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Conserved domains on  [gi|398365299|ref|NP_014775|]
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retromer subunit VPS17 [Saccharomyces cerevisiae S288C]

Protein Classification

vacuolar protein sorting-associated protein 17( domain architecture ID 10160867)

vacuolar protein sorting-associated protein 17 (Vps17p) is a membrane-associated protein required for the sorting of soluble vacuolar hydrolases; it contains PX (Phox homology) and BAR (Bin/Amphiphysin/Rvs) domains

Gene Symbol:  VPS17
Gene Ontology:  GO:0140090|GO:0030904
PubMed:  8416961|16782399|11884510|15649145

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR_Vps17p cd07625
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps17p; BAR domains are ...
 239-462 4.14e-137

The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps17p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Vsp17p forms a dimer with Vps5p, the yeast counterpart of human SNX1, and is part of the retromer complex that mediates the transport of the carboxypeptidase Y receptor Vps10p from endosomes to Golgi. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


:

Pssm-ID: 153309  Cd Length: 230  Bit Score: 396.75  E-value: 4.14e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299 239 GLKRKTLKQLAPPYDEITELAEFRPLVKSIYVVSQSLQEKLLRVSRNRKMMVQEENAFGQDFVNLDEHNK------LYRR 312
Cdd:cd07625    1 GLKRKTLKQFAPPYDEYTELAEFRPLVKSIYLTAQDLQEKLLRVSKARKQLSLEEADFGQKLIQLSVEEThhglgnLYEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299 313 YGKILTAVGDIDSIIATMDMATLYDGLEWIVRDAYAVKEALTNRHFIMRNLVQAQQNSKAKQEQARRFRSRRDINPMKID 392
Cdd:cd07625   81 FGKVLTAVGDIDSIQATVDMATLYDGLEWISRDAYVVKEALTNRHLLMRELIQAQQNTKSKQEAARRLKAKRDINPLKVD 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299 393 EALRQLKAAAKNEQVLTLKLQRITSNMIIERKQWISWYEEWIRSSIKEFTLRKIEYERKKLTLLERVRSD 462
Cdd:cd07625  161 EAIRQLEEATKHEHDLSLKLKRITGNMLIERKEWTDWTEEDLQSAIREYTLRKIEYERKKLSLLERIRLD 230
PX_Vps17p cd06891
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps17p; The PX domain ...
 85-223 1.04e-64

The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps17p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Vsp17p forms a dimer with Vps5p, the yeast counterpart of human SNX1, and is part of the retromer complex that mediates the transport of the carboxypeptidase Y receptor Vps10p from endosomes to Golgi. Similar to Vps5p and SNX1, Vps17p harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX-BAR structural unit helps determine specific membrane localization.


:

Pssm-ID: 132801  Cd Length: 140  Bit Score: 207.20  E-value: 1.04e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299  85 QQPSQPSERVILP------ERSDEKKKYTLLAKVTGLERFGSatgkkENPTIIFDCSTNLPTFRKQQYKNVKKSYEEFHQ 158
Cdd:cd06891    1 EQPSQPESRKILTsnrrelEPERKKPKYFLRVRVTGIERNKS-----KDPIIRFDVTTNLPTFRSSTYKDVRRTYEEFQK 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365299 159 LFKYLNVAIQESFVPTLPSAYTTFGINSEEDRMKVTRNFQLWFNRLSQDPLIIRNEEVAFFIESD 223
Cdd:cd06891   76 LFKYLNGANPETFVPALPLPSTSYGSNNEEDARKLKANLQRWFNRVCSDPILIRDEELRFFIESD 140
 
Name Accession Description Interval E-value
BAR_Vps17p cd07625
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps17p; BAR domains are ...
 239-462 4.14e-137

The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps17p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Vsp17p forms a dimer with Vps5p, the yeast counterpart of human SNX1, and is part of the retromer complex that mediates the transport of the carboxypeptidase Y receptor Vps10p from endosomes to Golgi. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153309  Cd Length: 230  Bit Score: 396.75  E-value: 4.14e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299 239 GLKRKTLKQLAPPYDEITELAEFRPLVKSIYVVSQSLQEKLLRVSRNRKMMVQEENAFGQDFVNLDEHNK------LYRR 312
Cdd:cd07625    1 GLKRKTLKQFAPPYDEYTELAEFRPLVKSIYLTAQDLQEKLLRVSKARKQLSLEEADFGQKLIQLSVEEThhglgnLYEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299 313 YGKILTAVGDIDSIIATMDMATLYDGLEWIVRDAYAVKEALTNRHFIMRNLVQAQQNSKAKQEQARRFRSRRDINPMKID 392
Cdd:cd07625   81 FGKVLTAVGDIDSIQATVDMATLYDGLEWISRDAYVVKEALTNRHLLMRELIQAQQNTKSKQEAARRLKAKRDINPLKVD 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299 393 EALRQLKAAAKNEQVLTLKLQRITSNMIIERKQWISWYEEWIRSSIKEFTLRKIEYERKKLTLLERVRSD 462
Cdd:cd07625  161 EAIRQLEEATKHEHDLSLKLKRITGNMLIERKEWTDWTEEDLQSAIREYTLRKIEYERKKLSLLERIRLD 230
PX_Vps17p cd06891
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps17p; The PX domain ...
 85-223 1.04e-64

