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Conserved domains on  [gi|19114338|ref|NP_593426|]
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phospholipid scramblase [Schizosaccharomyces pombe]

Protein Classification

LURP-one-related/scramblase family protein( domain architecture ID 1453)

LURP-one-related/scramblase family protein similar to Arabidopsis thaliana protein LURP16, which might be related to the phospholipid scramblase and tubby-like superfamily of membrane tethered transcription factors

PubMed:  19010806

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LOR super family cl02043
LURP-one-related; The structure of this family has been solved. It comprises a 12-stranded ...
 58-304 3.44e-93

LURP-one-related; The structure of this family has been solved. It comprises a 12-stranded beta barrel with a central C-terminal alpha helix. This helix is thought to be a transmembrane helix. It is structurally similar to the C-terminal domain of the Tubby protein. In plants it plays a role in defense against pathogens.


The actual alignment was detected with superfamily member pfam03803:

Pssm-ID: 470445  Cd Length: 221  Bit Score: 278.08  E-value: 3.44e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114338    58 ISSTGAIPLNSPAA--PLLSQDVLIVERQLEMMNVFLGYEQANRYVILNQQGQHLGYIAEQgassiLSSLSRQFFHTHRA 135
Cdd:pfam03803   1 MSGPGQPPANCPAGleYLLQLDQILVHQQIEPLEVFTGFETANRYVVKNVNGQPLYYAMER-----SNCCARQCCGTHRP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114338   136 FKADVMDSNGQLVLQLNRPFSWIN---SRLQIHSIdySKFSSTLVGEVLQKWHLWRRRYELFLAKR----SMFEQFAKID 208
Cdd:pfam03803  76 FVMRITDNFGNEVMTLKRPFSCISccpSCLQEQEI--QAPPGTTIGEVLQTWHLWRPNYELQNADGnqvlSIFGPCFKCD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114338   209 eRVLSWEFLLRNEQDRILGSVSRNFMGLPREFFTDTGNYVLRFTStsaangsvnenqllqaahgiandvcarDMSLEERA 288
Cdd:pfam03803 154 -CGGDWEFPVKTADGEVVGSISRNWPGLGREAFTDADTYVVRFPL---------------------------DLDVKLKA 205

                         250
                  ....*....|....*.
gi 19114338   289 VMLGSAVTIDFDYFSR 304
Cdd:pfam03803 206 VLLGAAFLIDFMYFER 221
 
Name Accession Description Interval E-value
Scramblase pfam03803
Scramblase; Scramblase is palmitoylated and contains a potential protein kinase C ...
 58-304 3.44e-93

Scramblase; Scramblase is palmitoylated and contains a potential protein kinase C phosphorylation site. Scramblase exhibits Ca2+-activated phospholipid scrambling activity in vitro. There are also possible SH3 and WW binding motifs. Scramblase is involved in the redistribution of phospholipids after cell activation or injury.


Pssm-ID: 252175  Cd Length: 221  Bit Score: 278.08  E-value: 3.44e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114338    58 ISSTGAIPLNSPAA--PLLSQDVLIVERQLEMMNVFLGYEQANRYVILNQQGQHLGYIAEQgassiLSSLSRQFFHTHRA 135
Cdd:pfam03803   1 MSGPGQPPANCPAGleYLLQLDQILVHQQIEPLEVFTGFETANRYVVKNVNGQPLYYAMER-----SNCCARQCCGTHRP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114338   136 FKADVMDSNGQLVLQLNRPFSWIN---SRLQIHSIdySKFSSTLVGEVLQKWHLWRRRYELFLAKR----SMFEQFAKID 208
Cdd:pfam03803  76 FVMRITDNFGNEVMTLKRPFSCISccpSCLQEQEI--QAPPGTTIGEVLQTWHLWRPNYELQNADGnqvlSIFGPCFKCD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114338   209 eRVLSWEFLLRNEQDRILGSVSRNFMGLPREFFTDTGNYVLRFTStsaangsvnenqllqaahgiandvcarDMSLEERA 288
Cdd:pfam03803 154 -CGGDWEFPVKTADGEVVGSISRNWPGLGREAFTDADTYVVRFPL---------------------------DLDVKLKA 205

                         250
                  ....*....|....*.
gi 19114338   289 VMLGSAVTIDFDYFSR 304
Cdd:pfam03803 206 VLLGAAFLIDFMYFER 221
 
Name Accession Description Interval E-value
Scramblase pfam03803
Scramblase; Scramblase is palmitoylated and contains a potential protein kinase C ...
 58-304 3.44e-93

Scramblase; Scramblase is palmitoylated and contains a potential protein kinase C phosphorylation site. Scramblase exhibits Ca2+-activated phospholipid scrambling activity in vitro. There are also possible SH3 and WW binding motifs. Scramblase is involved in the redistribution of phospholipids after cell activation or injury.


Pssm-ID: 252175  Cd Length: 221  Bit Score: 278.08  E-value: 3.44e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114338    58 ISSTGAIPLNSPAA--PLLSQDVLIVERQLEMMNVFLGYEQANRYVILNQQGQHLGYIAEQgassiLSSLSRQFFHTHRA 135
Cdd:pfam03803   1 MSGPGQPPANCPAGleYLLQLDQILVHQQIEPLEVFTGFETANRYVVKNVNGQPLYYAMER-----SNCCARQCCGTHRP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114338   136 FKADVMDSNGQLVLQLNRPFSWIN---SRLQIHSIdySKFSSTLVGEVLQKWHLWRRRYELFLAKR----SMFEQFAKID 208
Cdd:pfam03803  76 FVMRITDNFGNEVMTLKRPFSCISccpSCLQEQEI--QAPPGTTIGEVLQTWHLWRPNYELQNADGnqvlSIFGPCFKCD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114338   209 eRVLSWEFLLRNEQDRILGSVSRNFMGLPREFFTDTGNYVLRFTStsaangsvnenqllqaahgiandvcarDMSLEERA 288
Cdd:pfam03803 154 -CGGDWEFPVKTADGEVVGSISRNWPGLGREAFTDADTYVVRFPL---------------------------DLDVKLKA 205

                         250
                  ....*....|....*.
gi 19114338   289 VMLGSAVTIDFDYFSR 304
Cdd:pfam03803 206 VLLGAAFLIDFMYFER 221
 
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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