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Conserved domains on  [gi|755511627|ref|XP_011239060|]
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TBC1 domain family member 1 isoform X1 [Mus musculus]

Protein Classification

PTB domain-containing protein; TBC1D1 family PTB domain-containing protein( domain architecture ID 10097140)

PTB (phosphotyrosine-binding) domain-containing protein similar to Ciona intestinalis Not4 protein; TBC1D1 (TBC1 domain family member 1) family PTB (phosphotyrosine-binding) domain-containing protein similar to PTB domain region of Homo sapiens TBC1D1 that may act as a GTPase-activating protein for Rab family protein(s)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 884-1101 2.21e-77

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


:

Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 254.54  E-value: 2.21e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627    884 VGQGVPRHHRGEIWKFLAEQFHLKHpfpskqQPKDVPYKELLK----KLTSQQHAILIDLGRTFPTHPYFSAQLGAGQLS 959
Cdd:smart00164    1 VRKGVPPSLRGVVWKLLLNAQPMDT------SADKDLYSRLLKetapDDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQES 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627    960 LYNILKAYSLLDQEVGYCQGLSFVAGILLLHM-SEEEAFKMLKFLMFDMGLRKqYRPDMIILQIQMYQLSRLLHDYHRDL 1038
Cdd:smart00164   75 LRRVLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYGPNF-YLPDMSGLQLDLLQLDRLVKEYDPDL 153

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511627   1039 YNHLEEHEIGPSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEVIFKVALSLLGSHKPLIL 1101
Cdd:smart00164  154 YKHLKDLGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
 164-365 1.62e-76

TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The TBC1D1-like members here include TBC1D1, TBC1D4 (also called Akt substrate of 160 kDa or AS160), and pollux (PLX), a calmodulin-binding protein, and are thought to have a role in regulating cell growth and differentiation. These proteins are thought to function as GTPase-activating protein for Rab family protein(s). They may play a role in the cell cycle and differentiation of various tissues. They all contain an N-terminal PTB domain, a calmodulin CBD domain, and a C-terminal TBC domain which is thought to be a GTPase activator protein of Rab-like small GTPases. Recently, TBC1D1 and TBC1D4 were recognized to potentially link the proximal signalling of insulin and/or exercise with GLUT4. TBC1D4 is thought to be involved in contraction-stimulated glucose uptake, but TBC1D4-independent mechanisms (potentially involving TBC1D1) are likely to be essential for most of the contraction's effect. 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: 269967  Cd Length: 143  Bit Score: 248.75  E-value: 1.62e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627  164 EFDDTFAKKFEVLFCGRVTVAHKKAPPALIDECIEKFNHVSCGRrtdweaptgqpsapgprpmrksfsqpglrslafrke 243
Cdd:cd01269     1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEK------------------------------------ 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627  244 fqdasLRSstfssfdndienhligGHNVVQPTDMEENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDH 323
Cdd:cd01269    45 -----SRS----------------GPSSVQPTDSEENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDH 103

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 755511627  324 FGFICREcsGGGSGGFHFVCYVFQCTNEALVDEIMMTLKQAF 365
Cdd:cd01269   104 FGFICRE--SSEGGGFHFVCYVFKCQSESVVDEIMLTIKQAF 143
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 777-832 1.50e-23

Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found in eukaryotic proteins, such as TBC1 domain family members 1 and 4. This presumed domain is typically between 50 to 64 amino acids in length. TBC domain proteins may act as GTPase-activating proteins for RAB2A, RAB8A, RAB10 and RAB14.


:

Pssm-ID: 463365  Cd Length: 63  Bit Score: 94.92  E-value: 1.50e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511627   777 ELPPRSPLEPVCEDGP-------FGPVQEEKRKTSRELRELWKKAILQQILLLRMEKENQKLQ 832
Cdd:pfam11830    1 ELLPLSPLAPGGEEDPagllsseDSPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 21-150 1.54e-03

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: 39.80  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627   21 FGLQLVGSLPVHSLTTMPMLpwVVAEVRRLSGQCSKKEPRTKqVRLWVSPSGLRCEpDLEKSQPwdplicssIFECKPQR 100
Cdd:cd00934     3 FQVKYLGSVEVGSSRGVDVV--EEALKALAAALKSSKRKPGP-VLLEVSSKGVKLL-DLDTKEL--------LLRHPLHR 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 755511627  101 VHKLIHNSHDPSYFaCLIKEDAAHRQSLCYVFKADDQTKVPEIISSIRQA 150
Cdd:cd00934    71 ISYCGRDPDNPNVF-AFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQA 119
PRK12704 super family cl36166
phosphodiesterase; Provisional
 1139-1239 3.38e-03

phosphodiesterase; Provisional


The actual alignment was detected with superfamily member PRK12704:

Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627 1139 KQLQAYEvEYHVLQEELIESSPLSDN----------QRMEKLEKTNSSLRKQNLDLLEQLQVANARIQSLEATVEKLLTS 1208
Cdd:PRK12704   58 ALLEAKE-EIHKLRNEFEKELRERRNelqklekrllQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL 136

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 755511627 1209 ESKLKQ-----AALTLEVERSALLQMVE-ELRRQSAR 1239
Cdd:PRK12704  137 IEEQLQeleriSGLTAEEAKEILLEKVEeEARHEAAV 173
 
Name Accession Description Interval E-value
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 884-1101 2.21e-77

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 254.54  E-value: 2.21e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627    884 VGQGVPRHHRGEIWKFLAEQFHLKHpfpskqQPKDVPYKELLK----KLTSQQHAILIDLGRTFPTHPYFSAQLGAGQLS 959
Cdd:smart00164    1 VRKGVPPSLRGVVWKLLLNAQPMDT------SADKDLYSRLLKetapDDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQES 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627    960 LYNILKAYSLLDQEVGYCQGLSFVAGILLLHM-SEEEAFKMLKFLMFDMGLRKqYRPDMIILQIQMYQLSRLLHDYHRDL 1038
Cdd:smart00164   75 LRRVLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYGPNF-YLPDMSGLQLDLLQLDRLVKEYDPDL 153

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511627   1039 YNHLEEHEIGPSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEVIFKVALSLLGSHKPLIL 1101
Cdd:smart00164  154 YKHLKDLGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
 164-365 1.62e-76

TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The TBC1D1-like members here include TBC1D1, TBC1D4 (also called Akt substrate of 160 kDa or AS160), and pollux (PLX), a calmodulin-binding protein, and are thought to have a role in regulating cell growth and differentiation. These proteins are thought to function as GTPase-activating protein for Rab family protein(s). They may play a role in the cell cycle and differentiation of various tissues. They all contain an N-terminal PTB domain, a calmodulin CBD domain, and a C-terminal TBC domain which is thought to be a GTPase activator protein of Rab-like small GTPases. Recently, TBC1D1 and TBC1D4 were recognized to potentially link the proximal signalling of insulin and/or exercise with GLUT4. TBC1D4 is thought to be involved in contraction-stimulated glucose uptake, but TBC1D4-independent mechanisms (potentially involving TBC1D1) are likely to be essential for most of the contraction's effect. 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: 269967  Cd Length: 143  Bit Score: 248.75  E-value: 1.62e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627  164 EFDDTFAKKFEVLFCGRVTVAHKKAPPALIDECIEKFNHVSCGRrtdweaptgqpsapgprpmrksfsqpglrslafrke 243
Cdd:cd01269     1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEK------------------------------------ 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627  244 fqdasLRSstfssfdndienhligGHNVVQPTDMEENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDH 323
Cdd:cd01269    45 -----SRS----------------GPSSVQPTDSEENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDH 103

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 755511627  324 FGFICREcsGGGSGGFHFVCYVFQCTNEALVDEIMMTLKQAF 365
Cdd:cd01269   104 FGFICRE--SSEGGGFHFVCYVFKCQSESVVDEIMLTIKQAF 143
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 932-1101 2.29e-56

Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.


Pssm-ID: 459855  Cd Length: 178  Bit Score: 193.24  E-value: 2.29e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627   932 QHAILIDLGRTFPTHPYFsaQLGAGQLSLYNILKAYSLLDQEVGYCQGLSFVAGILLL-HMSEEEAFKMLKFLMFDMGLR 1010
Cdd:pfam00566    9 PEQIEKDVPRTFPHSFFF--DNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLR 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627  1011 KQYRPDMIILQIQMYQLSRLLHDYHRDLYNHLEEHEIGPSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEV-IFKVA 1089
Cdd:pfam00566   87 DFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVA 166

                          170
                   ....*....|..
gi 755511627  1090 LSLLGSHKPLIL 1101
Cdd:pfam00566  167 LAILKRFREELL 178
COG5210 COG5210
GTPase-activating protein [General function prediction only];
815-1115 8.37e-46

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 173.06  E-value: 8.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627  815 ILQQILLLRMEKENQKlqaseNDLLNKRLKLDYEEITPCLkevTTVWEKMLSTPGRSKIKFDMEKVHSAVGQGVPRHHRG 894
Cdd:COG5210   148 KGSSSLNSNPELNKEI-----NELSLKEEPQKLRYYELAA---DKLWISYLDPNPLSFLPVQLSKLRELIRKGIPNELRG 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627  895 EIWKFLaeqfhLKHPFPSKQQPKDVPYKELLKKLTSQQ-----HAILIDLGRTFPTHPYFSAQLGAGQLSLYNILKAYSL 969
Cdd:COG5210   220 DVWEFL-----LGIGFDLDKNPGLYERLLNLHREAKIPtqeiiSQIEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSL 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627  970 LDQEVGYCQGLSFVAGILLLHM-SEEEAFKMLKFLMFDMGLRKQYRPDMIILQIQMYQLSRLLHDYHRDLYNHLEEHEIG 1048
Cdd:COG5210   295 YNPEVGYVQGMNFLAAPLLLVLeSEEQAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVV 374

