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Conserved domains on  [gi|52076602|dbj|BAD45504|]
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phospholipase -like [Oryza sativa Japonica Group]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 581061)

alkaline phosphatase (ALP) family protein may catalyze the hydrolysis of substrates; the ALP superfamily includes alkaline phosphatases and sulfatases

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ALP_like super family cl23718
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
24-394 2.78e-97

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.


The actual alignment was detected with superfamily member pfam04185:

Pssm-ID: 474031  Cd Length: 348  Bit Score: 298.59  E-value: 2.78e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602    24 IKNVVVLALENRSFDHMLGWMQRLLGL-------PIDGLTGAECNPAPGPGPadSLLHCVSPDADLVVPDDPAHAFEDVL 96
Cdd:pfam04185   1 IKHVVIIMQENRSFDHYFGTLSGVRGFddpsplfQQDGVTKQALNPAGVSAP--YRLDTTFGPASGYVVPDPGHSWQAIH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602    97 EQLLGFRpndstgaaaspsdMSGFVRSAVSvsalltDAVMRGFTPSRLPAFSALASSFAVFDRWFSSIPGPTQPNRLFLY 176
Cdd:pfam04185  79 EQWNGGR-------------MDGFVAAAGS------TQVMGYFDRQDIPFLWLLAQEFTLCDRYFCSVPGPTQPNRLYLV 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602   177 SATS----HGAVAHDKWN--LLRGYPQRTIFDSLAADALDYRVYF------KTIPTTLFYRRLRTVANAARGtFRRYD-- 242
Cdd:pfam04185 140 SGTSdpgsHGGPSLVDPNttPVKGFPWPTIPDRLSQAGISWGIYQeafldnHHQPFNYYVRKHNPLPSFRDA-LHQYGla 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602   243 ----AAFRDHARRGLLPALSVIEPRYfdltgtpADDDHPAHDVANGQRLVKDVYEALRAGPQWNHTLLIITYDEHGGFYD 318
Cdd:pfam04185 219 phyfSDFKKDVKNGKLPQVSWVIPNG-------ANDEHPGHDIAAGQKWIKNVLEALLSSPQWNKTLLIVTYDENGGFYD 291
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52076602   319 HVPPPNVGVPSpdaIRGPLpfffrfdRLGVRVPTIMVSPWIRKGTVVGRPpggptptseYEHSSIPATIKKIFNLS 394
Cdd:pfam04185 292 HVPPPKAPVPG---IPGPY-------GLGNRVPTLVISPWAKPGTVDHTT---------FDHTSVLRFIEKRFGLP 348
 
Name Accession Description Interval E-value
Phosphoesterase pfam04185
Phosphoesterase family; This family includes both bacterial phospholipase C enzymes EC:3.1.4.3, ...
24-394 2.78e-97

Phosphoesterase family; This family includes both bacterial phospholipase C enzymes EC:3.1.4.3, but also eukaryotic acid phosphatases EC:3.1.3.2.


Pssm-ID: 309350  Cd Length: 348  Bit Score: 298.59  E-value: 2.78e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602    24 IKNVVVLALENRSFDHMLGWMQRLLGL-------PIDGLTGAECNPAPGPGPadSLLHCVSPDADLVVPDDPAHAFEDVL 96
Cdd:pfam04185   1 IKHVVIIMQENRSFDHYFGTLSGVRGFddpsplfQQDGVTKQALNPAGVSAP--YRLDTTFGPASGYVVPDPGHSWQAIH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602    97 EQLLGFRpndstgaaaspsdMSGFVRSAVSvsalltDAVMRGFTPSRLPAFSALASSFAVFDRWFSSIPGPTQPNRLFLY 176
Cdd:pfam04185  79 EQWNGGR-------------MDGFVAAAGS------TQVMGYFDRQDIPFLWLLAQEFTLCDRYFCSVPGPTQPNRLYLV 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602   177 SATS----HGAVAHDKWN--LLRGYPQRTIFDSLAADALDYRVYF------KTIPTTLFYRRLRTVANAARGtFRRYD-- 242
Cdd:pfam04185 140 SGTSdpgsHGGPSLVDPNttPVKGFPWPTIPDRLSQAGISWGIYQeafldnHHQPFNYYVRKHNPLPSFRDA-LHQYGla 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602   243 ----AAFRDHARRGLLPALSVIEPRYfdltgtpADDDHPAHDVANGQRLVKDVYEALRAGPQWNHTLLIITYDEHGGFYD 318
Cdd:pfam04185 219 phyfSDFKKDVKNGKLPQVSWVIPNG-------ANDEHPGHDIAAGQKWIKNVLEALLSSPQWNKTLLIVTYDENGGFYD 291
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52076602   319 HVPPPNVGVPSpdaIRGPLpfffrfdRLGVRVPTIMVSPWIRKGTVVGRPpggptptseYEHSSIPATIKKIFNLS 394
Cdd:pfam04185 292 HVPPPKAPVPG---IPGPY-------GLGNRVPTLVISPWAKPGTVDHTT---------FDHTSVLRFIEKRFGLP 348
AcpA cd16013
acid phosphatase A; Acid phosphatase A catalyzes the hydrolysis reaction via a phosphoseryl ...
22-395 2.61e-82

