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Conserved domains on  [gi|281361671|ref|NP_650222|]
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uncharacterized protein Dmel_CG14395, isoform B [Drosophila melanogaster]

Protein Classification

PH domain-containing protein( domain architecture ID 106840)

Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner

CATH:  2.30.29.30
Gene Ontology:  GO:0005515
PubMed:  22728242|17233582|15493994

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 183-322 2.53e-11

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd01217:

Pssm-ID: 473070  Cd Length: 166  Bit Score: 63.26  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361671  183 LQGLQEPLRQLYLSEvtkkklnsGSLDicATGLRvkiSALAI-SNGAAAP--EENEALITPFHNIAVW---SAVKFVI-- 254
Cdd:cd01217    25 LQGIQEPLRELYPEQ--------GALG--ARGID---SWLSVwSNGLLLEnvDENKKTVTRFFPIESLhycAAVRYVLvp 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361671  255 --SDDDGGAAFLPLITDPENIDKTAlfqplssseqlavehsihvHAPIFAVVMRSASSPKVLECHGFICK 322
Cdd:cd01217    92 gfSNGGGGERFLPLDSPFARHPNAQ-------------------HPPLFAAILRRTTGIKVLECHAFICK 142
 
Name Accession Description Interval E-value
PTB_CG12581 cd01217
CG12581 Phosphotyrosine-binding (PTB) domain; The function of CG12581 and its related proteins ...
 183-322 2.53e-11

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: 63.26  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361671  183 LQGLQEPLRQLYLSEvtkkklnsGSLDicATGLRvkiSALAI-SNGAAAP--EENEALITPFHNIAVW---SAVKFVI-- 254
Cdd:cd01217    25 LQGIQEPLRELYPEQ--------GALG--ARGID---SWLSVwSNGLLLEnvDENKKTVTRFFPIESLhycAAVRYVLvp 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361671  255 --SDDDGGAAFLPLITDPENIDKTAlfqplssseqlavehsihvHAPIFAVVMRSASSPKVLECHGFICK 322
Cdd:cd01217    92 gfSNGGGGERFLPLDSPFARHPNAQ-------------------HPPLFAAILRRTTGIKVLECHAFICK 142
 
Name Accession Description Interval E-value
PTB_CG12581 cd01217
CG12581 Phosphotyrosine-binding (PTB) domain; The function of CG12581 and its related proteins ...
 183-322 2.53e-11

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: 63.26  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361671  183 LQGLQEPLRQLYLSEvtkkklnsGSLDicATGLRvkiSALAI-SNGAAAP--EENEALITPFHNIAVW---SAVKFVI-- 254
Cdd:cd01217    25 LQGIQEPLRELYPEQ--------GALG--ARGID---SWLSVwSNGLLLEnvDENKKTVTRFFPIESLhycAAVRYVLvp 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361671  255 --SDDDGGAAFLPLITDPENIDKTAlfqplssseqlavehsihvHAPIFAVVMRSASSPKVLECHGFICK 322
Cdd:cd01217    92 gfSNGGGGERFLPLDSPFARHPNAQ-------------------HPPLFAAILRRTTGIKVLECHAFICK 142
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
 296-334 8.48e-03

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins Phosphotyrosine-binding (PTB) PH-like fold; The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains a single 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 contains insects, ticks, sea urchins, and nematodes.


Pssm-ID: 269982  Cd Length: 125  Bit Score: 37.70  E-value: 8.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 281361671  296 VHAPIFA--VVMRSASSPKVLECHGFICKSTEDAIVIAATL 334
Cdd:cd13160    81 VHTRVFSmiVVGEQDSSNHPFECHAFVCDSRADARNLTYWL 121
 
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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