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Conserved domains on  [gi|2172664142|ref|NP_001386146|]
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protein FAM43B [Rattus norvegicus]

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

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 ...
71-262 7.00e-89

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 pfam14719:

Pssm-ID: 473070  Cd Length: 184  Bit Score: 263.94  E-value: 7.00e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664142  71 TYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGG-GTKMKLTLGPHGIRMQPSERgsggsggrrPAHAYLLPRITYCA 149
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQGKsGTKMKLTVTRSGLKATTKEH---------GLTEYWSHRITYCS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664142 150 ADGRHPRVFTWVYRHQARHKAVVLRCHAVLLARAHKARSLARLLHQTALAAFSDFKRLQRQsdARHVRQQHLRAGGAAAS 229
Cdd:pfam14719  72 APPNYPRVFCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLC--ARHAQNARLSLGNAAYD 149
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2172664142 230 VPRAPLRRLLNAKCAYRpPPGERSRGAPRLSSI 262
Cdd:pfam14719 150 PPSVPRRKLLTGTCNYR-PPVERSKSAPKLGSI 181
 
Name Accession Description Interval E-value
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
71-262 7.00e-89

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 263.94  E-value: 7.00e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664142  71 TYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGG-GTKMKLTLGPHGIRMQPSERgsggsggrrPAHAYLLPRITYCA 149
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQGKsGTKMKLTVTRSGLKATTKEH---------GLTEYWSHRITYCS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664142 150 ADGRHPRVFTWVYRHQARHKAVVLRCHAVLLARAHKARSLARLLHQTALAAFSDFKRLQRQsdARHVRQQHLRAGGAAAS 229
Cdd:pfam14719  72 APPNYPRVFCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLC--ARHAQNARLSLGNAAYD 149
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2172664142 230 VPRAPLRRLLNAKCAYRpPPGERSRGAPRLSSI 262
Cdd:pfam14719 150 PPSVPRRKLLTGTCNYR-PPVERSKSAPKLGSI 181
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
65-196 3.98e-62

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: 193.66  E-value: 3.98e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664142  65 LNKEDPTYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGG--GTKMKLTLGPHGIRMQpsergsggsGGRRPAHAYLL 142
Cdd:cd01214     1 ITEEDPTYTVVYLGNVLTIWAKGEGCTDKPLATIWRNYTQGKkpDVKMKLTVTPSGLKAT---------TKQHGLTEYWL 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2172664142 143 PRITYCAADGRHPRVFTWVYRHQARHKAVVLRCHAVLLARAHKARSLARLLHQT 196
Cdd:cd01214    72 HRITYCSAPPNYPRVFCWIYRHEGRKLKVELRCHAVLCSKESKARAIALLLYQR 125
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
68-211 1.02e-11

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: 61.56  E-value: 1.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664142   68 EDPTYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGGG--TKMKLTLGPHGIRMqpsergsGGSGGRRPAHAYLLPRI 145
Cdd:smart00462   2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKepQKVILSISSRGVKL-------IDEDTKAVLHEHPLRRI 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2172664142  146 TYCAADGRHPRVFTWVYRHQARHKavvLRCHAVLLARAHKArslarlLHQTALAAFSD-FKRLQRQS 211
Cdd:smart00462  75 SFCAVGPDDLDVFGYIARDPGSSR---FACHVFRCEKAAED------IALAIGQAFQLaYELKLKAR 132
 
Name Accession Description Interval E-value
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
71-262 7.00e-89

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 263.94  E-value: 7.00e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664142  71 TYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGG-GTKMKLTLGPHGIRMQPSERgsggsggrrPAHAYLLPRITYCA 149
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQGKsGTKMKLTVTRSGLKATTKEH---------GLTEYWSHRITYCS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664142 150 ADGRHPRVFTWVYRHQARHKAVVLRCHAVLLARAHKARSLARLLHQTALAAFSDFKRLQRQsdARHVRQQHLRAGGAAAS 229
Cdd:pfam14719  72 APPNYPRVFCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLC--ARHAQNARLSLGNAAYD 149
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2172664142 230 VPRAPLRRLLNAKCAYRpPPGERSRGAPRLSSI 262
Cdd:pfam14719 150 PPSVPRRKLLTGTCNYR-PPVERSKSAPKLGSI 181
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
65-196 3.98e-62

