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Conserved domains on  [gi|767973454|ref|XP_011536325|]
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putative phospholipase B-like 2 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Phospholip_B super family cl20281
Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester ...
4-459 0e+00

Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester bonds of glycerophospholipids. This family of PLB enzymes has been identified in mammals, flies and nematodes but not in yeast. In Drosophila this protein was named LAMA for laminin ancestor since it is expressed in the neuronal and glial precursors that surround the lamina.


The actual alignment was detected with superfamily member pfam04916:

Pssm-ID: 398535  Cd Length: 536  Bit Score: 536.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973454    4 LIYMHWMNTVVNYCGPFEyevGYC-ERLKSFLEANLEWMQEEMESNPDSPYWHQVRLTLLQLKGLEDSYEGRVSFPAGKf 82
Cdd:pfam04916  98 LIYDHYSNTFPQYCKNST---GFCdPKLRAFLEENLKWMRKQVKENPDDPYWRQVGLVYAQLDGLVAGYNARAASDKRK- 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973454   83 TIKPLGFLLLQLSGDLEDLELALNKTKIKPS------LGSGSCSALIKLLPGQSDLLVAHNTWNNYQHMLRVIKKYWLQF 156
Cdd:pfam04916 174 PLTFFQILLLNLAGDLEDLVPALSPPKNSSQqakflmKEPGHCSALIKLLPGFEDLLFGHTTWSSYSAMLRIYKHYDFPV 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973454  157 regpwGDYPLVPGNKLVFSSYPGTIFSCDDFYILGSGLVTLETTIGNKNPALWKYVRPRGcVLEWVRNIVANRLASDGAT 236
Cdd:pfam04916 254 -----SDRAVVPGTTVSFSSYPGLLSSLDDFYITSSGLAVMETTNGIFNQTLYKLVKPSS-VLTWQRVMVANRLAHSGRE 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973454  237 WADIFKRFNSGTYNNQWMIVDYKAFIPGGPSPgSRVLTILEQIPGMVVVADKTSELYQKTYWASYNIPSFETVFNASGLQ 316
Cdd:pfam04916 328 WAEIFSRYNSGTYNNQWMVLDYKLFTPGQELP-DGTFWVVEQIPGYIEASDVTAVLNRTGYWPSYNIPYFPEIYNISGYP 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973454  317 ALVAQYGDWFSYDGSPRAQIFRRNQSLVQDMDSMVRLMRYNDFLHDPLSLCKACnpqpngeNAISARSDLNPANGsypfq 396
Cdd:pfam04916 407 AMVEKYGDWFSYDLTPRAKIFRRDQGNVTDLESMKALMRYNNYKKDPLSKGSPE-------NAISARGDLNPSGG----- 474
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973454  397 alrQRSHGGIDVKVTSMSLARILSLLAASGPTWDQVPPFQWSTSP-FSGLLHMGQPDLWKFAPV 459
Cdd:pfam04916 475 ---HRAFGAIDTKVTNYALVLSLQARAISGPTTDTQPPFDWSSSPfFNVTRHQGHPDVWNFDFV 535
 
Name Accession Description Interval E-value
Phospholip_B pfam04916
Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester ...
4-459 0e+00

Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester bonds of glycerophospholipids. This family of PLB enzymes has been identified in mammals, flies and nematodes but not in yeast. In Drosophila this protein was named LAMA for laminin ancestor since it is expressed in the neuronal and glial precursors that surround the lamina.


