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Conserved domains on  [gi|84781640|ref|NP_001034091|]
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protein FAM43A [Rattus norvegicus]

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);
69-256 9.80e-101

Phosphotyrosine interaction domain (PTB/PID);


:

Pssm-ID: 405418  Cd Length: 184  Bit Score: 297.84  E-value: 9.80e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781640    69 TYTVLYLGNATTIQARGDGCTDLAVGKIWSKSEAGRQGTKMKLTVSAQGIRMVHAEeralrRPGHLYLLHRVTYCVADAR 148
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQGKSGTKMKLTVTRSGLKATTKE-----HGLTEYWSHRITYCSAPPN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781640   149 LPKVFAWVYRHELKHKAVMLRCHAVLVSKPEKAQAMALLLYQTSANALAEFKRLKRRddARHQQQELV----GAHTIPLV 224
Cdd:pfam14719  76 YPRVFCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLC--ARHAQNARLslgnAAYDPPSV 153

                         170       180       190
                  ....*....|....*....|....*....|..
gi 84781640   225 PLRKlLLHGPCCYKPPVERSRSAPKLGSITED 256
Cdd:pfam14719 154 PRRK-LLTGTCNYRPPVERSKSAPKLGSITEE 184
 
Name Accession Description Interval E-value
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
69-256 9.80e-101

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 297.84  E-value: 9.80e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781640    69 TYTVLYLGNATTIQARGDGCTDLAVGKIWSKSEAGRQGTKMKLTVSAQGIRMVHAEeralrRPGHLYLLHRVTYCVADAR 148
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQGKSGTKMKLTVTRSGLKATTKE-----HGLTEYWSHRITYCSAPPN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781640   149 LPKVFAWVYRHELKHKAVMLRCHAVLVSKPEKAQAMALLLYQTSANALAEFKRLKRRddARHQQQELV----GAHTIPLV 224
Cdd:pfam14719  76 YPRVFCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLC--ARHAQNARLslgnAAYDPPSV 153

                         170       180       190
                  ....*....|....*....|....*....|..
gi 84781640   225 PLRKlLLHGPCCYKPPVERSRSAPKLGSITED 256
Cdd:pfam14719 154 PRRK-LLTGTCNYRPPVERSKSAPKLGSITEE 184
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
 63-191 4.06e-73

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: 225.25  E-value: 4.06e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781640  63 ITSEDPTYTVLYLGNATTIQARGDGCTDLAVGKIWSKSEAGRQ-GTKMKLTVSAQGIRMVHAEEralrrPGHLYLLHRVT 141
Cdd:cd01214   1 ITEEDPTYTVVYLGNVLTIWAKGEGCTDKPLATIWRNYTQGKKpDVKMKLTVTPSGLKATTKQH-----GLTEYWLHRIT 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 84781640 142 YCVADARLPKVFAWVYRHELKHKAVMLRCHAVLVSKPEKAQAMALLLYQT 191
Cdd:cd01214  76 YCSAPPNYPRVFCWIYRHEGRKLKVELRCHAVLCSKESKARAIALLLYQR 125
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 65-204 7.80e-16

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: 73.89  E-value: 7.80e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781640     65 SEDPTYTVLYLGNATTIQARGDGCTDLAVGKIWS-KSEAGRQGTKMKLTVSAQGIRMVHAEERALRrpgHLYLLHRVTYC 143
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAaQGSEKKEPQKVILSISSRGVKLIDEDTKAVL---HEHPLRRISFC 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 84781640    144 VADARLPKVFAWVYRHELkhkAVMLRCHAVLVSKPEKAQAMALLlyQTSANALAEFKRLKR 204
Cdd:smart00462  78 AVGPDDLDVFGYIARDPG---SSRFACHVFRCEKAAEDIALAIG--QAFQLAYELKLKARS 133
 
Name Accession Description Interval E-value
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
69-256 9.80e-101

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 297.84  E-value: 9.80e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781640    69 TYTVLYLGNATTIQARGDGCTDLAVGKIWSKSEAGRQGTKMKLTVSAQGIRMVHAEeralrRPGHLYLLHRVTYCVADAR 148
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQGKSGTKMKLTVTRSGLKATTKE-----HGLTEYWSHRITYCSAPPN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781640   149 LPKVFAWVYRHELKHKAVMLRCHAVLVSKPEKAQAMALLLYQTSANALAEFKRLKRRddARHQQQELV----GAHTIPLV 224
Cdd:pfam14719  76 YPRVFCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLC--ARHAQNARLslgnAAYDPPSV 153

                         170       180       190
                  ....*....|....*....|....*....|..
gi 84781640   225 PLRKlLLHGPCCYKPPVERSRSAPKLGSITED 256
Cdd:pfam14719 154 PRRK-LLTGTCNYRPPVERSKSAPKLGSITEE 184
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
 63-191 4.06e-73

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: 225.25  E-value: 4.06e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781640  63 ITSEDPTYTVLYLGNATTIQARGDGCTDLAVGKIWSKSEAGRQ-GTKMKLTVSAQGIRMVHAEEralrrPGHLYLLHRVT 141
Cdd:cd01214   1 ITEEDPTYTVVYLGNVLTIWAKGEGCTDKPLATIWRNYTQGKKpDVKMKLTVTPSGLKATTKQH-----GLTEYWLHRIT 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 84781640 142 YCVADARLPKVFAWVYRHELKHKAVMLRCHAVLVSKPEKAQAMALLLYQT 191
Cdd:cd01214  76 YCSAPPNYPRVFCWIYRHEGRKLKVELRCHAVLCSKESKARAIALLLYQR 125
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 69-190 8.28e-19

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: 81.99  E-value: 8.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781640  69 TYTVLYLGNATTIQARGDGCTDLAVGKIWS--KSEAGRQGtKMKLTVSAQGIRMVHA--EERALRRPghlylLHRVTYCV 144
Cdd:cd13159   4 TFYLKYLGSTLVEKPKGEGATAEAVKTIIAmaKASGKKLQ-KVTLTVSPKGIKVTDSatNETILEVS-----IYRISYCT 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 84781640 145 ADARLPKVFAWVYRHELKHKavmLRCHAVLVSKPEKAQAMALLLYQ 190
Cdd:cd13159  78 ADANHDKVFAFIATNQDNEK---LECHAFLCAKRKMAQAVTLTVAQ 120
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 68-190 3.70e-18

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: 79.86  E-value: 3.70e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781640  68 PTYTVLYLGNATTIQARGDGCTDLAVGKIW-SKSEAGRQGTKMKLTVSAQGIRMVHAEERALRrpgHLYLLHRVTYCVAD 146
Cdd:cd00934   1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAaALKSSKRKPGPVLLEVSSKGVKLLDLDTKELL---LRHPLHRISYCGRD 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 84781640 147 ARLPKVFAWVYRHELKhkaVMLRCHAVLVSKPEKAQAMALLLYQ 190
Cdd:cd00934  78 PDNPNVFAFIAGEEGG---SGFRCHVFQCEDEEEAEEILQAIGQ 118
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 65-204 7.80e-16

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: 73.89  E-value: 7.80e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781640     65 SEDPTYTVLYLGNATTIQARGDGCTDLAVGKIWS-KSEAGRQGTKMKLTVSAQGIRMVHAEERALRrpgHLYLLHRVTYC 143
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAaQGSEKKEPQKVILSISSRGVKLIDEDTKAVL---HEHPLRRISFC 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 84781640    144 VADARLPKVFAWVYRHELkhkAVMLRCHAVLVSKPEKAQAMALLlyQTSANALAEFKRLKR 204
Cdd:smart00462  78 AVGPDDLDVFGYIARDPG---SSRFACHVFRCEKAAEDIALAIG--QAFQLAYELKLKARS 133
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
 68-188 1.05e-09

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: 56.19  E-value: 1.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781640  68 PTYTVLYLGNATTIQARGDGCTDLAVGKIWSKSEAGRQGTKMKLTVSAQGIRMVhaEERALRRPGH--LYLLHRVTYCVA 145
Cdd:cd13160   1 PVFTVKYLGRMPARGLWGIKHTRKPLVDALKNLPKGKTLPKTKLEVSSDGVKLE--ELRGGFGSSKtvFFPIHTISYGVQ 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 84781640 146 DARLPKVFAWVYRHELKHKAVMLRCHAVLVSKPEKAQAMALLL 188
Cdd:cd13160  79 DLVHTRVFSMIVVGEQDSSNHPFECHAFVCDSRADARNLTYWL 121
PTB_P-CLI1 cd13167
PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like ...
 70-185 2.00e-09

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: 55.77  E-value: 2.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781640  70 YTVLYLGNATTIQAR-GDGCTDLAVGKIWSKSEAGRQ---GTKMKLTVSAQGIRMVHAEERAlRRPGHL--YLLHRVTYC 143
Cdd:cd13167   3 YKVTYLGKVSTTGTQfLSGCTESPVIELWKKHTLAREdifPSNALLEIRPFQVRLHHLDLRG-EATVHMdtFQVARIAYC 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 84781640 144 VADARL-PKVFAWVYRHELKHKAVMLRCHAVLVSKPEKAQAMA 185
Cdd:cd13167  82 TADHNIsPNIFAWVYREINDDLSFQMDCHAVECESKLEAKKLA 124
 
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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