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Conserved domains on  [gi|212506821|gb|EEB10923|]
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fam43, putative [Pediculus humanus corporis]

Protein Classification

FAM43A/B family PTB domain-containing protein( domain architecture ID 10631605)

FAM43A/B family (phosphotyrosine-binding) domain-containing protein similar to mammalian proteins FAM43A and FAM43B

CATH:  2.30.29.30
Gene Ontology:  GO:0005515
PubMed:  15567406|8987385|10610414
SCOP:  4002427

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
15-198 1.98e-114

Phosphotyrosine interaction domain (PTB/PID);


:

Pssm-ID: 405418  Cd Length: 184  Bit Score: 332.50  E-value: 1.98e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212506821   15 TYKVSYLGNVLTGLAKGEGCIEKPLNTLWKNYNESlKPSIQMKIKVTQSGLKAVTKDHGLIEYWSHRITFCTVPPEFPNI 94
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQG-KSGTKMKLTVTRSGLKATTKEHGLTEYWSHRITYCSAPPNYPRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212506821   95 FCWIYRHEGRKLKQELRCHAVLCSKESVASKMSDTLKTRLTQALVEFKRDKLLR---QNARLSLVNSVYDNPSLPKRKIL 171
Cdd:pfam14719  80 FCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLCArhaQNARLSLGNAAYDPPSVPRRKLL 159

                         170       180
                  ....*....|....*....|....*..
gi 212506821  172 LSTgcHNYKPPIERSKSAPKLMKVSDD 198
Cdd:pfam14719 160 TGT--CNYRPPVERSKSAPKLGSITEE 184
 
Name Accession Description Interval E-value
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
15-198 1.98e-114

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 332.50  E-value: 1.98e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212506821   15 TYKVSYLGNVLTGLAKGEGCIEKPLNTLWKNYNESlKPSIQMKIKVTQSGLKAVTKDHGLIEYWSHRITFCTVPPEFPNI 94
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQG-KSGTKMKLTVTRSGLKATTKEHGLTEYWSHRITYCSAPPNYPRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212506821   95 FCWIYRHEGRKLKQELRCHAVLCSKESVASKMSDTLKTRLTQALVEFKRDKLLR---QNARLSLVNSVYDNPSLPKRKIL 171
Cdd:pfam14719  80 FCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLCArhaQNARLSLGNAAYDPPSVPRRKLL 159

                         170       180
                  ....*....|....*....|....*..
gi 212506821  172 LSTgcHNYKPPIERSKSAPKLMKVSDD 198
Cdd:pfam14719 160 TGT--CNYRPPVERSKSAPKLGSITEE 184
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
 9-133 1.68e-84

Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; The function of FAM43A is currently unknown. Human FAM43A is located on chromosome 3 at location 3q29. It encodes a 3182 base pair mRNA which possesses one Pleckstrin homology-like domain. The mRNA translates into LOC131583, a hydrophilic protein that is predicted to localize in the nucleus. The FAM43A gene is conserved through a broad range of vertebrates. It is highly conserved from chimpanzees to zebrafish. 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.


Pssm-ID: 269925  Cd Length: 125  Bit Score: 254.14  E-value: 1.68e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212506821   9 ITAEDPTYKVSYLGNVLTGLAKGEGCIEKPLNTLWKNYNESLKPSIQMKIKVTQSGLKAVTKDHGLIEYWSHRITFCTVP 88
Cdd:cd01214    1 ITEEDPTYTVVYLGNVLTIWAKGEGCTDKPLATIWRNYTQGKKPDVKMKLTVTPSGLKATTKQHGLTEYWLHRITYCSAP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 212506821  89 PEFPNIFCWIYRHEGRKLKQELRCHAVLCSKESVASKMSDTLKTR 133
Cdd:cd01214   81 PNYPRVFCWIYRHEGRKLKVELRCHAVLCSKESKARAIALLLYQR 125
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 12-140 2.06e-15

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: 72.73  E-value: 2.06e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212506821    12 EDPTYKVSYLGNVLTGLAKGEGCIEKPLNTLWKNYNESLKPSIQMKIKVTQSGLKAVTKD-HGLI-EYWSHRITFCTVPP 89
Cdd:smart00462   2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDtKAVLhEHPLRRISFCAVGP 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 212506821    90 EFPNIFCWIYRHEGrklKQELRCHAVLCSKES--VASKMSDTLKTRLTQALVE 140
Cdd:smart00462  82 DDLDVFGYIARDPG---SSRFACHVFRCEKAAedIALAIGQAFQLAYELKLKA 131
 
Name Accession Description Interval E-value
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
15-198 1.98e-114

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 332.50  E-value: 1.98e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212506821   15 TYKVSYLGNVLTGLAKGEGCIEKPLNTLWKNYNESlKPSIQMKIKVTQSGLKAVTKDHGLIEYWSHRITFCTVPPEFPNI 94
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQG-KSGTKMKLTVTRSGLKATTKEHGLTEYWSHRITYCSAPPNYPRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212506821   95 FCWIYRHEGRKLKQELRCHAVLCSKESVASKMSDTLKTRLTQALVEFKRDKLLR---QNARLSLVNSVYDNPSLPKRKIL 171
Cdd:pfam14719  80 FCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLCArhaQNARLSLGNAAYDPPSVPRRKLL 159

                         170       180
                  ....*....|....*....|....*..
gi 212506821  172 LSTgcHNYKPPIERSKSAPKLMKVSDD 198
Cdd:pfam14719 160 TGT--CNYRPPVERSKSAPKLGSITEE 184
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
 9-133 1.68e-84

Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; The function of FAM43A is currently unknown. Human FAM43A is located on chromosome 3 at location 3q29. It encodes a 3182 base pair mRNA which possesses one Pleckstrin homology-like domain. The mRNA translates into LOC131583, a hydrophilic protein that is predicted to localize in the nucleus. The FAM43A gene is conserved through a broad range of vertebrates. It is highly conserved from chimpanzees to zebrafish. 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.