The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps17p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Vsp17p forms a dimer with Vps5p, the yeast counterpart of human SNX1, and is part of the retromer complex that mediates the transport of the carboxypeptidase Y receptor Vps10p from endosomes to Golgi. Similar to Vps5p and SNX1, Vps17p harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX-BAR structural unit helps determine specific membrane localization.


Pssm-ID: 132801  Cd Length: 140  Bit Score: 207.20  E-value: 1.04e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299  85 QQPSQPSERVILP------ERSDEKKKYTLLAKVTGLERFGSatgkkENPTIIFDCSTNLPTFRKQQYKNVKKSYEEFHQ 158
Cdd:cd06891    1 EQPSQPESRKILTsnrrelEPERKKPKYFLRVRVTGIERNKS-----KDPIIRFDVTTNLPTFRSSTYKDVRRTYEEFQK 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365299 159 LFKYLNVAIQESFVPTLPSAYTTFGINSEEDRMKVTRNFQLWFNRLSQDPLIIRNEEVAFFIESD 223
Cdd:cd06891   76 LFKYLNGANPETFVPALPLPSTSYGSNNEEDARKLKANLQRWFNRVCSDPILIRDEELRFFIESD 140
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 139-223 5.48e-13

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 64.57  E-value: 5.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299  139 PTFRKQQYKNVKKSYEEFHQLFKYLNVAIQESFVPTLPSAYTTFGINSE--EDRMKvtrNFQLWFNRLSQDPLIIRNEEV 216
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEfiEKRRK---GLEQYLQRLLQHPELRNSEVL 77


                  ....*..
gi 398365299  217 AFFIESD 223
Cdd:pfam00787  78 LEFLESD 84
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 123-221 3.72e-12

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 62.75  E-value: 3.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299   123 GKKENPTIIFDCSTNLPTfrkqQYKNVKKSYEEFHQLFKYLNVAIQESFVPTLPSAYT--TFGINSEEDRMKVTRNFQLW 200
Cdd:smart00312   8 GDGKHYYYVIEIETKTGL----EEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLfgRLNNFSEEFIEKRRRGLEKY 83

                           90       100
                   ....*....|....*....|..
gi 398365299   201 FNRLSQDPLIIRN-EEVAFFIE 221
Cdd:smart00312  84 LQSLLNHPELINHsEVVLEFLE 105
 
Name Accession Description Interval E-value
BAR_Vps17p cd07625
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps17p; BAR domains are ...
 239-462 4.14e-137

The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps17p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Vsp17p forms a dimer with Vps5p, the yeast counterpart of human SNX1, and is part of the retromer complex that mediates the transport of the carboxypeptidase Y receptor Vps10p from endosomes to Golgi. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153309  Cd Length: 230  Bit Score: 396.75  E-value: 4.14e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299 239 GLKRKTLKQLAPPYDEITELAEFRPLVKSIYVVSQSLQEKLLRVSRNRKMMVQEENAFGQDFVNLDEHNK------LYRR 312
Cdd:cd07625    1 GLKRKTLKQFAPPYDEYTELAEFRPLVKSIYLTAQDLQEKLLRVSKARKQLSLEEADFGQKLIQLSVEEThhglgnLYEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299 313 YGKILTAVGDIDSIIATMDMATLYDGLEWIVRDAYAVKEALTNRHFIMRNLVQAQQNSKAKQEQARRFRSRRDINPMKID 392
Cdd:cd07625   81 FGKVLTAVGDIDSIQATVDMATLYDGLEWISRDAYVVKEALTNRHLLMRELIQAQQNTKSKQEAARRLKAKRDINPLKVD 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299 393 EALRQLKAAAKNEQVLTLKLQRITSNMIIERKQWISWYEEWIRSSIKEFTLRKIEYERKKLTLLERVRSD 462
Cdd:cd07625  161 EAIRQLEEATKHEHDLSLKLKRITGNMLIERKEWTDWTEEDLQSAIREYTLRKIEYERKKLSLLERIRLD 230
PX_Vps17p cd06891
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps17p; The PX domain ...
 85-223 1.04e-64

The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps17p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Vsp17p forms a dimer with Vps5p, the yeast counterpart of human SNX1, and is part of the retromer complex that mediates the transport of the carboxypeptidase Y receptor Vps10p from endosomes to Golgi. Similar to Vps5p and SNX1, Vps17p harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX-BAR structural unit helps determine specific membrane localization.