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: 193.66  E-value: 3.98e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664142  65 LNKEDPTYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGG--GTKMKLTLGPHGIRMQpsergsggsGGRRPAHAYLL 142
Cdd:cd01214     1 ITEEDPTYTVVYLGNVLTIWAKGEGCTDKPLATIWRNYTQGKkpDVKMKLTVTPSGLKAT---------TKQHGLTEYWL 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2172664142 143 PRITYCAADGRHPRVFTWVYRHQARHKAVVLRCHAVLLARAHKARSLARLLHQT 196
Cdd:cd01214    72 HRITYCSAPPNYPRVFCWIYRHEGRKLKVELRCHAVLCSKESKARAIALLLYQR 125
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
70-195 3.14e-13

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: 65.61  E-value: 3.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664142  70 PTYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGGG--TKMKLTLGPHGIRMqpsergsGGSGGRRPAHAYLLPRITY 147
Cdd:cd00934     1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRkpGPVLLEVSSKGVKL-------LDLDTKELLLRHPLHRISY 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2172664142 148 CAADGRHPRVFTWVYRHQARHKavvLRCHAVLLARAHKARSLARLLHQ 195
Cdd:cd00934    74 CGRDPDNPNVFAFIAGEEGGSG---FRCHVFQCEDEEEAEEILQAIGQ 118
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
68-211 1.02e-11

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: 61.56  E-value: 1.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664142   68 EDPTYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGGG--TKMKLTLGPHGIRMqpsergsGGSGGRRPAHAYLLPRI 145
Cdd:smart00462   2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKepQKVILSISSRGVKL-------IDEDTKAVLHEHPLRRI 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2172664142  146 TYCAADGRHPRVFTWVYRHQARHKavvLRCHAVLLARAHKArslarlLHQTALAAFSD-FKRLQRQS 211
Cdd:smart00462  75 SFCAVGPDDLDVFGYIARDPGSSR---FACHVFRCEKAAED------IALAIGQAFQLaYELKLKAR 132
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
71-190 1.04e-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: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664142  71 TYTVWYLGNAVTLHAKGDGCTDDAVGRI--WARCGPGGGTKMKLTLGPHGIRMqpSERGSGGSGGRRPAHayllpRITYC 148
Cdd:cd13159     4 TFYLKYLGSTLVEKPKGEGATAEAVKTIiaMAKASGKKLQKVTLTVSPKGIKV--TDSATNETILEVSIY-----RISYC 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2172664142 149 AADGRHPRVFTWVYRHQARHKavvLRCHAVLLARAHKARSLA 190
Cdd:cd13159    77 TADANHDKVFAFIATNQDNEK---LECHAFLCAKRKMAQAVT 115
PTB_P-CLI1 cd13167
PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like ...
72-190 7.60e-06

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: 44.98  E-value: 7.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664142  72 YTVWYLGNAVTLHAK-GDGCTDDAVGRIWARCGPGGGT----KMKLTLGPHGIRMQPSERGSGGSGGRrpaHAYLLPRIT 146
Cdd:cd13167     3 YKVTYLGKVSTTGTQfLSGCTESPVIELWKKHTLAREDifpsNALLEIRPFQVRLHHLDLRGEATVHM---DTFQVARIA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2172664142 147 YCAADGR-HPRVFTWVYRHQARHKAVVLRCHAVLLARAHKARSLA 190
Cdd:cd13167    80 YCTADHNiSPNIFAWVYREINDDLSFQMDCHAVECESKLEAKKLA 124
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
70-201 2.43e-04

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: 40.40  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664142  70 PTYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGGGT-KMKLTLGPHGIRMQPSERGSGGSGGRR-PAHayllpRITY 147
Cdd:cd13160     1 PVFTVKYLGRMPARGLWGIKHTRKPLVDALKNLPKGKTLpKTKLEVSSDGVKLEELRGGFGSSKTVFfPIH-----TISY 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2172664142 148 CAADGRHPRVFTWVYRHQARHKAVVLRCHAVLLARAHKARSLARLLhqtaLAAF 201
Cdd:cd13160    76 GVQDLVHTRVFSMIVVGEQDSSNHPFECHAFVCDSRADARNLTYWL----AKAF 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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