NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|665390042|ref|NP_001284964|]
View 

shifted, isoform C [Drosophila melanogaster]

Protein Classification

RYK family tyrosine-protein kinase( domain architecture ID 10488361)

RYK family tyrosine-protein kinase contains an extracellular Wnt-inhibitory factor-1 like domain, a transmembrane segment, and an intracellular tyr kinase domain that may be inactive or may catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
WIF super family cl02623
WIF domain; The WIF domain is found in the RYK tyrosine kinase receptors and WIF, the ...
 120-258 1.30e-39

WIF domain; The WIF domain is found in the RYK tyrosine kinase receptors and WIF, the Wnt-inhibitory- factor. The domain is extracellular and contains two conserved cysteines that may form a disulphide bridge. This domain is Wnt binding in WIF, and it has been suggested that RYK may also bind to Wnt. The WIF domain is a member of the immunoglobulin superfamily, and it comprises nine beta-strands and two alpha-helices, with two of the beta-strands (6 and 9) interrupted by four and six residues of irregular secondary structure, respectively. Considering that the activity of Wnts depends on the presence of a palmitoylated cysteine residue in their amino-terminal polypeptide segment, Wnt proteins are lipid-modified and can act as stem cell growth factors, it is likely that the WIF domain recognizes and binds to Wnts that have been activated by palmitoylation and that the recognition of palmitoylated Wnts by WIF-1 is effected by its WIF domain rather than by its EGF domains. A strong binding affinity for palmitoylated cysteine residues would further explain the remarkably high affinity of human WIF-1 not only for mammalian Wnts, but also for Wnts from Xenopus and Drosophila.


The actual alignment was detected with superfamily member pfam02019:

Pssm-ID: 470637  Cd Length: 126  Bit Score: 138.51  E-value: 1.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390042  120 WINEQQLKMLTalyfpqGYSERLYAIHNSRVTNDLRDttlynFLV-IPSEVNYVNFTWKSG-RRKYFYDFdRLQTMDESI 197
Cdd:pfam02019   1 YIDEQEVKRLL------GLEAELYYVREGIVNPYALD-----FLPpVPSEVNSLNFTWKSGgKKKVPYSF-SLESDDESI 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665390042  198 LKAPTLSIRKSGRIPQEQKNFSIFLPCTGNSSGTASFNVGLKIQTrhNKPLSGTPirLNFK 258
Cdd:pfam02019  69 LNPPTLNISLKGTVPREPSVFSVLLPCSGNRSGEATVSIQLNITI--GSSLNGTP--LNLK 125
 
Name Accession Description Interval E-value
WIF pfam02019
WIF domain; The WIF domain is found in the RYK tyrosine kinase receptors and WIF, the ...
 120-258 1.30e-39

WIF domain; The WIF domain is found in the RYK tyrosine kinase receptors and WIF, the Wnt-inhibitory- factor. The domain is extracellular and contains two conserved cysteines that may form a disulphide bridge. This domain is Wnt binding in WIF, and it has been suggested that RYK may also bind to Wnt. The WIF domain is a member of the immunoglobulin superfamily, and it comprises nine beta-strands and two alpha-helices, with two of the beta-strands (6 and 9) interrupted by four and six residues of irregular secondary structure, respectively. Considering that the activity of Wnts depends on the presence of a palmitoylated cysteine residue in their amino-terminal polypeptide segment, Wnt proteins are lipid-modified and can act as stem cell growth factors, it is likely that the WIF domain recognizes and binds to Wnts that have been activated by palmitoylation and that the recognition of palmitoylated Wnts by WIF-1 is effected by its WIF domain rather than by its EGF domains. A strong binding affinity for palmitoylated cysteine residues would further explain the remarkably high affinity of human WIF-1 not only for mammalian Wnts, but also for Wnts from Xenopus and Drosophila.


Pssm-ID: 460414  Cd Length: 126  Bit Score: 138.51  E-value: 1.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390042  120 WINEQQLKMLTalyfpqGYSERLYAIHNSRVTNDLRDttlynFLV-IPSEVNYVNFTWKSG-RRKYFYDFdRLQTMDESI 197
Cdd:pfam02019   1 YIDEQEVKRLL------GLEAELYYVREGIVNPYALD-----FLPpVPSEVNSLNFTWKSGgKKKVPYSF-SLESDDESI 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665390042  198 LKAPTLSIRKSGRIPQEQKNFSIFLPCTGNSSGTASFNVGLKIQTrhNKPLSGTPirLNFK 258
Cdd:pfam02019  69 LNPPTLNISLKGTVPREPSVFSVLLPCSGNRSGEATVSIQLNITI--GSSLNGTP--LNLK 125
WIF smart00469
Wnt-inhibitory factor-1 like domain; Occurs as extracellular domain in metazoan Ryk receptor ...
 117-262 1.52e-17

Wnt-inhibitory factor-1 like domain; Occurs as extracellular domain in metazoan Ryk receptor tyrosine kinases. C. elegans Ryk is required for cell-cuticle recognition. WIF-1 binds to Wnt and inhibits its activity.


