKRL-AEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNyfydpktNEEFS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062  74 KQAS-----------IFDLCKEQGLKagCAAYHW-VFElynkkefipflhRHIEDENLTlPYGHFYYEDDYLDSHLFAD- 140
Cdd:cd16018    80 DSDWvwdpwwiggepIWVTAEKAGLK--TASYFWpGSE------------VAIIGYNPT-PIPLGGYWQPYNDSFPFEEr 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062 141 ---GEHLRNKYDLDFTLIHSMNIDDTGHKFGSHSCEYANKTKKVDTLISeYLLIWLEQ-----GINVIITSDHGMTEGKS 212
Cdd:cd16018   145 vdtILEWLDLERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLG-YLIEALKErglldDTNIIVVSDHGMTDVGT 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1248065062 213 HGGLSED-EILVPFFTFGSAFS--YENAKIKQDEICGSVCEILG 253
Cdd:cd16018   224 HGYDNELpDMRAIFIARGPAFKkgKKLGPFRNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
5-222 1.84e-15

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: 74.77  E-value: 1.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062   5 VILVVLDGLNYKsasinmgYLNALCKE-NLGKFYS-------LECELPSMSRPLYECLLTGVKPVLSGIINN-------- 68
Cdd:pfam01663   1 LLVISLDGFRAD-------YLDRFELTpNLAALAKegvsapnLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNtfydpktg 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062  69 -KLSFSKQAS----------IFDLCKEQGLKAgcAAYHWvfelynkkefiPFLHRHIEDENLTLPyghFYYEDDY----- 132
Cdd:pfam01663  74 eYLVFVISDPedprwwqgepIWDTAAKAGVRA--AALFW-----------PGSEVDYSTYYGTPP---RYLKDDYnnsvp 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062 133 ----LDSHLFADGEHLRNKYDL----DFTLIHSMNIDDTGHKFGSHSCEYANKTKKVDTLIsEYLLIWLEQ-----GINV 199
Cdd:pfam01663 138 fedrVDTAVLQTWLDLPFADVAaerpDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAI-GDLLEALDErglfeDTNV 216
                         250       260
                  ....*....|....*....|...
gi 1248065062 200 IITSDHGMTEGKSHGGLSEDEIL 222
Cdd:pfam01663 217 IVVSDHGMTPVSDDKVIFLNDYL 239
 
Name Accession Description Interval E-value
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
2-255 1.46e-38

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 138.34  E-value: 1.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062   2 MSKVILVVLDGLNYKS-ASINMGYLNALCKENLgKFYSLECELPSMSRPLYECLLTGVKPVLSGIINN------------ 68
Cdd:COG1524    23 AKKVVLILVDGLRADLlERAHAPNLAALAARGV-YARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNgwydpelgrvvn 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062  69 KLSFS----------KQASIFDLCKEQGLKagCAAYHWVFelYNKKEFIpflhrhiedeNLTLPY---GHFYYEDDY-LD 134
Cdd:COG1524   102 SLSWVedgfgsnsllPVPTIFERARAAGLT--TAAVFWPS--FEGSGLI----------DAARPYpydGRKPLLGNPaAD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062 135 SHLFADGEHLRNKYDLDFTLIHSMNIDDTGHKFGSHSCEYANKTKKVDTLISEyLLIWLE-----QGINVIITSDHGMTE 209
Cdd:COG1524   168 RWIAAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGR-LLDALKarglyEGTLVIVTADHGMVD 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062 210 GK------------------------------------------------------------------------------ 211
Cdd:COG1524   247 VPpdidlnrlrlagllavragesahlylkdgadaevrallglparvltreelaaghfgphrigdlvlvakpgwaldaplk 326
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1248065062 212 -SHGGLSEDEILVPFFTFGSAFsyeNAKIKQDEICGSVCEILGLK 255
Cdd:COG1524   327 gSHGGLPDEEMRVPLLASGPGF---RPGVRNVDVAPTIARLLGLP 368
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
3-253 6.89e-21