acid phosphatase A; Acid phosphatase A catalyzes the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at low pH. AcpA hydrolyzes a variety of substrates, including p-nitrophenylphosphate (pNPP), p-nitrophenylphosphorylcholine (pNPPC), peptides containing phosphotyrosine, inositol phosphates, AMP, ATP, fructose 1,6-bisphosphate, glucose and fructose 6-phosphates, NADP, and ribose 5-phosphate. AcpA is distinct from histidine ACPs and purple ACPs, as well as class A, B, and C bacterial nonspecific ACPs.


Pssm-ID: 293737  Cd Length: 370  Bit Score: 260.69  E-value: 2.61e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602  22 SKIKNVVVLALENRSFDHMLGWMQRLLGLPIDGLTGAECNPAPGPGPADSLL----------HCVSPDADLVVPDDPAHA 91
Cdd:cd16013   1 TPIKHVVVIMQENRSFDNYFGTYPGANGPPGANLFSAGPGTNLGIPPGPDSDpltglpnnpfRLDRTVGLGAVTPDPVHR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602  92 FEDVLEQLLGfrpndstGAaaspsdMSGFVrsAVSVSALLTDA-VMRGFTPSRLPAFSALASSFAVFDRWFSSIPGPTQP 170
Cdd:cd16013  81 FYQEQQQING-------GK------MDGFV--AGSGGTTGDGGqVMGYYDGNDLPFLWDLAQEYTLADNFFASVFGGTFP 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 171 NRLFLYSATSHGAVAHDKW--------------NLLRGYPQRTIFDSLAADALDYRVYFKTIPTTLFYRRLRT------V 230
Cdd:cd16013 146 NRLYLIAAQSPGFTNAGPSsaapldplddtastPPLPPQTQPTIGDRLSAAGVSWGWYSGGWNPALAGAPKSTfpfpyfF 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 231 ANAARGTFRR---YDAA-FRDHARRGLLPALSVIEPRYFDltgtpadDDHPA-HDVANGQRLVKDVYEALRAGPQWNHTL 305
Cdd:cd16013 226 FTFIGTTAGAnhlKDLTdFYADAKAGTLPAVSFVKPSGLN-------DGHPGySDVLAGQAFLADVINALQKSPQWNSTA 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 306 LIITYDEHGGFYDHVPPPNVGVPSPDairgplpfffrFDRLGVRVPTIMVSPWIRKGTVVGrppggptptSEYEHSSIPA 385
Cdd:cd16013 299 IIITYDEHGGFYDHVPPPKADAPDPG-----------RWGPGFRVPAIVISPYAKRGYVDH---------TVYDHTSILK 358
                       410
                ....*....|
gi 52076602 386 TIKKIFNLSS 395
Cdd:cd16013 359 FIEDRWGLPP 368
PlcC COG3511
Phospholipase C [Cell wall/membrane/envelope biogenesis];
15-412 2.16e-69

Phospholipase C [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442734  Cd Length: 392  Bit Score: 227.80  E-value: 2.16e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602  15 APNSNGDSKIKNVVVLALENRSFDHMLGWM--------QRLLGLPiDGLTGAECNPAPGPGPADSLLHCVSPDADLVVPD 86
Cdd:COG3511   1 ANRTGTLTDIKHVVVLMQENRSFDHYFGTLpgvrgfgdPNPIPQP-DGKPVFTQLPDPNGALPNLPFRLDTTQTNAQRTG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602  87 DPAHAFEDVLEQLLGFRpndstgaaaspsdMSGFVRSAVSVsalltDAVMRGFTPSRLPAFSALASSFAVFDRWFSSIPG 166
Cdd:COG3511  80 DLPHSWYDEQAAWNGGK-------------MDGFVAAKDAG-----GLTMGYYDRADLPFYYALADAFTLCDNYFCSVFG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 167 PTQPNRLFLYSATSHGAVAHDKWNL------------LRGYPQRTIFDSLAADALDYRVY------FKTIPTT---LFYR 225
Cdd:COG3511 142 GTTPNRLYLVSGTTPPYGNAGGPDVynvdadpssattLPPQTWTTIGDRLEAAGVSWKWYqggwdnALAGPHHnplQYFA 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 226 RLRTVANAARGTFRRYDAAFRDHARRGLLPALSVIEPRYfdltgtpADDDHPA-HDVANGQRLVKDVYEALRAGPQWNHT 304
Cdd:COG3511 222 QFANATPDRASHLYDRLDDFRADVAAGTLPAVSFIKPPG-------AYSEHPGySDPADGAAYIADVLDALTASPVWSKT 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 305 LLIITYDEHGGFYDHVPPPNVGVPSPDAIRGPLPFffrfdRLGVRVPTIMVSPWIRKGTVVgrppggptptSE-YEHSSI 383
Cdd:COG3511 295 AIIITYDENGGFFDHVPPPVPPSSTDGEGGDGDPY-----GLGPRVPMLVISPWAKGGWVD----------HTvFDHTSV 359
                       410       420
                ....*....|....*....|....*....
gi 52076602 384 PATIKKIFNLSSDFLTRRDAWAGTFEHLF 412
Cdd:COG3511 360 LRFIEKRFGLPELNIPWRRAVAGDLTSAF 388
 
Name Accession Description Interval E-value
Phosphoesterase pfam04185
Phosphoesterase family; This family includes both bacterial phospholipase C enzymes EC:3.1.4.3, ...
24-394 2.78e-97

Phosphoesterase family; This family includes both bacterial phospholipase C enzymes EC:3.1.4.3, but also eukaryotic acid phosphatases EC:3.1.3.2.


Pssm-ID: 309350  Cd Length: 348  Bit Score: 298.59  E-value: 2.78e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602    24 IKNVVVLALENRSFDHMLGWMQRLLGL-------PIDGLTGAECNPAPGPGPadSLLHCVSPDADLVVPDDPAHAFEDVL 96
Cdd:pfam04185   1 IKHVVIIMQENRSFDHYFGTLSGVRGFddpsplfQQDGVTKQALNPAGVSAP--YRLDTTFGPASGYVVPDPGHSWQAIH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602    97 EQLLGFRpndstgaaaspsdMSGFVRSAVSvsalltDAVMRGFTPSRLPAFSALASSFAVFDRWFSSIPGPTQPNRLFLY 176
Cdd:pfam04185  79 EQWNGGR-------------MDGFVAAAGS------TQVMGYFDRQDIPFLWLLAQEFTLCDRYFCSVPGPTQPNRLYLV 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602   177 SATS----HGAVAHDKWN--LLRGYPQRTIFDSLAADALDYRVYF------KTIPTTLFYRRLRTVANAARGtFRRYD-- 242
Cdd:pfam04185 140 SGTSdpgsHGGPSLVDPNttPVKGFPWPTIPDRLSQAGISWGIYQeafldnHHQPFNYYVRKHNPLPSFRDA-LHQYGla 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602   243 ----AAFRDHARRGLLPALSVIEPRYfdltgtpADDDHPAHDVANGQRLVKDVYEALRAGPQWNHTLLIITYDEHGGFYD 318
Cdd:pfam04185 219 phyfSDFKKDVKNGKLPQVSWVIPNG-------ANDEHPGHDIAAGQKWIKNVLEALLSSPQWNKTLLIVTYDENGGFYD 291
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52076602   319 HVPPPNVGVPSpdaIRGPLpfffrfdRLGVRVPTIMVSPWIRKGTVVGRPpggptptseYEHSSIPATIKKIFNLS 394
Cdd:pfam04185 292 HVPPPKAPVPG---IPGPY-------GLGNRVPTLVISPWAKPGTVDHTT---------FDHTSVLRFIEKRFGLP 348
AcpA cd16013
acid phosphatase A; Acid phosphatase A catalyzes the hydrolysis reaction via a phosphoseryl ...
22-395 2.61e-82

acid phosphatase A; Acid phosphatase A catalyzes the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at low pH. AcpA hydrolyzes a variety of substrates, including p-nitrophenylphosphate (pNPP), p-nitrophenylphosphorylcholine (pNPPC), peptides containing phosphotyrosine, inositol phosphates, AMP, ATP, fructose 1,6-bisphosphate, glucose and fructose 6-phosphates, NADP, and ribose 5-phosphate. AcpA is distinct from histidine ACPs and purple ACPs, as well as class A, B, and C bacterial nonspecific ACPs.


