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Conserved domains on  [gi|117558485|gb|AAI26079|]
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P76 protein, partial [Rattus norvegicus]

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 ...
1-318 3.78e-139

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: 428195  Cd Length: 483  Bit Score: 402.49  E-value: 3.78e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117558485    1 YQNMLRIIKKYRLQFregpqEEYPLIAGNNLIFSSYPGTIFSGDDFYILGSGLVTLETTIGNKNPALWKYVQPQGcVLEW 80
Cdd:pfam04916 185 YSSMLRIYKHYTFPV-----SDRAVVPGTTVSFSSYPGLLSSLDDFYITSSGLAVMETTNGIFNQTLYKLIKPSS-VLTW 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117558485   81 IRNIVANRLALDGATWADVFRRFNSGTYNNQWMIVDYKAFIPNGPSPgSRVLTILEQIPGMVVVADKTAELYKTTYWASY 160
Cdd:pfam04916 259 QRVMVANRLAHSGREWAEIFSRYNSGTYNNQWMVLDYKLFTPGQELP-DGTFWVVEQIPGYIEASDVTAVLNRTGYWPSY 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117558485  161 NIPYFESVFNASGLQALVAQYGDWFSYTRNPRAKIFQRDQSLVEDVDTMVRLMRYNDFLHDPLSLCEACspkpnaeNAIS 240
Cdd:pfam04916 338 NIPYFPEIYNISGYPAMVEKYGDWFSYDLTPRAKIFRRDQGNVTDLESMKALMRYNNYKKDPLSKGSPE-------NAIS 410
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117558485  241 ARSDLNPANGsypfqalrQRAHGGIDVKVTSVALAKYMSMLAASGPTWDQLPPFQWSKSPFHNML-HMGQPDLWMFSPV 318
Cdd:pfam04916 411 ARGDLNPAGG--------HRAFGAIDTKVTNYALVLSLQARAISGPTTDTQPPFDWSSSPFFNVTrHQGHPDVWNFDFV 481
 
Name Accession Description Interval E-value
Phospholip_B pfam04916
Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester ...
1-318 3.78e-139

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: 428195  Cd Length: 483  Bit Score: 402.49  E-value: 3.78e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117558485    1 YQNMLRIIKKYRLQFregpqEEYPLIAGNNLIFSSYPGTIFSGDDFYILGSGLVTLETTIGNKNPALWKYVQPQGcVLEW 80
Cdd:pfam04916 185 YSSMLRIYKHYTFPV-----SDRAVVPGTTVSFSSYPGLLSSLDDFYITSSGLAVMETTNGIFNQTLYKLIKPSS-VLTW 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117558485   81 IRNIVANRLALDGATWADVFRRFNSGTYNNQWMIVDYKAFIPNGPSPgSRVLTILEQIPGMVVVADKTAELYKTTYWASY 160
Cdd:pfam04916 259 QRVMVANRLAHSGREWAEIFSRYNSGTYNNQWMVLDYKLFTPGQELP-DGTFWVVEQIPGYIEASDVTAVLNRTGYWPSY 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117558485  161 NIPYFESVFNASGLQALVAQYGDWFSYTRNPRAKIFQRDQSLVEDVDTMVRLMRYNDFLHDPLSLCEACspkpnaeNAIS 240
Cdd:pfam04916 338 NIPYFPEIYNISGYPAMVEKYGDWFSYDLTPRAKIFRRDQGNVTDLESMKALMRYNNYKKDPLSKGSPE-------NAIS 410
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117558485  241 ARSDLNPANGsypfqalrQRAHGGIDVKVTSVALAKYMSMLAASGPTWDQLPPFQWSKSPFHNML-HMGQPDLWMFSPV 318
Cdd:pfam04916 411 ARGDLNPAGG--------HRAFGAIDTKVTNYALVLSLQARAISGPTTDTQPPFDWSSSPFFNVTrHQGHPDVWNFDFV 481
 
Name Accession Description Interval E-value
Phospholip_B pfam04916
Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester ...
1-318 3.78e-139

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: 428195  Cd Length: 483  Bit Score: 402.49  E-value: 3.78e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117558485    1 YQNMLRIIKKYRLQFregpqEEYPLIAGNNLIFSSYPGTIFSGDDFYILGSGLVTLETTIGNKNPALWKYVQPQGcVLEW 80
Cdd:pfam04916 185 YSSMLRIYKHYTFPV-----SDRAVVPGTTVSFSSYPGLLSSLDDFYITSSGLAVMETTNGIFNQTLYKLIKPSS-VLTW 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117558485   81 IRNIVANRLALDGATWADVFRRFNSGTYNNQWMIVDYKAFIPNGPSPgSRVLTILEQIPGMVVVADKTAELYKTTYWASY 160
Cdd:pfam04916 259 QRVMVANRLAHSGREWAEIFSRYNSGTYNNQWMVLDYKLFTPGQELP-DGTFWVVEQIPGYIEASDVTAVLNRTGYWPSY 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117558485  161 NIPYFESVFNASGLQALVAQYGDWFSYTRNPRAKIFQRDQSLVEDVDTMVRLMRYNDFLHDPLSLCEACspkpnaeNAIS 240
Cdd:pfam04916 338 NIPYFPEIYNISGYPAMVEKYGDWFSYDLTPRAKIFRRDQGNVTDLESMKALMRYNNYKKDPLSKGSPE-------NAIS 410
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117558485  241 ARSDLNPANGsypfqalrQRAHGGIDVKVTSVALAKYMSMLAASGPTWDQLPPFQWSKSPFHNML-HMGQPDLWMFSPV 318
Cdd:pfam04916 411 ARGDLNPAGG--------HRAFGAIDTKVTNYALVLSLQARAISGPTTDTQPPFDWSSSPFFNVTrHQGHPDVWNFDFV 481
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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