Pssm-ID: 398535  Cd Length: 536  Bit Score: 536.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973454    4 LIYMHWMNTVVNYCGPFEyevGYC-ERLKSFLEANLEWMQEEMESNPDSPYWHQVRLTLLQLKGLEDSYEGRVSFPAGKf 82
Cdd:pfam04916  98 LIYDHYSNTFPQYCKNST---GFCdPKLRAFLEENLKWMRKQVKENPDDPYWRQVGLVYAQLDGLVAGYNARAASDKRK- 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973454   83 TIKPLGFLLLQLSGDLEDLELALNKTKIKPS------LGSGSCSALIKLLPGQSDLLVAHNTWNNYQHMLRVIKKYWLQF 156
Cdd:pfam04916 174 PLTFFQILLLNLAGDLEDLVPALSPPKNSSQqakflmKEPGHCSALIKLLPGFEDLLFGHTTWSSYSAMLRIYKHYDFPV 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973454  157 regpwGDYPLVPGNKLVFSSYPGTIFSCDDFYILGSGLVTLETTIGNKNPALWKYVRPRGcVLEWVRNIVANRLASDGAT 236
Cdd:pfam04916 254 -----SDRAVVPGTTVSFSSYPGLLSSLDDFYITSSGLAVMETTNGIFNQTLYKLVKPSS-VLTWQRVMVANRLAHSGRE 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973454  237 WADIFKRFNSGTYNNQWMIVDYKAFIPGGPSPgSRVLTILEQIPGMVVVADKTSELYQKTYWASYNIPSFETVFNASGLQ 316
Cdd:pfam04916 328 WAEIFSRYNSGTYNNQWMVLDYKLFTPGQELP-DGTFWVVEQIPGYIEASDVTAVLNRTGYWPSYNIPYFPEIYNISGYP 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973454  317 ALVAQYGDWFSYDGSPRAQIFRRNQSLVQDMDSMVRLMRYNDFLHDPLSLCKACnpqpngeNAISARSDLNPANGsypfq 396
Cdd:pfam04916 407 AMVEKYGDWFSYDLTPRAKIFRRDQGNVTDLESMKALMRYNNYKKDPLSKGSPE-------NAISARGDLNPSGG----- 474
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973454  397 alrQRSHGGIDVKVTSMSLARILSLLAASGPTWDQVPPFQWSTSP-FSGLLHMGQPDLWKFAPV 459
Cdd:pfam04916 475 ---HRAFGAIDTKVTNYALVLSLQARAISGPTTDTQPPFDWSSSPfFNVTRHQGHPDVWNFDFV 535
 
Name Accession Description Interval E-value
Phospholip_B pfam04916
Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester ...
4-459 0e+00

Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester bonds of glycerophospholipids. This family of PLB enzymes has been identified in mammals, flies and nematodes but not in yeast. In Drosophila this protein was named LAMA for laminin ancestor since it is expressed in the neuronal and glial precursors that surround the lamina.


Pssm-ID: 398535  Cd Length: 536  Bit Score: 536.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973454    4 LIYMHWMNTVVNYCGPFEyevGYC-ERLKSFLEANLEWMQEEMESNPDSPYWHQVRLTLLQLKGLEDSYEGRVSFPAGKf 82
Cdd:pfam04916  98 LIYDHYSNTFPQYCKNST---GFCdPKLRAFLEENLKWMRKQVKENPDDPYWRQVGLVYAQLDGLVAGYNARAASDKRK- 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973454   83 TIKPLGFLLLQLSGDLEDLELALNKTKIKPS------LGSGSCSALIKLLPGQSDLLVAHNTWNNYQHMLRVIKKYWLQF 156
Cdd:pfam04916 174 PLTFFQILLLNLAGDLEDLVPALSPPKNSSQqakflmKEPGHCSALIKLLPGFEDLLFGHTTWSSYSAMLRIYKHYDFPV 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973454  157 regpwGDYPLVPGNKLVFSSYPGTIFSCDDFYILGSGLVTLETTIGNKNPALWKYVRPRGcVLEWVRNIVANRLASDGAT 236
Cdd:pfam04916 254 -----SDRAVVPGTTVSFSSYPGLLSSLDDFYITSSGLAVMETTNGIFNQTLYKLVKPSS-VLTWQRVMVANRLAHSGRE 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973454  237 WADIFKRFNSGTYNNQWMIVDYKAFIPGGPSPgSRVLTILEQIPGMVVVADKTSELYQKTYWASYNIPSFETVFNASGLQ 316
Cdd:pfam04916 328 WAEIFSRYNSGTYNNQWMVLDYKLFTPGQELP-DGTFWVVEQIPGYIEASDVTAVLNRTGYWPSYNIPYFPEIYNISGYP 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973454  317 ALVAQYGDWFSYDGSPRAQIFRRNQSLVQDMDSMVRLMRYNDFLHDPLSLCKACnpqpngeNAISARSDLNPANGsypfq 396
Cdd:pfam04916 407 AMVEKYGDWFSYDLTPRAKIFRRDQGNVTDLESMKALMRYNNYKKDPLSKGSPE-------NAISARGDLNPSGG----- 474
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973454  397 alrQRSHGGIDVKVTSMSLARILSLLAASGPTWDQVPPFQWSTSP-FSGLLHMGQPDLWKFAPV 459
Cdd:pfam04916 475 ---HRAFGAIDTKVTNYALVLSLQARAISGPTTDTQPPFDWSSSPfFNVTRHQGHPDVWNFDFV 535
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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