Pssm-ID: 293737  Cd Length: 370  Bit Score: 260.69  E-value: 2.61e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602  22 SKIKNVVVLALENRSFDHMLGWMQRLLGLPIDGLTGAECNPAPGPGPADSLL----------HCVSPDADLVVPDDPAHA 91
Cdd:cd16013   1 TPIKHVVVIMQENRSFDNYFGTYPGANGPPGANLFSAGPGTNLGIPPGPDSDpltglpnnpfRLDRTVGLGAVTPDPVHR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602  92 FEDVLEQLLGfrpndstGAaaspsdMSGFVrsAVSVSALLTDA-VMRGFTPSRLPAFSALASSFAVFDRWFSSIPGPTQP 170
Cdd:cd16013  81 FYQEQQQING-------GK------MDGFV--AGSGGTTGDGGqVMGYYDGNDLPFLWDLAQEYTLADNFFASVFGGTFP 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 171 NRLFLYSATSHGAVAHDKW--------------NLLRGYPQRTIFDSLAADALDYRVYFKTIPTTLFYRRLRT------V 230
Cdd:cd16013 146 NRLYLIAAQSPGFTNAGPSsaapldplddtastPPLPPQTQPTIGDRLSAAGVSWGWYSGGWNPALAGAPKSTfpfpyfF 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 231 ANAARGTFRR---YDAA-FRDHARRGLLPALSVIEPRYFDltgtpadDDHPA-HDVANGQRLVKDVYEALRAGPQWNHTL 305
Cdd:cd16013 226 FTFIGTTAGAnhlKDLTdFYADAKAGTLPAVSFVKPSGLN-------DGHPGySDVLAGQAFLADVINALQKSPQWNSTA 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 306 LIITYDEHGGFYDHVPPPNVGVPSPDairgplpfffrFDRLGVRVPTIMVSPWIRKGTVVGrppggptptSEYEHSSIPA 385
Cdd:cd16013 299 IIITYDEHGGFYDHVPPPKADAPDPG-----------RWGPGFRVPAIVISPYAKRGYVDH---------TVYDHTSILK 358
                       410
                ....*....|
gi 52076602 386 TIKKIFNLSS 395
Cdd:cd16013 359 FIEDRWGLPP 368
PlcC COG3511
Phospholipase C [Cell wall/membrane/envelope biogenesis];
15-412 2.16e-69

Phospholipase C [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442734  Cd Length: 392  Bit Score: 227.80  E-value: 2.16e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602  15 APNSNGDSKIKNVVVLALENRSFDHMLGWM--------QRLLGLPiDGLTGAECNPAPGPGPADSLLHCVSPDADLVVPD 86
Cdd:COG3511   1 ANRTGTLTDIKHVVVLMQENRSFDHYFGTLpgvrgfgdPNPIPQP-DGKPVFTQLPDPNGALPNLPFRLDTTQTNAQRTG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602  87 DPAHAFEDVLEQLLGFRpndstgaaaspsdMSGFVRSAVSVsalltDAVMRGFTPSRLPAFSALASSFAVFDRWFSSIPG 166
Cdd:COG3511  80 DLPHSWYDEQAAWNGGK-------------MDGFVAAKDAG-----GLTMGYYDRADLPFYYALADAFTLCDNYFCSVFG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 167 PTQPNRLFLYSATSHGAVAHDKWNL------------LRGYPQRTIFDSLAADALDYRVY------FKTIPTT---LFYR 225
Cdd:COG3511 142 GTTPNRLYLVSGTTPPYGNAGGPDVynvdadpssattLPPQTWTTIGDRLEAAGVSWKWYqggwdnALAGPHHnplQYFA 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 226 RLRTVANAARGTFRRYDAAFRDHARRGLLPALSVIEPRYfdltgtpADDDHPA-HDVANGQRLVKDVYEALRAGPQWNHT 304
Cdd:COG3511 222 QFANATPDRASHLYDRLDDFRADVAAGTLPAVSFIKPPG-------AYSEHPGySDPADGAAYIADVLDALTASPVWSKT 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 305 LLIITYDEHGGFYDHVPPPNVGVPSPDAIRGPLPFffrfdRLGVRVPTIMVSPWIRKGTVVgrppggptptSE-YEHSSI 383
Cdd:COG3511 295 AIIITYDENGGFFDHVPPPVPPSSTDGEGGDGDPY-----GLGPRVPMLVISPWAKGGWVD----------HTvFDHTSV 359
                       410       420
                ....*....|....*....|....*....
gi 52076602 384 PATIKKIFNLSSDFLTRRDAWAGTFEHLF 412
Cdd:COG3511 360 LRFIEKRFGLPELNIPWRRAVAGDLTSAF 388
PLC cd16014
non-hemolytic phospholipase C; Nonhemolytic Phospholipases C is produced by pathogenic ...
24-364 2.32e-37

