NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|55778435|gb|AAH86408|]
View 

P76 protein, partial [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
1-294 3.50e-132

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: 385.56  E-value: 3.50e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55778435     1 LIAGNNLIFSSYPGTIFSGDDFYILGSGLVTLETTIGNKNPALWKYVQPQGcVLEWIRNIVANRLALDGATWADVFRRFN 80
Cdd:pfam04916 258 VVPGTTVSFSSYPGLLSSLDDFYITSSGLAVMETTNGIFNQTLYKLVKPSS-VLTWQRVMVANRLAHSGREWAEIFSRYN 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55778435    81 SGTYNNQWMIVDYKAFIPNGPSPgSRVLTILEQIPGMVVVADKTAELYKTTYWASYNIPYFESVFNASGLQALVAQYGDW 160
Cdd:pfam04916 337 SGTYNNQWMVLDYKLFTPGQELP-DGTFWVVEQIPGYIEASDVTAVLNRTGYWPSYNIPYFPEIYNISGYPAMVEKYGDW 415
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55778435   161 FSYTRNPRAKIFQRDQSLVEDVDTMVRLMRYNDFLHDPLSLCEACspkpnaeNAISARSDLNPANGsypfqalrQRAHGG 240
Cdd:pfam04916 416 FSYDLTPRAKIFRRDQGNVTDLESMKALMRYNNYKKDPLSKGSPE-------NAISARGDLNPSGG--------HRAFGA 480
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 55778435   241 IDVKVTSVALAKYMSMLAASGPTWDQLPPFQWSKSPFHNML-HMGQPDLWMFSPV 294
Cdd:pfam04916 481 IDTKVTNYALVLSLQARAISGPTTDTQPPFDWSSSPFFNVTrHQGHPDVWNFDFV 535
 
Name Accession Description Interval E-value
Phospholip_B pfam04916
Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester ...
1-294 3.50e-132

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: 385.56  E-value: 3.50e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55778435     1 LIAGNNLIFSSYPGTIFSGDDFYILGSGLVTLETTIGNKNPALWKYVQPQGcVLEWIRNIVANRLALDGATWADVFRRFN 80
Cdd:pfam04916 258 VVPGTTVSFSSYPGLLSSLDDFYITSSGLAVMETTNGIFNQTLYKLVKPSS-VLTWQRVMVANRLAHSGREWAEIFSRYN 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55778435    81 SGTYNNQWMIVDYKAFIPNGPSPgSRVLTILEQIPGMVVVADKTAELYKTTYWASYNIPYFESVFNASGLQALVAQYGDW 160
Cdd:pfam04916 337 SGTYNNQWMVLDYKLFTPGQELP-DGTFWVVEQIPGYIEASDVTAVLNRTGYWPSYNIPYFPEIYNISGYPAMVEKYGDW 415
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55778435   161 FSYTRNPRAKIFQRDQSLVEDVDTMVRLMRYNDFLHDPLSLCEACspkpnaeNAISARSDLNPANGsypfqalrQRAHGG 240
Cdd:pfam04916 416 FSYDLTPRAKIFRRDQGNVTDLESMKALMRYNNYKKDPLSKGSPE-------NAISARGDLNPSGG--------HRAFGA 480
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 55778435   241 IDVKVTSVALAKYMSMLAASGPTWDQLPPFQWSKSPFHNML-HMGQPDLWMFSPV 294
Cdd:pfam04916 481 IDTKVTNYALVLSLQARAISGPTTDTQPPFDWSSSPFFNVTrHQGHPDVWNFDFV 535
 
Name Accession Description Interval E-value
Phospholip_B pfam04916
Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester ...
1-294 3.50e-132

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: 385.56  E-value: 3.50e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55778435     1 LIAGNNLIFSSYPGTIFSGDDFYILGSGLVTLETTIGNKNPALWKYVQPQGcVLEWIRNIVANRLALDGATWADVFRRFN 80
Cdd:pfam04916 258 VVPGTTVSFSSYPGLLSSLDDFYITSSGLAVMETTNGIFNQTLYKLVKPSS-VLTWQRVMVANRLAHSGREWAEIFSRYN 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55778435    81 SGTYNNQWMIVDYKAFIPNGPSPgSRVLTILEQIPGMVVVADKTAELYKTTYWASYNIPYFESVFNASGLQALVAQYGDW 160
Cdd:pfam04916 337 SGTYNNQWMVLDYKLFTPGQELP-DGTFWVVEQIPGYIEASDVTAVLNRTGYWPSYNIPYFPEIYNISGYPAMVEKYGDW 415
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55778435   161 FSYTRNPRAKIFQRDQSLVEDVDTMVRLMRYNDFLHDPLSLCEACspkpnaeNAISARSDLNPANGsypfqalrQRAHGG 240
Cdd:pfam04916 416 FSYDLTPRAKIFRRDQGNVTDLESMKALMRYNNYKKDPLSKGSPE-------NAISARGDLNPSGG--------HRAFGA 480
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 55778435   241 IDVKVTSVALAKYMSMLAASGPTWDQLPPFQWSKSPFHNML-HMGQPDLWMFSPV 294
Cdd:pfam04916 481 IDTKVTNYALVLSLQARAISGPTTDTQPPFDWSSSPFFNVTrHQGHPDVWNFDFV 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH