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Conserved domains on  [gi|442633952|ref|NP_001262166|]
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M6, isoform F [Drosophila melanogaster]

Protein Classification

myelin proteolipid family protein( domain architecture ID 10472648)

myelin proteolipid family protein similar to human myelin proteolipid protein (PLP) that plays an important role in the formation or maintenance of the multilamellar structure of myelin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Myelin_PLP pfam01275
Myelin proteolipid protein (PLP or lipophilin);
122-345 4.35e-106

Myelin proteolipid protein (PLP or lipophilin);


:

Pssm-ID: 460144  Cd Length: 231  Bit Score: 311.15  E-value: 4.35e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633952  122 GECCQSCMARIPYATLIATLMCLLGVGIFCFTMYRGASLTVIMVDQVFH-------LRLIWIEAVQMIFVIIGAGMAALG 194
Cdd:pfam01275   1 YDCCVRCLGRVPYASLIATILCFAGVALFCGCGHRALTLTVLMLETVFHrnyqdyeLLATWIDAFQYVIYGIAAFFFLLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633952  195 FMILFVGFLATGATRyKVYRAWRSRVGGRISCAVLMGITYLLNFVWSLILCFLVVVTFIYTMFWNMCTSV---EHSQSCI 271
Cdd:pfam01275  81 LLLLAEGFLTTGATK-QVYGAFRSTVGGRCSCAVFMGITYVLALVWLLVFAFLAIPVFIFTNFWSTCQNInvlSTNQLCI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442633952  272 DLTQFHFMFPPNTkleDMKVCEKYEIKAFCKDGVENAEV-MFILATLSTLLVLLSLVHYLMCLSANYAHIRDHEK 345
Cdd:pfam01275 160 DFRQFGFLPWNAT---PGKVCGMTELKAFCKDYEEKMTFhLFILAFAGAGATLLALVHYLMCLTANYAHLRDHGR 231
 
Name Accession Description Interval E-value
Myelin_PLP pfam01275
Myelin proteolipid protein (PLP or lipophilin);
122-345 4.35e-106

Myelin proteolipid protein (PLP or lipophilin);


Pssm-ID: 460144  Cd Length: 231  Bit Score: 311.15  E-value: 4.35e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633952  122 GECCQSCMARIPYATLIATLMCLLGVGIFCFTMYRGASLTVIMVDQVFH-------LRLIWIEAVQMIFVIIGAGMAALG 194
Cdd:pfam01275   1 YDCCVRCLGRVPYASLIATILCFAGVALFCGCGHRALTLTVLMLETVFHrnyqdyeLLATWIDAFQYVIYGIAAFFFLLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633952  195 FMILFVGFLATGATRyKVYRAWRSRVGGRISCAVLMGITYLLNFVWSLILCFLVVVTFIYTMFWNMCTSV---EHSQSCI 271
Cdd:pfam01275  81 LLLLAEGFLTTGATK-QVYGAFRSTVGGRCSCAVFMGITYVLALVWLLVFAFLAIPVFIFTNFWSTCQNInvlSTNQLCI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442633952  272 DLTQFHFMFPPNTkleDMKVCEKYEIKAFCKDGVENAEV-MFILATLSTLLVLLSLVHYLMCLSANYAHIRDHEK 345
Cdd:pfam01275 160 DFRQFGFLPWNAT---PGKVCGMTELKAFCKDYEEKMTFhLFILAFAGAGATLLALVHYLMCLTANYAHLRDHGR 231
TM_ABC_iron-siderophores_like cd06550
Transmembrane subunit (TM), of Periplasmic Binding Protein (PBP)-dependent ATP-Binding ...
 129-254 1.88e-03

Transmembrane subunit (TM), of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters involved in the uptake of siderophores, heme, vitamin B12, or the divalent cations Mg2+ and Zn2+. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The TMs are bundles of alpha helices that transverse the cytoplasmic membrane multiple times. The two ABCs bind and hydrolyze ATP and drive the transport reaction. Each TM has a prominent cytoplasmic loop which contacts an ABC and represents a conserved motif. The two TMs form either a homodimer (e.g. in the case of the BtuC subunits of the Escherichia coli BtuCD vitamin B12 transporter), a heterodimer (e.g. the TroC and TroD subunits of the Treponema pallidum general transition metal transporter, TroBCD), or a pseudo-heterodimer (e.g. the FhuB protein of the E. coli ferrichrome transporter, FhuBC). FhuB contains two tandem TMs which associate to form the pseudo-heterodimer. Both FhuB TMs are found in this hierarchy.


Pssm-ID: 119348 [Multi-domain]  Cd Length: 261  Bit Score: 39.46  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633952 129 MARIPYATLIATLMCLLGVGIFCFTMYRgaSLTVIMVDQVF----HLRLIWIEAVQMIFV--IIGAGMAALGfMILFVGF 202
Cdd:cd06550  123 ILGVTWEDLLILLIILLLVLLLLLLLSR--KLNLLTFDEDLakslGINVNLLRLLLLLLValLVVAAVALVG-VILFVGL 199

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442633952 203 LATGATRykvyRAWRSRVGGRISCAVLMGITyllnfvwSLILCFLVVVTFIY 254
Cdd:cd06550  200 IAPHLAR----RLFGRSHRYLLPLSALLGAI-------LLLLGDLLSRTLLP 240
 
Name Accession Description Interval E-value
Myelin_PLP pfam01275
Myelin proteolipid protein (PLP or lipophilin);
122-345 4.35e-106

Myelin proteolipid protein (PLP or lipophilin);


Pssm-ID: 460144  Cd Length: 231  Bit Score: 311.15  E-value: 4.35e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633952  122 GECCQSCMARIPYATLIATLMCLLGVGIFCFTMYRGASLTVIMVDQVFH-------LRLIWIEAVQMIFVIIGAGMAALG 194
Cdd:pfam01275   1 YDCCVRCLGRVPYASLIATILCFAGVALFCGCGHRALTLTVLMLETVFHrnyqdyeLLATWIDAFQYVIYGIAAFFFLLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633952  195 FMILFVGFLATGATRyKVYRAWRSRVGGRISCAVLMGITYLLNFVWSLILCFLVVVTFIYTMFWNMCTSV---EHSQSCI 271
Cdd:pfam01275  81 LLLLAEGFLTTGATK-QVYGAFRSTVGGRCSCAVFMGITYVLALVWLLVFAFLAIPVFIFTNFWSTCQNInvlSTNQLCI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442633952  272 DLTQFHFMFPPNTkleDMKVCEKYEIKAFCKDGVENAEV-MFILATLSTLLVLLSLVHYLMCLSANYAHIRDHEK 345
Cdd:pfam01275 160 DFRQFGFLPWNAT---PGKVCGMTELKAFCKDYEEKMTFhLFILAFAGAGATLLALVHYLMCLTANYAHLRDHGR 231
TM_ABC_iron-siderophores_like cd06550
Transmembrane subunit (TM), of Periplasmic Binding Protein (PBP)-dependent ATP-Binding ...
 129-254 1.88e-03

Transmembrane subunit (TM), of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters involved in the uptake of siderophores, heme, vitamin B12, or the divalent cations Mg2+ and Zn2+. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The TMs are bundles of alpha helices that transverse the cytoplasmic membrane multiple times. The two ABCs bind and hydrolyze ATP and drive the transport reaction. Each TM has a prominent cytoplasmic loop which contacts an ABC and represents a conserved motif. The two TMs form either a homodimer (e.g. in the case of the BtuC subunits of the Escherichia coli BtuCD vitamin B12 transporter), a heterodimer (e.g. the TroC and TroD subunits of the Treponema pallidum general transition metal transporter, TroBCD), or a pseudo-heterodimer (e.g. the FhuB protein of the E. coli ferrichrome transporter, FhuBC). FhuB contains two tandem TMs which associate to form the pseudo-heterodimer. Both FhuB TMs are found in this hierarchy.


Pssm-ID: 119348 [Multi-domain]  Cd Length: 261  Bit Score: 39.46  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633952 129 MARIPYATLIATLMCLLGVGIFCFTMYRgaSLTVIMVDQVF----HLRLIWIEAVQMIFV--IIGAGMAALGfMILFVGF 202
Cdd:cd06550  123 ILGVTWEDLLILLIILLLVLLLLLLLSR--KLNLLTFDEDLakslGINVNLLRLLLLLLValLVVAAVALVG-VILFVGL 199

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442633952 203 LATGATRykvyRAWRSRVGGRISCAVLMGITyllnfvwSLILCFLVVVTFIY 254
Cdd:cd06550  200 IAPHLAR----RLFGRSHRYLLPLSALLGAI-------LLLLGDLLSRTLLP 240
 
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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