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: 88.80  E-value: 6.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062   3 SKVILVVLDGL--NYKSASINMGYLNALcKENLGKFYSLECELPSMSRPLYECLLTGVKPVLSGIINN-------KLSFS 73
Cdd:cd16018     1 PPLIVISIDGFrwDYLDRAGLTPNLKRL-AEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNyfydpktNEEFS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062  74 KQAS-----------IFDLCKEQGLKagCAAYHW-VFElynkkefipflhRHIEDENLTlPYGHFYYEDDYLDSHLFAD- 140
Cdd:cd16018    80 DSDWvwdpwwiggepIWVTAEKAGLK--TASYFWpGSE------------VAIIGYNPT-PIPLGGYWQPYNDSFPFEEr 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062 141 ---GEHLRNKYDLDFTLIHSMNIDDTGHKFGSHSCEYANKTKKVDTLISeYLLIWLEQ-----GINVIITSDHGMTEGKS 212
Cdd:cd16018   145 vdtILEWLDLERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLG-YLIEALKErglldDTNIIVVSDHGMTDVGT 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1248065062 213 HGGLSED-EILVPFFTFGSAFS--YENAKIKQDEICGSVCEILG 253
Cdd:cd16018   224 HGYDNELpDMRAIFIARGPAFKkgKKLGPFRNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
5-222 1.84e-15

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: 74.77  E-value: 1.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062   5 VILVVLDGLNYKsasinmgYLNALCKE-NLGKFYS-------LECELPSMSRPLYECLLTGVKPVLSGIINN-------- 68
Cdd:pfam01663   1 LLVISLDGFRAD-------YLDRFELTpNLAALAKegvsapnLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNtfydpktg 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062  69 -KLSFSKQAS----------IFDLCKEQGLKAgcAAYHWvfelynkkefiPFLHRHIEDENLTLPyghFYYEDDY----- 132
Cdd:pfam01663  74 eYLVFVISDPedprwwqgepIWDTAAKAGVRA--AALFW-----------PGSEVDYSTYYGTPP---RYLKDDYnnsvp 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062 133 ----LDSHLFADGEHLRNKYDL----DFTLIHSMNIDDTGHKFGSHSCEYANKTKKVDTLIsEYLLIWLEQ-----GINV 199
Cdd:pfam01663 138 fedrVDTAVLQTWLDLPFADVAaerpDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAI-GDLLEALDErglfeDTNV 216
                         250       260
                  ....*....|....*....|...
gi 1248065062 200 IITSDHGMTEGKSHGGLSEDEIL 222
Cdd:pfam01663 217 IVVSDHGMTPVSDDKVIFLNDYL 239
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
3-226 1.81e-13

GPI ethanolamine phosphate transferase; 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: 293743 [Multi-domain]  Cd Length: 292  Bit Score: 68.93  E-value: 1.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062   3 SKVILVVLDGLNYKSA------SINMGYLNAL--CKENLGKFYSLeCELPSMSRPLYECLLTGVKPVLSGIINNKLSFS- 73
Cdd:cd16019     5 DKVVLIVIDGLRYDLAvnvnkqSSFFSFLQKLneQPNNSFLALSF-ADPPTVTGPRLKALTTGNPPTFLDLISNFASSEi 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062  74 KQASIFDLCKEQGLKAGCAAYHWVFELYNKKEFIPFLHRHIEDenltlpyGHFYYEDDYLDSHLFADGEHLRNKYDLDFT 153
Cdd:cd16019    84 KEDNIIRQLKKNGKKILFYGDDTWLDLFPEIFTYKFTITSFNI-------RDMHDVDPIFYNHINDNLDENIYYDNWDFI 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1248065062 154 LIHSMNIDDTGHKFG-SHSCEYANKTKKVDTLIseYLLIwleQGIN----VIITSDHGMTEGKSHGGLSEDEILVPFF 226
Cdd:cd16019   157 ILHFLGLDHLGHKHNtTSSPELEKKLDQMDNLI--RDIY---DRMDndtlLVVVSDHGMNNDGNHGGSSTEETSSFFF 229
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
155-242 6.48e-13

GPI ethanolamine phosphate transferase 1; PIG-N; 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: 293744  Cd Length: 294  Bit Score: 67.23  E-value: 6.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062 155 IHSMNIDDTGHKFGSHSCEYANKTKKVDTLISEylliwLEQGINV---------IITSDHGMTEGKSHGGLSEDEILVPF 225
Cdd:cd16020   162 LHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEK-----TYPLIEEyfndgrtayIFTSDHGMTDWGSHGDGSPDETETPF 236
                          90
                  ....*....|....*..
gi 1248065062 226 FTFGSAFSYENAKIKQD 242
Cdd:cd16020   237 IAWGAGIKHPTPGRGPS 253
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
3-233 1.87e-11

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: 62.58  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062   3 SKVILVVLDGLNY---KSASINMGYLNALCKENLGKFYSLECELPSMSRPLYECLLTGVKPV-LSGIINNKLSFSKQASI 78
Cdd:cd16024     5 DKLVFMVIDALRAdfvFGPDSNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSfLDVVLNFASSLLEEDNW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062  79 FDLCKEQGLKAgcaayhwVFelYNkkefipflhrhieDEN-LTLPYGHF-------------YYEDDY-----LDSHLFA 139
Cdd:cd16024    85 LSQLKAAGKKI-------VF--YG-------------DDTwLKLFPGSFtrsdgttsffvsdFTEVDNnvtrhLDSELSR 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062 140 DgehlrnkyDLDFTLIHSMNIDDTGHKFGSHSCEYANKTKKVDTLISEYLLIWLEQGIN----VIITSDHGMTEGKSHGG 215
Cdd:cd16024   143 D--------DWDVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQSSNnptlLVVCGDHGMTDAGNHGG 214
                         250
                  ....*....|....*...
gi 1248065062 216 LSEDEILVPFFTFGSAFS 233
Cdd:cd16024   215 SSPGETSVPLLFISPKFS 232
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
5-226 2.51e-11

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: 62.05  E-value: 2.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062   5 VILVVLDGL------NYKSASINMGYLNALcKENLGKFYSLECELPSMSRPLYECLLTGVKPVLSGIINNKLSFS----- 73
Cdd:cd00016     3 VVLIVLDGLgaddlgKAGNPAPTTPNLKRL-ASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPelpsr 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062  74 ------KQASIFDLCKEQGLKAGCAAyhwvfelynkkefipfLHRHIEDENLTLPyghfyyeddyldshlfadgehlrnk 147
Cdd:cd00016    82 aagkdeDGPTIPELLKQAGYRTGVIG----------------LLKAIDETSKEKP------------------------- 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062 148 ydlDFTLIHSMNIDDTGHKFGSHSCEYANKTKKVDTLISEYLLIWLEQGI----NVIITSDHGMtEGKSHGGL------- 216
Cdd:cd00016   121 ---FVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDaddtVIIVTADHGG-IDKGHGGDpkadgka 196
                         250
                  ....*....|..
gi 1248065062 217 --SEDEILVPFF 226
Cdd:cd00016   197 dkSHTGMRVPFI 208
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
130-221 3.47e-09

GPI ethanolamine phosphate transferase 3, PIG-O; 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: 293747  Cd Length: 289  Bit Score: 56.41  E-value: 3.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062 130 DDYLDSHLFadgEHLRNKYDLDFTLIHSMNIDDTGHKFGSHSCEYANKTKKVDTLISEyLLIWLEQGINVIITSDHGMTE 209
Cdd:cd16023   143 DNGVLKHLF---PELQSEDDWDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRD-IIERLDDDTLLLVFGDHGMTE 218
                          90
                  ....*....|..
gi 1248065062 210 GKSHGGLSEDEI 221
Cdd:cd16023   219 TGDHGGDSDEEV 230
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
4-226 4.57e-04

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: 40.61  E-value: 4.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062   4 KVILVVLDGLN------YKSASINMGYLNALCKENLG--KFYSlecelPSMS-RPLYECLLTGVKPVLSGIINNKLSfSK 74
Cdd:cd16148     2 NVILIVIDSLRadhlgcYGYDRVTTPNLDRLAAEGVVfdNHYS-----GSNPtLPSRFSLFTGLYPFYHGVWGGPLE-PD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062  75 QASIFDLCKEQGLKAGCAAYH-WVFELYNkkefipFLHRHIEDENLTLPYGHFYYEDDYLDSHLFADGEHL--RNKYDLD 151
Cdd:cd16148    76 DPTLAEILRKAGYYTAAVSSNpHLFGGPG------FDRGFDTFEDFRGQEGDPGEEGDERAERVTDRALEWldRNADDDP 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065062 152 FTL-IHSMnidDTgHkfgsHSCEYANKTKKVDTLISEyLLIWL-EQGI----NVIITSDHG--MTE----GKSHGGLSED 219
Cdd:cd16148   150 FFLfLHYF---DP-H----EPYLYDAEVRYVDEQIGR-LLDKLkELGLledtLVIVTSDHGeeFGEhglyWGHGSNLYDE 220

                  ....*..
gi 1248065062 220 EILVPFF 226
Cdd:cd16148   221 QLHVPLI 227
 
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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