Pssm-ID: 128745  Cd Length: 136  Bit Score: 78.68  E-value: 1.52e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390042   117 ISLWINEQQLKMLTalyfpqGYSERLYAIHNSRVTNdlrdtTLYNFLV-IPSEVNYVNFTWKSGRRKYFYDFDRLQTMDE 195
Cdd:smart00469   2 LNLFLSAHEVRRLI------GVSAELYYVREGKISP-----YALNFMVpVPANIHDLSFTWQALGQEYVPYSLNVRSDDK 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665390042   196 SILKAPTLSIRKSGRIPQEQKNFSIFLPCTGNSSgtASFNVGLKIQTRHNKPLSGTPIRLNFKKECA 262
Cdd:smart00469  71 EVLPRPIVNISLLGTVPHTLQVFQVELKCSGKRD--AEVEVTVIVEVSLGSTKNPTPLNFRRKKICL 135
 
Name Accession Description Interval E-value
WIF pfam02019
WIF domain; The WIF domain is found in the RYK tyrosine kinase receptors and WIF, the ...
 120-258 1.30e-39

WIF domain; The WIF domain is found in the RYK tyrosine kinase receptors and WIF, the Wnt-inhibitory- factor. The domain is extracellular and contains two conserved cysteines that may form a disulphide bridge. This domain is Wnt binding in WIF, and it has been suggested that RYK may also bind to Wnt. The WIF domain is a member of the immunoglobulin superfamily, and it comprises nine beta-strands and two alpha-helices, with two of the beta-strands (6 and 9) interrupted by four and six residues of irregular secondary structure, respectively. Considering that the activity of Wnts depends on the presence of a palmitoylated cysteine residue in their amino-terminal polypeptide segment, Wnt proteins are lipid-modified and can act as stem cell growth factors, it is likely that the WIF domain recognizes and binds to Wnts that have been activated by palmitoylation and that the recognition of palmitoylated Wnts by WIF-1 is effected by its WIF domain rather than by its EGF domains. A strong binding affinity for palmitoylated cysteine residues would further explain the remarkably high affinity of human WIF-1 not only for mammalian Wnts, but also for Wnts from Xenopus and Drosophila.


Pssm-ID: 460414  Cd Length: 126  Bit Score: 138.51  E-value: 1.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390042  120 WINEQQLKMLTalyfpqGYSERLYAIHNSRVTNDLRDttlynFLV-IPSEVNYVNFTWKSG-RRKYFYDFdRLQTMDESI 197
Cdd:pfam02019   1 YIDEQEVKRLL------GLEAELYYVREGIVNPYALD-----FLPpVPSEVNSLNFTWKSGgKKKVPYSF-SLESDDESI 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665390042  198 LKAPTLSIRKSGRIPQEQKNFSIFLPCTGNSSGTASFNVGLKIQTrhNKPLSGTPirLNFK 258
Cdd:pfam02019  69 LNPPTLNISLKGTVPREPSVFSVLLPCSGNRSGEATVSIQLNITI--GSSLNGTP--LNLK 125
WIF smart00469
Wnt-inhibitory factor-1 like domain; Occurs as extracellular domain in metazoan Ryk receptor ...
 117-262 1.52e-17

Wnt-inhibitory factor-1 like domain; Occurs as extracellular domain in metazoan Ryk receptor tyrosine kinases. C. elegans Ryk is required for cell-cuticle recognition. WIF-1 binds to Wnt and inhibits its activity.


Pssm-ID: 128745  Cd Length: 136  Bit Score: 78.68  E-value: 1.52e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390042   117 ISLWINEQQLKMLTalyfpqGYSERLYAIHNSRVTNdlrdtTLYNFLV-IPSEVNYVNFTWKSGRRKYFYDFDRLQTMDE 195
Cdd:smart00469   2 LNLFLSAHEVRRLI------GVSAELYYVREGKISP-----YALNFMVpVPANIHDLSFTWQALGQEYVPYSLNVRSDDK 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665390042   196 SILKAPTLSIRKSGRIPQEQKNFSIFLPCTGNSSgtASFNVGLKIQTRHNKPLSGTPIRLNFKKECA 262
Cdd:smart00469  71 EVLPRPIVNISLLGTVPHTLQVFQVELKCSGKRD--AEVEVTVIVEVSLGSTKNPTPLNFRRKKICL 135
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH