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Conserved domains on  [gi|2462547443|ref|XP_054235535|]
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CKLF-like MARVEL transmembrane domain-containing protein 3 isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MARVEL pfam01284
Membrane-associating domain; MARVEL domain-containing proteins are often found in ...
 35-132 1.85e-06

Membrane-associating domain; MARVEL domain-containing proteins are often found in lipid-associating proteins - such as Occludin and MAL family proteins. It may be part of the machinery of membrane apposition events, such as transport vesicle biogenesis.


:

Pssm-ID: 366555  Cd Length: 136  Bit Score: 45.01  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547443  35 SFITFICYVASSASAFLTAPLLEFLLALYFLFADaMQLNDKWQGLCWPMMDFLRCVTAALIYFAISITAIAKYSD----- 109
Cdd:pfam01284  26 SLIAYAGSYPSAVNFAVFVAVFSFLIALFFLLLY-LFGYSYFPSIAWPLIDLIFDALAALFWLAAFIALAAALRGhsenq 104

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462547443 110 ---------GASKAAGVFGFFATIVFATDFYL 132
Cdd:pfam01284 105 gsgdltrrcRAAQAAIAFGFFAWLLFLASAVL 136
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 7-32 1.67e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


:

Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.16  E-value: 1.67e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462547443   7 EPGAPALSGPRGL-------GQLGPPGLPGRSG 32
Cdd:pfam01391  20 PPGPPGPPGPPGEpgppgppGPPGPPGPPGAPG 52
 
Name Accession Description Interval E-value
MARVEL pfam01284
Membrane-associating domain; MARVEL domain-containing proteins are often found in ...
 35-132 1.85e-06

Membrane-associating domain; MARVEL domain-containing proteins are often found in lipid-associating proteins - such as Occludin and MAL family proteins. It may be part of the machinery of membrane apposition events, such as transport vesicle biogenesis.


Pssm-ID: 366555  Cd Length: 136  Bit Score: 45.01  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547443  35 SFITFICYVASSASAFLTAPLLEFLLALYFLFADaMQLNDKWQGLCWPMMDFLRCVTAALIYFAISITAIAKYSD----- 109
Cdd:pfam01284  26 SLIAYAGSYPSAVNFAVFVAVFSFLIALFFLLLY-LFGYSYFPSIAWPLIDLIFDALAALFWLAAFIALAAALRGhsenq 104

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462547443 110 ---------GASKAAGVFGFFATIVFATDFYL 132
Cdd:pfam01284 105 gsgdltrrcRAAQAAIAFGFFAWLLFLASAVL 136
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 7-32 1.67e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.16  E-value: 1.67e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462547443   7 EPGAPALSGPRGL-------GQLGPPGLPGRSG 32
Cdd:pfam01391  20 PPGPPGPPGPPGEpgppgppGPPGPPGPPGAPG 52
 
Name Accession Description Interval E-value
MARVEL pfam01284
Membrane-associating domain; MARVEL domain-containing proteins are often found in ...
 35-132 1.85e-06

Membrane-associating domain; MARVEL domain-containing proteins are often found in lipid-associating proteins - such as Occludin and MAL family proteins. It may be part of the machinery of membrane apposition events, such as transport vesicle biogenesis.


Pssm-ID: 366555  Cd Length: 136  Bit Score: 45.01  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547443  35 SFITFICYVASSASAFLTAPLLEFLLALYFLFADaMQLNDKWQGLCWPMMDFLRCVTAALIYFAISITAIAKYSD----- 109
Cdd:pfam01284  26 SLIAYAGSYPSAVNFAVFVAVFSFLIALFFLLLY-LFGYSYFPSIAWPLIDLIFDALAALFWLAAFIALAAALRGhsenq 104

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462547443 110 ---------GASKAAGVFGFFATIVFATDFYL 132
Cdd:pfam01284 105 gsgdltrrcRAAQAAIAFGFFAWLLFLASAVL 136
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 7-32 1.67e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.16  E-value: 1.67e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462547443   7 EPGAPALSGPRGL-------GQLGPPGLPGRSG 32
Cdd:pfam01391  20 PPGPPGPPGPPGEpgppgppGPPGPPGPPGAPG 52
 
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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