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Conserved domains on  [gi|1002227803|ref|XP_015633975|]
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non-specific phospholipase C6 [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 ...
43-413 1.88e-96

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: 297.05  E-value: 1.88e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803  43 IKNVVVLALENRSFDHMLGWMQRLLGL-------PIDGLTGAECNPAPGPGPadSLLHCVSPDADLVVPDDPAHAFEDVL 115
Cdd:pfam04185   1 IKHVVIIMQENRSFDHYFGTLSGVRGFddpsplfQQDGVTKQALNPAGVSAP--YRLDTTFGPASGYVVPDPGHSWQAIH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 116 EQLLGFRpndstgaaaspsdMSGFVRSAVSvsalltDAVMRGFTPSRLPAFSALASSFAVFDRWFSSIPGPTQPNRLFLY 195
Cdd:pfam04185  79 EQWNGGR-------------MDGFVAAAGS------TQVMGYFDRQDIPFLWLLAQEFTLCDRYFCSVPGPTQPNRLYLV 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 196 SATS----HGAVAHDKWN--LLRGYPQRTIFDSLAADALDYRVYF------KTIPTTLFYRRLRTVANAARGtFRRYD-- 261
Cdd:pfam04185 140 SGTSdpgsHGGPSLVDPNttPVKGFPWPTIPDRLSQAGISWGIYQeafldnHHQPFNYYVRKHNPLPSFRDA-LHQYGla 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 262 ----AAFRDHARRGLLPALSVIEPRYfdltgtpADDDHPAHDVANGQRLVKDVYEALRAGPQWNHTLLIITYDEHGGFYD 337
Cdd:pfam04185 219 phyfSDFKKDVKNGKLPQVSWVIPNG-------ANDEHPGHDIAAGQKWIKNVLEALLSSPQWNKTLLIVTYDENGGFYD 291
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002227803 338 HVPPPNVGVPSpdaIRGPLpfffrfdRLGVRVPTIMVSPWIRKGTVVGRPpggptptseYEHSSIPATIKKIFNLS 413
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, ...
43-413 1.88e-96

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: 297.05  E-value: 1.88e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803  43 IKNVVVLALENRSFDHMLGWMQRLLGL-------PIDGLTGAECNPAPGPGPadSLLHCVSPDADLVVPDDPAHAFEDVL 115
Cdd:pfam04185   1 IKHVVIIMQENRSFDHYFGTLSGVRGFddpsplfQQDGVTKQALNPAGVSAP--YRLDTTFGPASGYVVPDPGHSWQAIH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 116 EQLLGFRpndstgaaaspsdMSGFVRSAVSvsalltDAVMRGFTPSRLPAFSALASSFAVFDRWFSSIPGPTQPNRLFLY 195
Cdd:pfam04185  79 EQWNGGR-------------MDGFVAAAGS------TQVMGYFDRQDIPFLWLLAQEFTLCDRYFCSVPGPTQPNRLYLV 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 196 SATS----HGAVAHDKWN--LLRGYPQRTIFDSLAADALDYRVYF------KTIPTTLFYRRLRTVANAARGtFRRYD-- 261
Cdd:pfam04185 140 SGTSdpgsHGGPSLVDPNttPVKGFPWPTIPDRLSQAGISWGIYQeafldnHHQPFNYYVRKHNPLPSFRDA-LHQYGla 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 262 ----AAFRDHARRGLLPALSVIEPRYfdltgtpADDDHPAHDVANGQRLVKDVYEALRAGPQWNHTLLIITYDEHGGFYD 337
Cdd:pfam04185 219 phyfSDFKKDVKNGKLPQVSWVIPNG-------ANDEHPGHDIAAGQKWIKNVLEALLSSPQWNKTLLIVTYDENGGFYD 291
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002227803 338 HVPPPNVGVPSpdaIRGPLpfffrfdRLGVRVPTIMVSPWIRKGTVVGRPpggptptseYEHSSIPATIKKIFNLS 413
Cdd:pfam04185 292 HVPPPKAPVPG---IPGPY-------GLGNRVPTLVISPWAKPGTVDHTT---------FDHTSVLRFIEKRFGLP 348
AcpA cd16013
acid phosphatase A; Acid phosphatase A catalyzes the hydrolysis reaction via a phosphoseryl ...
41-414 9.89e-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: 259.53  E-value: 9.89e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803  41 SKIKNVVVLALENRSFDHMLGWMQRLLGLPIDGLTGAECNPAPGPGPADSLL----------HCVSPDADLVVPDDPAHA 110
Cdd:cd16013     1 TPIKHVVVIMQENRSFDNYFGTYPGANGPPGANLFSAGPGTNLGIPPGPDSDpltglpnnpfRLDRTVGLGAVTPDPVHR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 111 FEDVLEQLLGfrpndstGAaaspsdMSGFVrsAVSVSALLTDA-VMRGFTPSRLPAFSALASSFAVFDRWFSSIPGPTQP 189
Cdd:cd16013    81 FYQEQQQING-------GK------MDGFV--AGSGGTTGDGGqVMGYYDGNDLPFLWDLAQEYTLADNFFASVFGGTFP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 190 NRLFLYSATSHGAVAHDKW--------------NLLRGYPQRTIFDSLAADALDYRVYFKTIPTTLFYRRLRT------V 249
Cdd:cd16013   146 NRLYLIAAQSPGFTNAGPSsaapldplddtastPPLPPQTQPTIGDRLSAAGVSWGWYSGGWNPALAGAPKSTfpfpyfF 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 250 ANAARGTFRR---YDAA-FRDHARRGLLPALSVIEPRYFDltgtpadDDHPA-HDVANGQRLVKDVYEALRAGPQWNHTL 324
Cdd:cd16013   226 FTFIGTTAGAnhlKDLTdFYADAKAGTLPAVSFVKPSGLN-------DGHPGySDVLAGQAFLADVINALQKSPQWNSTA 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 325 LIITYDEHGGFYDHVPPPNVGVPSPDairgplpfffrFDRLGVRVPTIMVSPWIRKGTVVGrppggptptSEYEHSSIPA 404
Cdd:cd16013   299 IIITYDEHGGFYDHVPPPKADAPDPG-----------RWGPGFRVPAIVISPYAKRGYVDH---------TVYDHTSILK 358
                         410
                  ....*....|
gi 1002227803 405 TIKKIFNLSS 414
Cdd:cd16013   359 FIEDRWGLPP 368
PlcC COG3511
Phospholipase C [Cell wall/membrane/envelope biogenesis];
34-431 7.68e-69

