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Conserved domains on  [gi|18422886|ref|NP_568693|]
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prolamin-like protein (DUF1278) [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Prolamin_like super family cl05275
Prolamin-like; Prolamin_like (in which DUF784 and DUF1278 have been merged) is found to be ...
 7-97 1.62e-13

Prolamin-like; Prolamin_like (in which DUF784 and DUF1278 have been merged) is found to be expressed in the plant embryo sac and to be regulated by the Myb98 transcription factor. Computational analysis has revealed that members are homologous to the plant prolamin superfamily (Protease inhibitor-seed storage-LTP family, pfam00234). In contrast to typical prolamin members that have eight conserved Cys residues forming four pairs of disulfide bonds, this domain contains only six conserved Cys residues that may form three pairs of disulfide bonds. The domain may have a potential function in lipid transfer or protection during plant embryo sac development and reproduction.


The actual alignment was detected with superfamily member PLN00213:

Pssm-ID: 471214  Cd Length: 118  Bit Score: 61.18  E-value: 1.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422886    7 FFLLPVVCIVVFATSQ------PLPSPQPSQL--------DCWSSLEVIPDCVPEIFRSITNGQFGNVGPSCCHAFIGLD 72
Cdd:PLN00213   7 FLLLAVLCIIVSVNAQlpqfpaQLPFLFPFQLipglpditKCFSSVMDIPGCIAEISQSIFTGKFGNLGPACCKAFLDAD 86

                         90       100
                 ....*....|....*....|....*
gi 18422886   73 TeCIPQMfIFAPLIPPsrRLRDHCS 97
Cdd:PLN00213  87 N-CIPKI-PFIPFFPP--MLKEQCS 107
 
Name Accession Description Interval E-value
PLN00213 PLN00213
predicted protein; Provisional
 7-97 1.62e-13

predicted protein; Provisional


Pssm-ID: 165778  Cd Length: 118  Bit Score: 61.18  E-value: 1.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422886    7 FFLLPVVCIVVFATSQ------PLPSPQPSQL--------DCWSSLEVIPDCVPEIFRSITNGQFGNVGPSCCHAFIGLD 72
Cdd:PLN00213   7 FLLLAVLCIIVSVNAQlpqfpaQLPFLFPFQLipglpditKCFSSVMDIPGCIAEISQSIFTGKFGNLGPACCKAFLDAD 86

                         90       100
                 ....*....|....*....|....*
gi 18422886   73 TeCIPQMfIFAPLIPPsrRLRDHCS 97
Cdd:PLN00213  87 N-CIPKI-PFIPFFPP--MLKEQCS 107
Prolamin_like pfam05617
Prolamin-like; Prolamin_like (in which DUF784 and DUF1278 have been merged) is found to be ...
 33-82 2.70e-11

Prolamin-like; Prolamin_like (in which DUF784 and DUF1278 have been merged) is found to be expressed in the plant embryo sac and to be regulated by the Myb98 transcription factor. Computational analysis has revealed that members are homologous to the plant prolamin superfamily (Protease inhibitor-seed storage-LTP family, pfam00234). In contrast to typical prolamin members that have eight conserved Cys residues forming four pairs of disulfide bonds, this domain contains only six conserved Cys residues that may form three pairs of disulfide bonds. The domain may have a potential function in lipid transfer or protection during plant embryo sac development and reproduction.


Pssm-ID: 461693  Cd Length: 70  Bit Score: 54.37  E-value: 2.70e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 18422886    33 DCWSSLEVIPDCVPEIFRSITNGQFGnVGPSCCHAFIGLDTECIPQMFIF 82
Cdd:pfam05617   1 KCWSKLSELPGCGDEILLFFLDNGEP-VGRECCLAILKIGKDCWPAMFKS 49
 
Name Accession Description Interval E-value
PLN00213 PLN00213
predicted protein; Provisional
 7-97 1.62e-13

predicted protein; Provisional


Pssm-ID: 165778  Cd Length: 118  Bit Score: 61.18  E-value: 1.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422886    7 FFLLPVVCIVVFATSQ------PLPSPQPSQL--------DCWSSLEVIPDCVPEIFRSITNGQFGNVGPSCCHAFIGLD 72
Cdd:PLN00213   7 FLLLAVLCIIVSVNAQlpqfpaQLPFLFPFQLipglpditKCFSSVMDIPGCIAEISQSIFTGKFGNLGPACCKAFLDAD 86

                         90       100
                 ....*....|....*....|....*
gi 18422886   73 TeCIPQMfIFAPLIPPsrRLRDHCS 97
Cdd:PLN00213  87 N-CIPKI-PFIPFFPP--MLKEQCS 107
Prolamin_like pfam05617
Prolamin-like; Prolamin_like (in which DUF784 and DUF1278 have been merged) is found to be ...
 33-82 2.70e-11

Prolamin-like; Prolamin_like (in which DUF784 and DUF1278 have been merged) is found to be expressed in the plant embryo sac and to be regulated by the Myb98 transcription factor. Computational analysis has revealed that members are homologous to the plant prolamin superfamily (Protease inhibitor-seed storage-LTP family, pfam00234). In contrast to typical prolamin members that have eight conserved Cys residues forming four pairs of disulfide bonds, this domain contains only six conserved Cys residues that may form three pairs of disulfide bonds. The domain may have a potential function in lipid transfer or protection during plant embryo sac development and reproduction.


Pssm-ID: 461693  Cd Length: 70  Bit Score: 54.37  E-value: 2.70e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 18422886    33 DCWSSLEVIPDCVPEIFRSITNGQFGnVGPSCCHAFIGLDTECIPQMFIF 82
Cdd:pfam05617   1 KCWSKLSELPGCGDEILLFFLDNGEP-VGRECCLAILKIGKDCWPAMFKS 49
 
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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