Pssm-ID: 132801  Cd Length: 140  Bit Score: 207.20  E-value: 1.04e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299  85 QQPSQPSERVILP------ERSDEKKKYTLLAKVTGLERFGSatgkkENPTIIFDCSTNLPTFRKQQYKNVKKSYEEFHQ 158
Cdd:cd06891    1 EQPSQPESRKILTsnrrelEPERKKPKYFLRVRVTGIERNKS-----KDPIIRFDVTTNLPTFRSSTYKDVRRTYEEFQK 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365299 159 LFKYLNVAIQESFVPTLPSAYTTFGINSEEDRMKVTRNFQLWFNRLSQDPLIIRNEEVAFFIESD 223
Cdd:cd06891   76 LFKYLNGANPETFVPALPLPSTSYGSNNEEDARKLKANLQRWFNRVCSDPILIRDEELRFFIESD 140
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 139-223 5.48e-13

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 64.57  E-value: 5.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299  139 PTFRKQQYKNVKKSYEEFHQLFKYLNVAIQESFVPTLPSAYTTFGINSE--EDRMKvtrNFQLWFNRLSQDPLIIRNEEV 216
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEfiEKRRK---GLEQYLQRLLQHPELRNSEVL 77


                  ....*..
gi 398365299  217 AFFIESD 223
Cdd:pfam00787  78 LEFLESD 84
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 123-221 3.72e-12

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 62.75  E-value: 3.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299   123 GKKENPTIIFDCSTNLPTfrkqQYKNVKKSYEEFHQLFKYLNVAIQESFVPTLPSAYT--TFGINSEEDRMKVTRNFQLW 200
Cdd:smart00312   8 GDGKHYYYVIEIETKTGL----EEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLfgRLNNFSEEFIEKRRRGLEKY 83

                           90       100
                   ....*....|....*....|..
gi 398365299   201 FNRLSQDPLIIRN-EEVAFFIE 221
Cdd:smart00312  84 LQSLLNHPELINHsEVVLEFLE 105
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 140-222 2.11e-09

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


Pssm-ID: 132768 [Multi-domain]  Cd Length: 106  Bit Score: 55.06  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299 140 TFRKQQYKNVKKSYEEFHQLFKYLNVAIQESFVPTLPSAyTTFGINSEEDRMKVTRNFQLWFNRLSQDPLIIRNEEVAFF 219
Cdd:cd06093   25 TTQGGEEWTVYRRYSDFEELHEKLKKKFPGVILPPLPPK-KLFGNLDPEFIEERRKQLEQYLQSLLNHPELRNSEELKEF 103


                 ...
gi 398365299 220 IES 222
Cdd:cd06093  104 LEL 106
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 331-462 4.25e-06

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 47.74  E-value: 4.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299 331 DMATLYDGLEWIVRDAYAVKEALTNRHFIMRNLVQAQQNSKAKQEQARRFRSRRDINPMKIDEALRQLKAAAKNEQVLTL 410
Cdd:cd07596   87 ELVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAESALEEARK 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 398365299 411 KLQRITSNMIIERKQWISWYEEWIRSSIKEFTLRKIEYERKKLTLLERVRSD 462
Cdd:cd07596  167 RYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAEAWESLLPE 218
PX_Atg24p cd06863
The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation ...
 136-222 9.62e-03

The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation protein; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The yeast Atg24p is a sorting nexin (SNX) which is involved in membrane fusion events at the vacuolar surface during pexophagy. This is facilitated via binding of Atg24p to phosphatidylinositol 3-phosphate (PI3P) through its PX domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132773  Cd Length: 118  Bit Score: 36.11  E-value: 9.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365299 136 TNLPTFRKQQYKnVKKSYEEFHQLFKYLNVAIQESFVPTLPS----AYTTFGINSEEDRMKVTRNFQLWFNRLSQDPLII 211
Cdd:cd06863   28 TNLPSFSRKEFK-VRRRYSDFVFLHECLSNDFPACVVPPLPDkhrlEYITGDRFSPEFITRRAQSLQRFLRRISLHPVLS 106

                         90
                 ....*....|.
gi 398365299 212 RNEEVAFFIES 222
Cdd:cd06863  107 QSKILHQFLES 117
 
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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