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Conserved domains on  [gi|1720414843|ref|XP_030110675|]
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putative phospholipase B-like 2 isoform X1 [Mus musculus]

Protein Classification

phospholipase B family protein( domain architecture ID 139914)

phospholipase B family protein may catalyze the hydrolytic cleavage of acylester bonds in glycerophospholipids; similar to Drosophila melanogaster phospholipase B-like lamina ancestor involved in the regulation of cellular plasticity in imaginal disks

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 ...
 1-315 5.45e-138

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: 461479  Cd Length: 483  Bit Score: 399.40  E-value: 5.45e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414843   1 MLRIIKKYRLQFregpqEEYPLVAGNNLVFSSYPGTIFSGDDFYILGSGLVTLETTIGNKNPALWKYVQPQGcVLEWIRN 80
Cdd:pfam04916 188 MLRIYKHYTFPV-----SDRAVVPGTTVSFSSYPGLLSSLDDFYITSSGLAVMETTNGIFNQTLYKLIKPSS-VLTWQRV 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414843  81 VVANRLALDGATWADVFKRFNSGTYNNQWMIVDYKAFLPNGPSPgSRVLTILEQIPGMVVVADKTAELYKTTYWASYNIP 160
Cdd:pfam04916 262 MVANRLAHSGREWAEIFSRYNSGTYNNQWMVLDYKLFTPGQELP-DGTFWVVEQIPGYIEASDVTAVLNRTGYWPSYNIP 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414843 161 YFETVFNASGLQALVAQYGDWFSYTKNPRAKIFQRDQSLVEDMDAMVRLMRYNDFLHDPLSLCEACnpkpnaeNAISARS 240
Cdd:pfam04916 341 YFPEIYNISGYPAMVEKYGDWFSYDLTPRAKIFRRDQGNVTDLESMKALMRYNNYKKDPLSKGSPE-------NAISARG 413

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720414843 241 DLNPANGsypfqalhQRAHGGIDVKVTSFTLAKYMSMLAASGPTWDQCPPFQWSKSPFHSML-HMGQPDLWMFSPI 315
Cdd:pfam04916 414 DLNPAGG--------HRAFGAIDTKVTNYALVLSLQARAISGPTTDTQPPFDWSSSPFFNVTrHQGHPDVWNFDFV 481
 
Name Accession Description Interval E-value
Phospholip_B pfam04916
Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester ...
 1-315 5.45e-138

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: 461479  Cd Length: 483  Bit Score: 399.40  E-value: 5.45e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414843   1 MLRIIKKYRLQFregpqEEYPLVAGNNLVFSSYPGTIFSGDDFYILGSGLVTLETTIGNKNPALWKYVQPQGcVLEWIRN 80
Cdd:pfam04916 188 MLRIYKHYTFPV-----SDRAVVPGTTVSFSSYPGLLSSLDDFYITSSGLAVMETTNGIFNQTLYKLIKPSS-VLTWQRV 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414843  81 VVANRLALDGATWADVFKRFNSGTYNNQWMIVDYKAFLPNGPSPgSRVLTILEQIPGMVVVADKTAELYKTTYWASYNIP 160
Cdd:pfam04916 262 MVANRLAHSGREWAEIFSRYNSGTYNNQWMVLDYKLFTPGQELP-DGTFWVVEQIPGYIEASDVTAVLNRTGYWPSYNIP 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414843 161 YFETVFNASGLQALVAQYGDWFSYTKNPRAKIFQRDQSLVEDMDAMVRLMRYNDFLHDPLSLCEACnpkpnaeNAISARS 240
Cdd:pfam04916 341 YFPEIYNISGYPAMVEKYGDWFSYDLTPRAKIFRRDQGNVTDLESMKALMRYNNYKKDPLSKGSPE-------NAISARG 413

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720414843 241 DLNPANGsypfqalhQRAHGGIDVKVTSFTLAKYMSMLAASGPTWDQCPPFQWSKSPFHSML-HMGQPDLWMFSPI 315
Cdd:pfam04916 414 DLNPAGG--------HRAFGAIDTKVTNYALVLSLQARAISGPTTDTQPPFDWSSSPFFNVTrHQGHPDVWNFDFV 481
 
Name Accession Description Interval E-value
Phospholip_B pfam04916
Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester ...
 1-315 5.45e-138

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: 461479  Cd Length: 483  Bit Score: 399.40  E-value: 5.45e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414843   1 MLRIIKKYRLQFregpqEEYPLVAGNNLVFSSYPGTIFSGDDFYILGSGLVTLETTIGNKNPALWKYVQPQGcVLEWIRN 80
Cdd:pfam04916 188 MLRIYKHYTFPV-----SDRAVVPGTTVSFSSYPGLLSSLDDFYITSSGLAVMETTNGIFNQTLYKLIKPSS-VLTWQRV 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414843  81 VVANRLALDGATWADVFKRFNSGTYNNQWMIVDYKAFLPNGPSPgSRVLTILEQIPGMVVVADKTAELYKTTYWASYNIP 160
Cdd:pfam04916 262 MVANRLAHSGREWAEIFSRYNSGTYNNQWMVLDYKLFTPGQELP-DGTFWVVEQIPGYIEASDVTAVLNRTGYWPSYNIP 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414843 161 YFETVFNASGLQALVAQYGDWFSYTKNPRAKIFQRDQSLVEDMDAMVRLMRYNDFLHDPLSLCEACnpkpnaeNAISARS 240
Cdd:pfam04916 341 YFPEIYNISGYPAMVEKYGDWFSYDLTPRAKIFRRDQGNVTDLESMKALMRYNNYKKDPLSKGSPE-------NAISARG 413

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720414843 241 DLNPANGsypfqalhQRAHGGIDVKVTSFTLAKYMSMLAASGPTWDQCPPFQWSKSPFHSML-HMGQPDLWMFSPI 315
Cdd:pfam04916 414 DLNPAGG--------HRAFGAIDTKVTNYALVLSLQARAISGPTTDTQPPFDWSSSPFFNVTrHQGHPDVWNFDFV 481
 
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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