Pssm-ID: 269925  Cd Length: 125  Bit Score: 254.14  E-value: 1.68e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212506821   9 ITAEDPTYKVSYLGNVLTGLAKGEGCIEKPLNTLWKNYNESLKPSIQMKIKVTQSGLKAVTKDHGLIEYWSHRITFCTVP 88
Cdd:cd01214    1 ITEEDPTYTVVYLGNVLTIWAKGEGCTDKPLATIWRNYTQGKKPDVKMKLTVTPSGLKATTKQHGLTEYWLHRITYCSAP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 212506821  89 PEFPNIFCWIYRHEGRKLKQELRCHAVLCSKESVASKMSDTLKTR 133
Cdd:cd01214   81 PNYPRVFCWIYRHEGRKLKVELRCHAVLCSKESKARAIALLLYQR 125
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 14-130 1.18e-19

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: 84.10  E-value: 1.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212506821  14 PTYKVSYLGNVLTGLAKGEGCIEKPLNTLWKNYNESLKPSIQMKIKVTQSGLKAVTKDHG--LIEYWSHRITFCTVPPEF 91
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKelLLRHPLHRISYCGRDPDN 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 212506821  92 PNIFCWIYRHEGrklKQELRCHAVLCSKESVASKMSDTL 130
Cdd:cd00934   81 PNVFAFIAGEEG---GSGFRCHVFQCEDEEEAEEILQAI 116
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 12-140 2.06e-15

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: 72.73  E-value: 2.06e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212506821    12 EDPTYKVSYLGNVLTGLAKGEGCIEKPLNTLWKNYNESLKPSIQMKIKVTQSGLKAVTKD-HGLI-EYWSHRITFCTVPP 89
Cdd:smart00462   2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDtKAVLhEHPLRRISFCAVGP 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 212506821    90 EFPNIFCWIYRHEGrklKQELRCHAVLCSKES--VASKMSDTLKTRLTQALVE 140
Cdd:smart00462  82 DDLDVFGYIARDPG---SSRFACHVFRCEKAAedIALAIGQAFQLAYELKLKA 131
PTB_P-CLI1 cd13167
PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like ...
 16-130 1.06e-12

PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like fold; P-CLI1 (also called Phosphotyrosine interaction domain-containing protein 1) increases proliferation of preadipocytes without affecting adipocytic differentiation. It forms a complex with PID1/PCLI1, LRP1 and CUBNI. It is found in subcutaneous fat, heart, skeletal muscle, brain, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood leukocyte. P-CLI1 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.


Pssm-ID: 269988  Cd Length: 139  Bit Score: 65.01  E-value: 1.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212506821  16 YKVSYLGNV-LTGLAKGEGCIEKPLNTLWKNY---NESLKPSIQ-MKIKVTQ--------SGLKAVTKDhgliEYWSHRI 82
Cdd:cd13167    3 YKVTYLGKVsTTGTQFLSGCTESPVIELWKKHtlaREDIFPSNAlLEIRPFQvrlhhldlRGEATVHMD----TFQVARI 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 212506821  83 TFCTVPPEF-PNIFCWIYRHEGRKLKQELRCHAVLCSKESVASKMSDTL 130
Cdd:cd13167   79 AYCTADHNIsPNIFAWVYREINDDLSFQMDCHAVECESKLEAKKLAHAM 127
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 15-130 1.50e-11

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals 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 mammals, insects, and sponges.


Pssm-ID: 269981  Cd Length: 123  Bit Score: 61.19  E-value: 1.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212506821  15 TYKVSYLGNVLTGLAKGEGCIEKPLNTLWKNYNESLKPSIQMKIKVTQSGLK---AVTKDhgLIEYWS-HRITFCTVPPE 90
Cdd:cd13159    4 TFYLKYLGSTLVEKPKGEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKvtdSATNE--TILEVSiYRISYCTADAN 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 212506821  91 FPNIFCWIYRHegrKLKQELRCHAVLCSKESVASKMSDTL 130
Cdd:cd13159   82 HDKVFAFIATN---QDNEKLECHAFLCAKRKMAQAVTLTV 118
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
 14-138 1.25e-07

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: 50.03  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212506821  14 PTYKVSYLGN-VLTGLAkGEGCIEKPLNTLWKNY--NESLKpsiQMKIKVTQSGLKAVTKDHGLIEYWS-----HRITFC 85
Cdd:cd13160    1 PVFTVKYLGRmPARGLW-GIKHTRKPLVDALKNLpkGKTLP---KTKLEVSSDGVKLEELRGGFGSSKTvffpiHTISYG 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 212506821  86 TVPPEFPNIFCWIYRHEGRKLKQELRCHAVLCSKesvaSKMSDTLKTRLTQAL 138
Cdd:cd13160   77 VQDLVHTRVFSMIVVGEQDSSNHPFECHAFVCDS----RADARNLTYWLAKAF 125
 
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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