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Conserved domains on  [gi|32565452|ref|NP_871690|]
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PID domain-containing protein [Caenorhabditis elegans]

Protein Classification

PTB domain-containing protein( domain architecture ID 10100634)

PTB (phosphotyrosine-binding) domain-containing protein similar to Drosophila melanogaster uncharacterized protein Dmel_CG12581

Gene Ontology:  GO:0005515
PubMed:  15567406|8987385|10610414

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB_CG12581 cd01217
CG12581 Phosphotyrosine-binding (PTB) domain; The function of CG12581 and its related proteins ...
 1-166 2.25e-116

CG12581 Phosphotyrosine-binding (PTB) domain; The function of CG12581 and its related proteins are unknown to date. Members here contain a single N-terminal PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


:

Pssm-ID: 241252  Cd Length: 166  Bit Score: 339.83  E-value: 2.25e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565452   1 MPLPLCRCRVLYIGSSVPTITKDGLQGIQQPLKERYPIQESPDTRGIDSWLSVWSNGVLLEYIEGEKKTETVFFPIITLH 80
Cdd:cd01217   1 DSTPICRCRVLYLGSAVPHITKDGLQGIQEPLRELYPEQGALGARGIDSWLSVWSNGLLLENVDENKKTVTRFFPIESLH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565452  81 YCAAVRYVNVEGFKVGGGGEQFMPLDSPFANIPNSPHPPIFAAIFRRTTGVKVLECHGFICTNVKAANALVRCMVHAYTE 160
Cdd:cd01217  81 YCAAVRYVLVPGFSNGGGGERFLPLDSPFARHPNAQHPPLFAAILRRTTGIKVLECHAFICKREKAANALVRCCFHAYAD 160


                ....*.
gi 32565452 161 TMHLRM 166
Cdd:cd01217 161 SSYAKQ 166
 
Name Accession Description Interval E-value
PTB_CG12581 cd01217
CG12581 Phosphotyrosine-binding (PTB) domain; The function of CG12581 and its related proteins ...
 1-166 2.25e-116

CG12581 Phosphotyrosine-binding (PTB) domain; The function of CG12581 and its related proteins are unknown to date. Members here contain a single N-terminal PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 241252  Cd Length: 166  Bit Score: 339.83  E-value: 2.25e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565452   1 MPLPLCRCRVLYIGSSVPTITKDGLQGIQQPLKERYPIQESPDTRGIDSWLSVWSNGVLLEYIEGEKKTETVFFPIITLH 80
Cdd:cd01217   1 DSTPICRCRVLYLGSAVPHITKDGLQGIQEPLRELYPEQGALGARGIDSWLSVWSNGLLLENVDENKKTVTRFFPIESLH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565452  81 YCAAVRYVNVEGFKVGGGGEQFMPLDSPFANIPNSPHPPIFAAIFRRTTGVKVLECHGFICTNVKAANALVRCMVHAYTE 160
Cdd:cd01217  81 YCAAVRYVLVPGFSNGGGGERFLPLDSPFARHPNAQHPPLFAAILRRTTGIKVLECHAFICKREKAANALVRCCFHAYAD 160


                ....*.
gi 32565452 161 TMHLRM 166
Cdd:cd01217 161 SSYAKQ 166
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 6-171 4.14e-17

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 77.74  E-value: 4.14e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565452      6 CRCRVLYIGSsVPTITKDGLQGIQQPLKE-RYPI-QESPDTRGIDSWLSVWSNGVLLEyiegEKKTETVFFPIITLHYCA 83
Cdd:smart00462   4 VSFRVKYLGS-VEVPEARGLQVVQEAIRKlRAAQgSEKKEPQKVILSISSRGVKLIDE----DTKAVLHEHPLRRISFCA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565452     84 AvryvnvegfkvggggeqfmpldspfanipNSPHPPIFAAIFRRTTGVKvLECHGFICTnvKAANALVRCMVHAYTETMH 163
Cdd:smart00462  79 V-----------------------------GPDDLDVFGYIARDPGSSR-FACHVFRCE--KAAEDIALAIGQAFQLAYE 126


                   ....*...
gi 32565452    164 LRMDERIP 171
Cdd:smart00462 127 LKLKARSE 134
 
Name Accession Description Interval E-value
PTB_CG12581 cd01217
CG12581 Phosphotyrosine-binding (PTB) domain; The function of CG12581 and its related proteins ...
 1-166 2.25e-116

CG12581 Phosphotyrosine-binding (PTB) domain; The function of CG12581 and its related proteins are unknown to date. Members here contain a single N-terminal PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 241252  Cd Length: 166  Bit Score: 339.83  E-value: 2.25e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565452   1 MPLPLCRCRVLYIGSSVPTITKDGLQGIQQPLKERYPIQESPDTRGIDSWLSVWSNGVLLEYIEGEKKTETVFFPIITLH 80
Cdd:cd01217   1 DSTPICRCRVLYLGSAVPHITKDGLQGIQEPLRELYPEQGALGARGIDSWLSVWSNGLLLENVDENKKTVTRFFPIESLH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565452  81 YCAAVRYVNVEGFKVGGGGEQFMPLDSPFANIPNSPHPPIFAAIFRRTTGVKVLECHGFICTNVKAANALVRCMVHAYTE 160
Cdd:cd01217  81 YCAAVRYVLVPGFSNGGGGERFLPLDSPFARHPNAQHPPLFAAILRRTTGIKVLECHAFICKREKAANALVRCCFHAYAD 160


                ....*.
gi 32565452 161 TMHLRM 166
Cdd:cd01217 161 SSYAKQ 166
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 6-171 4.14e-17

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 77.74  E-value: 4.14e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565452      6 CRCRVLYIGSsVPTITKDGLQGIQQPLKE-RYPI-QESPDTRGIDSWLSVWSNGVLLEyiegEKKTETVFFPIITLHYCA 83
Cdd:smart00462   4 VSFRVKYLGS-VEVPEARGLQVVQEAIRKlRAAQgSEKKEPQKVILSISSRGVKLIDE----DTKAVLHEHPLRRISFCA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565452     84 AvryvnvegfkvggggeqfmpldspfanipNSPHPPIFAAIFRRTTGVKvLECHGFICTnvKAANALVRCMVHAYTETMH 163
Cdd:smart00462  79 V-----------------------------GPDDLDVFGYIARDPGSSR-FACHVFRCE--KAAEDIALAIGQAFQLAYE 126


                   ....*...
gi 32565452    164 LRMDERIP 171
Cdd:smart00462 127 LKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 6-154 1.10e-10

Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269911  Cd Length: 120  Bit Score: 59.06  E-value: 1.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565452   6 CRCRVLYIGSsVPTITKDGLQGIQQPLKERYPIQESPDTRGIDSWLSVWSNGVLLeyIEGEKKTETVFFPIITLHYCAAV 85
Cdd:cd00934   1 ASFQVKYLGS-VEVGSSRGVDVVEEALKALAAALKSSKRKPGPVLLEVSSKGVKL--LDLDTKELLLRHPLHRISYCGRD 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32565452  86 RyvnvegfkvggggeqfmpldspfanipnsPHPPIFAAIFRRTTGvKVLECHGFICTNVKAANALVRCM 154
Cdd:cd00934  78 P-----------------------------DNPNVFAFIAGEEGG-SGFRCHVFQCEDEEEAEEILQAI 116
 
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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