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


Pssm-ID: 442734  Cd Length: 392  Bit Score: 226.65  E-value: 7.68e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803  34 APNSNGDSKIKNVVVLALENRSFDHMLGWM--------QRLLGLPiDGLTGAECNPAPGPGPADSLLHCVSPDADLVVPD 105
Cdd:COG3511     1 ANRTGTLTDIKHVVVLMQENRSFDHYFGTLpgvrgfgdPNPIPQP-DGKPVFTQLPDPNGALPNLPFRLDTTQTNAQRTG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 106 DPAHAFEDVLEQLLGFRpndstgaaaspsdMSGFVRSAVSVsalltDAVMRGFTPSRLPAFSALASSFAVFDRWFSSIPG 185
Cdd:COG3511    80 DLPHSWYDEQAAWNGGK-------------MDGFVAAKDAG-----GLTMGYYDRADLPFYYALADAFTLCDNYFCSVFG 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 186 PTQPNRLFLYSATSHGAVAHDKWNL------------LRGYPQRTIFDSLAADALDYRVY------FKTIPTT---LFYR 244
Cdd:COG3511   142 GTTPNRLYLVSGTTPPYGNAGGPDVynvdadpssattLPPQTWTTIGDRLEAAGVSWKWYqggwdnALAGPHHnplQYFA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 245 RLRTVANAARGTFRRYDAAFRDHARRGLLPALSVIEPRYfdltgtpADDDHPA-HDVANGQRLVKDVYEALRAGPQWNHT 323
Cdd:COG3511   222 QFANATPDRASHLYDRLDDFRADVAAGTLPAVSFIKPPG-------AYSEHPGySDPADGAAYIADVLDALTASPVWSKT 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 324 LLIITYDEHGGFYDHVPPPNVGVPSPDAIRGPLPFffrfdRLGVRVPTIMVSPWIRKGTVVgrppggptptSE-YEHSSI 402
Cdd:COG3511   295 AIIITYDENGGFFDHVPPPVPPSSTDGEGGDGDPY-----GLGPRVPMLVISPWAKGGWVD----------HTvFDHTSV 359
                         410       420
                  ....*....|....*....|....*....
gi 1002227803 403 PATIKKIFNLSSDFLTRRDAWAGTFEHLF 431
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, ...
43-413 1.88e-96

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: 297.05  E-value: 1.88e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803  43 IKNVVVLALENRSFDHMLGWMQRLLGL-------PIDGLTGAECNPAPGPGPadSLLHCVSPDADLVVPDDPAHAFEDVL 115
Cdd:pfam04185   1 IKHVVIIMQENRSFDHYFGTLSGVRGFddpsplfQQDGVTKQALNPAGVSAP--YRLDTTFGPASGYVVPDPGHSWQAIH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 116 EQLLGFRpndstgaaaspsdMSGFVRSAVSvsalltDAVMRGFTPSRLPAFSALASSFAVFDRWFSSIPGPTQPNRLFLY 195
Cdd:pfam04185  79 EQWNGGR-------------MDGFVAAAGS------TQVMGYFDRQDIPFLWLLAQEFTLCDRYFCSVPGPTQPNRLYLV 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 196 SATS----HGAVAHDKWN--LLRGYPQRTIFDSLAADALDYRVYF------KTIPTTLFYRRLRTVANAARGtFRRYD-- 261
Cdd:pfam04185 140 SGTSdpgsHGGPSLVDPNttPVKGFPWPTIPDRLSQAGISWGIYQeafldnHHQPFNYYVRKHNPLPSFRDA-LHQYGla 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 262 ----AAFRDHARRGLLPALSVIEPRYfdltgtpADDDHPAHDVANGQRLVKDVYEALRAGPQWNHTLLIITYDEHGGFYD 337
Cdd:pfam04185 219 phyfSDFKKDVKNGKLPQVSWVIPNG-------ANDEHPGHDIAAGQKWIKNVLEALLSSPQWNKTLLIVTYDENGGFYD 291
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002227803 338 HVPPPNVGVPSpdaIRGPLpfffrfdRLGVRVPTIMVSPWIRKGTVVGRPpggptptseYEHSSIPATIKKIFNLS 413
Cdd:pfam04185 292 HVPPPKAPVPG---IPGPY-------GLGNRVPTLVISPWAKPGTVDHTT---------FDHTSVLRFIEKRFGLP 348
AcpA cd16013
acid phosphatase A; Acid phosphatase A catalyzes the hydrolysis reaction via a phosphoseryl ...
41-414 9.89e-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: 259.53  E-value: 9.89e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803  41 SKIKNVVVLALENRSFDHMLGWMQRLLGLPIDGLTGAECNPAPGPGPADSLL----------HCVSPDADLVVPDDPAHA 110
Cdd:cd16013     1 TPIKHVVVIMQENRSFDNYFGTYPGANGPPGANLFSAGPGTNLGIPPGPDSDpltglpnnpfRLDRTVGLGAVTPDPVHR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 111 FEDVLEQLLGfrpndstGAaaspsdMSGFVrsAVSVSALLTDA-VMRGFTPSRLPAFSALASSFAVFDRWFSSIPGPTQP 189
Cdd:cd16013    81 FYQEQQQING-------GK------MDGFV--AGSGGTTGDGGqVMGYYDGNDLPFLWDLAQEYTLADNFFASVFGGTFP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 190 NRLFLYSATSHGAVAHDKW--------------NLLRGYPQRTIFDSLAADALDYRVYFKTIPTTLFYRRLRT------V 249
Cdd:cd16013   146 NRLYLIAAQSPGFTNAGPSsaapldplddtastPPLPPQTQPTIGDRLSAAGVSWGWYSGGWNPALAGAPKSTfpfpyfF 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 250 ANAARGTFRR---YDAA-FRDHARRGLLPALSVIEPRYFDltgtpadDDHPA-HDVANGQRLVKDVYEALRAGPQWNHTL 324
Cdd:cd16013   226 FTFIGTTAGAnhlKDLTdFYADAKAGTLPAVSFVKPSGLN-------DGHPGySDVLAGQAFLADVINALQKSPQWNSTA 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 325 LIITYDEHGGFYDHVPPPNVGVPSPDairgplpfffrFDRLGVRVPTIMVSPWIRKGTVVGrppggptptSEYEHSSIPA 404
Cdd:cd16013   299 IIITYDEHGGFYDHVPPPKADAPDPG-----------RWGPGFRVPAIVISPYAKRGYVDH---------TVYDHTSILK 358
                         410
                  ....*....|
gi 1002227803 405 TIKKIFNLSS 414
Cdd:cd16013   359 FIEDRWGLPP 368
PlcC COG3511
Phospholipase C [Cell wall/membrane/envelope biogenesis];
34-431 7.68e-69

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


Pssm-ID: 442734  Cd Length: 392  Bit Score: 226.65  E-value: 7.68e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803  34 APNSNGDSKIKNVVVLALENRSFDHMLGWM--------QRLLGLPiDGLTGAECNPAPGPGPADSLLHCVSPDADLVVPD 105
Cdd:COG3511     1 ANRTGTLTDIKHVVVLMQENRSFDHYFGTLpgvrgfgdPNPIPQP-DGKPVFTQLPDPNGALPNLPFRLDTTQTNAQRTG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 106 DPAHAFEDVLEQLLGFRpndstgaaaspsdMSGFVRSAVSVsalltDAVMRGFTPSRLPAFSALASSFAVFDRWFSSIPG 185
Cdd:COG3511    80 DLPHSWYDEQAAWNGGK-------------MDGFVAAKDAG-----GLTMGYYDRADLPFYYALADAFTLCDNYFCSVFG 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 186 PTQPNRLFLYSATSHGAVAHDKWNL------------LRGYPQRTIFDSLAADALDYRVY------FKTIPTT---LFYR 244
Cdd:COG3511   142 GTTPNRLYLVSGTTPPYGNAGGPDVynvdadpssattLPPQTWTTIGDRLEAAGVSWKWYqggwdnALAGPHHnplQYFA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 245 RLRTVANAARGTFRRYDAAFRDHARRGLLPALSVIEPRYfdltgtpADDDHPA-HDVANGQRLVKDVYEALRAGPQWNHT 323
Cdd:COG3511   222 QFANATPDRASHLYDRLDDFRADVAAGTLPAVSFIKPPG-------AYSEHPGySDPADGAAYIADVLDALTASPVWSKT 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 324 LLIITYDEHGGFYDHVPPPNVGVPSPDAIRGPLPFffrfdRLGVRVPTIMVSPWIRKGTVVgrppggptptSE-YEHSSI 402
Cdd:COG3511   295 AIIITYDENGGFFDHVPPPVPPSSTDGEGGDGDPY-----GLGPRVPMLVISPWAKGGWVD----------HTvFDHTSV 359
                         410       420
                  ....*....|....*....|....*....
gi 1002227803 403 PATIKKIFNLSSDFLTRRDAWAGTFEHLF 431
Cdd:COG3511   360 LRFIEKRFGLPELNIPWRRAVAGDLTSAF 388
PLC cd16014
non-hemolytic phospholipase C; Nonhemolytic Phospholipases C is produced by pathogenic ...
43-383 6.08e-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: 138.55  E-value: 6.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803  43 IKNVVVLALENRSFDHMLGWMQRLLGLpidgltgaecnpapgpgpADSllhcvspdadlvvpddpaHAFEDVLEQLLGFR 122
Cdd:cd16014     1 IEHVVIFMQENRSFDHYFGTLAGVRGF------------------NDS------------------NSWNNNHAAWNGGL 44
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 123 pNDSTGAAASPSDMsGFvrsavsvsalltdavmrgFTPSRLPAFSALASSFAVFDRWFSSIPGPTQPNRLFLYSATSHGA 202
Cdd:cd16014    45 -NDNWILAKTPYSM-GY------------------FTREDIPFHYALADAFTICDMYHCSVLGSTDPNRLYLWSGTIDPP 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 203 VAHdkwnllrGYPQRTIFDslAADALDYRVY-FKTIPTTLfyrrlrtvaNAARGTFRRYD--AAFRDHARRGLLPALSVI 279
Cdd:cd16014   105 GGN-------GGPQATPGP--ATNNLDCFPLtWTTYPEYL---------EDAGVSWRVYQdlDAFKADAANGTLPQVSWI 166
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 280 EPRYfdltgtpADDDHPAHDVANGQRLVKDVYEALRAGPQ-WNHTLLIITYDEHGGFYDHVPPPNvgVPSPDAIRGPLPF 358
Cdd:cd16014   167 VAPQ-------ELSEHPPNTPADGAWLVKQVLDALASSPDvWNKTVFIINYDENGGFFDHVTPPV--PPPGTAGEWLTPP 237
                         330       340
                  ....*....|....*....|....*....
gi 1002227803 359 FFRFDR----LGVRVPTIMVSPWIRKGTV 383
Cdd:cd16014   238 YETGGGtpigLGFRVPMLVISPWSRGGNV 266
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
162-410 3.09e-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: 48.57  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 162 RLPAFSALASSFAVFDRWFSSIPGPTQPNRLFLysATSHGAVAHDkwnlLRGYPQRTIFDSLAADALDYRVYfkTIPTTL 241
Cdd:cd00016    25 TTPNLKRLASEGATFNFRSVSPPTSSAPNHAAL--LTGAYPTLHG----YTGNGSADPELPSRAAGKDEDGP--TIPELL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 242 fyrrlrtvaNAARGTFRRYdaAFRDHARRGLL--PALSVIEPRYFDLTGTPADDDHPAHDvANGQRL---VKDVYEALRA 316
Cdd:cd00016    97 ---------KQAGYRTGVI--GLLKAIDETSKekPFVLFLHFDGPDGPGHAYGPNTPEYY-DAVEEIderIGKVLDALKK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227803 317 GPQWNHTLLIITYDEHGGFYDHVPPPNvgvpspdairgPLPFFFRFDrLGVRVPTIMVSPWIRKGTVVGRPpggptptse 396
Cdd:cd00016   165 AGDADDTVIIVTADHGGIDKGHGGDPK-----------ADGKADKSH-TGMRVPFIAYGPGVKKGGVKHEL--------- 223
                         250
                  ....*....|....
gi 1002227803 397 YEHSSIPATIKKIF 410
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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