non-hemolytic phospholipase C; Nonhemolytic Phospholipases C is produced by pathogenic bacterial. The toxic phospholipases C can interact with eukaryotic cell membranes and hydrolyze phosphatidylcholine and sphingomyelin, leading to cell lysis.


Pssm-ID: 293738  Cd Length: 287  Bit Score: 139.32  E-value: 2.32e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602  24 IKNVVVLALENRSFDHMLGWMQRLLGLpidgltgaecnpapgpgpADSllhcvspdadlvvpddpaHAFEDVLEQLLGFR 103
Cdd:cd16014   1 IEHVVIFMQENRSFDHYFGTLAGVRGF------------------NDS------------------NSWNNNHAAWNGGL 44
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 104 pNDSTGAAASPSDMsGFvrsavsvsalltdavmrgFTPSRLPAFSALASSFAVFDRWFSSIPGPTQPNRLFLYSATSHGA 183
Cdd:cd16014  45 -NDNWILAKTPYSM-GY------------------FTREDIPFHYALADAFTICDMYHCSVLGSTDPNRLYLWSGTIDPP 104
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 184 VAHdkwnllrGYPQRTIFDslAADALDYRVY-FKTIPTTLfyrrlrtvaNAARGTFRRYD--AAFRDHARRGLLPALSVI 260
Cdd:cd16014 105 GGN-------GGPQATPGP--ATNNLDCFPLtWTTYPEYL---------EDAGVSWRVYQdlDAFKADAANGTLPQVSWI 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 261 EPRYfdltgtpADDDHPAHDVANGQRLVKDVYEALRAGPQ-WNHTLLIITYDEHGGFYDHVPPPNvgVPSPDAIRGPLPF 339
Cdd:cd16014 167 VAPQ-------ELSEHPPNTPADGAWLVKQVLDALASSPDvWNKTVFIINYDENGGFFDHVTPPV--PPPGTAGEWLTPP 237
                       330       340
                ....*....|....*....|....*....
gi 52076602 340 FFRFDR----LGVRVPTIMVSPWIRKGTV 364
Cdd:cd16014 238 YETGGGtpigLGFRVPMLVISPWSRGGNV 266
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
143-391 2.26e-06

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: 48.96  E-value: 2.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 143 RLPAFSALASSFAVFDRWFSSIPGPTQPNRLFLysATSHGAVAHDkwnlLRGYPQRTIFDSLAADALDYRVYfkTIPTTL 222
Cdd:cd00016  25 TTPNLKRLASEGATFNFRSVSPPTSSAPNHAAL--LTGAYPTLHG----YTGNGSADPELPSRAAGKDEDGP--TIPELL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 223 fyrrlrtvaNAARGTFRRYdaAFRDHARRGLL--PALSVIEPRYFDLTGTPADDDHPAHDvANGQRL---VKDVYEALRA 297
Cdd:cd00016  97 ---------KQAGYRTGVI--GLLKAIDETSKekPFVLFLHFDGPDGPGHAYGPNTPEYY-DAVEEIderIGKVLDALKK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076602 298 GPQWNHTLLIITYDEHGGFYDHVPPPNvgvpspdairgPLPFFFRFDrLGVRVPTIMVSPWIRKGTVVGRPpggptptse 377
Cdd:cd00016 165 AGDADDTVIIVTADHGGIDKGHGGDPK-----------ADGKADKSH-TGMRVPFIAYGPGVKKGGVKHEL--------- 223
                       250
                ....*....|....
gi 52076602 378 YEHSSIPATIKKIF 391
Cdd:cd00016 224 ISQYDIAPTLADLL 237
 
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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