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511627 1049 PSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEVIFKVALSLLGSHKPLILQHENLETIVDFIKN 1115
Cdd:COG5210   375 LLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLDLLLKQ 441
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 777-832 1.50e-23

Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found in eukaryotic proteins, such as TBC1 domain family members 1 and 4. This presumed domain is typically between 50 to 64 amino acids in length. TBC domain proteins may act as GTPase-activating proteins for RAB2A, RAB8A, RAB10 and RAB14.


Pssm-ID: 463365  Cd Length: 63  Bit Score: 94.92  E-value: 1.50e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511627   777 ELPPRSPLEPVCEDGP-------FGPVQEEKRKTSRELRELWKKAILQQILLLRMEKENQKLQ 832
Cdd:pfam11830    1 ELLPLSPLAPGGEEDPagllsseDSPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 273-377 1.43e-21

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: 91.61  E-value: 1.43e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627    273 QPTDMEENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRECSGGgsggfHFVCYVFQCTNEA 352
Cdd:smart00462   36 QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIARDPGSS-----RFACHVFRCEKAA 110

                            90       100
                    ....*....|....*....|....*
gi 755511627    353 lvDEIMMTLKQAFTVAAVQQTAKAP 377
Cdd:smart00462  111 --EDIALAIGQAFQLAYELKLKARS 133
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 21-150 1.54e-03

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: 39.80  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627   21 FGLQLVGSLPVHSLTTMPMLpwVVAEVRRLSGQCSKKEPRTKqVRLWVSPSGLRCEpDLEKSQPwdplicssIFECKPQR 100
Cdd:cd00934     3 FQVKYLGSVEVGSSRGVDVV--EEALKALAAALKSSKRKPGP-VLLEVSSKGVKLL-DLDTKEL--------LLRHPLHR 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 755511627  101 VHKLIHNSHDPSYFaCLIKEDAAHRQSLCYVFKADDQTKVPEIISSIRQA 150
Cdd:cd00934    71 ISYCGRDPDNPNVF-AFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQA 119
PRK12704 PRK12704
phosphodiesterase; Provisional
 1139-1239 3.38e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627 1139 KQLQAYEvEYHVLQEELIESSPLSDN----------QRMEKLEKTNSSLRKQNLDLLEQLQVANARIQSLEATVEKLLTS 1208
Cdd:PRK12704   58 ALLEAKE-EIHKLRNEFEKELRERRNelqklekrllQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL 136

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 755511627 1209 ESKLKQ-----AALTLEVERSALLQMVE-ELRRQSAR 1239
Cdd:PRK12704  137 IEEQLQeleriSGLTAEEAKEILLEKVEeEARHEAAV 173
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1121-1236 8.63e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 8.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627 1121 GLVQMEKTISQVFemDIAKQLQAYEVEYHVLQEELIESSplSDNQRM-EKLEKTNSSLRKQNLDLL---EQLQVANARIQ 1196
Cdd:COG4372    36 ALFELDKLQEELE--QLREELEQAREELEQLEEELEQAR--SELEQLeEELEELNEQLQAAQAELAqaqEELESLQEEAE 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 755511627 1197 SLEATVEKLLTSESKLKQAALTLEVERSALLQMVEELRRQ 1236
Cdd:COG4372   112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
 
Name Accession Description Interval E-value
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 884-1101 2.21e-77

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 254.54  E-value: 2.21e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627    884 VGQGVPRHHRGEIWKFLAEQFHLKHpfpskqQPKDVPYKELLK----KLTSQQHAILIDLGRTFPTHPYFSAQLGAGQLS 959
Cdd:smart00164    1 VRKGVPPSLRGVVWKLLLNAQPMDT------SADKDLYSRLLKetapDDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQES 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627    960 LYNILKAYSLLDQEVGYCQGLSFVAGILLLHM-SEEEAFKMLKFLMFDMGLRKqYRPDMIILQIQMYQLSRLLHDYHRDL 1038
Cdd:smart00164   75 LRRVLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYGPNF-YLPDMSGLQLDLLQLDRLVKEYDPDL 153

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511627   1039 YNHLEEHEIGPSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEVIFKVALSLLGSHKPLIL 1101
Cdd:smart00164  154 YKHLKDLGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
 164-365 1.62e-76

TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The TBC1D1-like members here include TBC1D1, TBC1D4 (also called Akt substrate of 160 kDa or AS160), and pollux (PLX), a calmodulin-binding protein, and are thought to have a role in regulating cell growth and differentiation. These proteins are thought to function as GTPase-activating protein for Rab family protein(s). They may play a role in the cell cycle and differentiation of various tissues. They all contain an N-terminal PTB domain, a calmodulin CBD domain, and a C-terminal TBC domain which is thought to be a GTPase activator protein of Rab-like small GTPases. Recently, TBC1D1 and TBC1D4 were recognized to potentially link the proximal signalling of insulin and/or exercise with GLUT4. TBC1D4 is thought to be involved in contraction-stimulated glucose uptake, but TBC1D4-independent mechanisms (potentially involving TBC1D1) are likely to be essential for most of the contraction's effect. 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: 269967  Cd Length: 143  Bit Score: 248.75  E-value: 1.62e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627  164 EFDDTFAKKFEVLFCGRVTVAHKKAPPALIDECIEKFNHVSCGRrtdweaptgqpsapgprpmrksfsqpglrslafrke 243
Cdd:cd01269     1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEK------------------------------------ 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627  244 fqdasLRSstfssfdndienhligGHNVVQPTDMEENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDH 323
Cdd:cd01269    45 -----SRS----------------GPSSVQPTDSEENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDH 103

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 755511627  324 FGFICREcsGGGSGGFHFVCYVFQCTNEALVDEIMMTLKQAF 365
Cdd:cd01269   104 FGFICRE--SSEGGGFHFVCYVFKCQSESVVDEIMLTIKQAF 143
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 932-1101 2.29e-56

Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.


Pssm-ID: 459855  Cd Length: 178  Bit Score: 193.24  E-value: 2.29e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627   932 QHAILIDLGRTFPTHPYFsaQLGAGQLSLYNILKAYSLLDQEVGYCQGLSFVAGILLL-HMSEEEAFKMLKFLMFDMGLR 1010
Cdd:pfam00566    9 PEQIEKDVPRTFPHSFFF--DNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLR 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627  1011 KQYRPDMIILQIQMYQLSRLLHDYHRDLYNHLEEHEIGPSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEV-IFKVA 1089
Cdd:pfam00566   87 DFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVA 166

                          170
                   ....*....|..
gi 755511627  1090 LSLLGSHKPLIL 1101
Cdd:pfam00566  167 LAILKRFREELL 178
COG5210 COG5210
GTPase-activating protein [General function prediction only];
815-1115 8.37e-46

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 173.06  E-value: 8.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627  815 ILQQILLLRMEKENQKlqaseNDLLNKRLKLDYEEITPCLkevTTVWEKMLSTPGRSKIKFDMEKVHSAVGQGVPRHHRG 894
Cdd:COG5210   148 KGSSSLNSNPELNKEI-----NELSLKEEPQKLRYYELAA---DKLWISYLDPNPLSFLPVQLSKLRELIRKGIPNELRG 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627  895 EIWKFLaeqfhLKHPFPSKQQPKDVPYKELLKKLTSQQ-----HAILIDLGRTFPTHPYFSAQLGAGQLSLYNILKAYSL 969
Cdd:COG5210   220 DVWEFL-----LGIGFDLDKNPGLYERLLNLHREAKIPtqeiiSQIEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSL 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627  970 LDQEVGYCQGLSFVAGILLLHM-SEEEAFKMLKFLMFDMGLRKQYRPDMIILQIQMYQLSRLLHDYHRDLYNHLEEHEIG 1048
Cdd:COG5210   295 YNPEVGYVQGMNFLAAPLLLVLeSEEQAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVV 374

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511627 1049 PSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEVIFKVALSLLGSHKPLILQHENLETIVDFIKN 1115
Cdd:COG5210   375 LLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLDLLLKQ 441
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 777-832 1.50e-23

Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found in eukaryotic proteins, such as TBC1 domain family members 1 and 4. This presumed domain is typically between 50 to 64 amino acids in length. TBC domain proteins may act as GTPase-activating proteins for RAB2A, RAB8A, RAB10 and RAB14.


Pssm-ID: 463365  Cd Length: 63  Bit Score: 94.92  E-value: 1.50e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511627   777 ELPPRSPLEPVCEDGP-------FGPVQEEKRKTSRELRELWKKAILQQILLLRMEKENQKLQ 832
Cdd:pfam11830    1 ELLPLSPLAPGGEEDPagllsseDSPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 273-377 1.43e-21

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: 91.61  E-value: 1.43e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627    273 QPTDMEENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRECSGGgsggfHFVCYVFQCTNEA 352
Cdd:smart00462   36 QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIARDPGSS-----RFACHVFRCEKAA 110

                            90       100
                    ....*....|....*....|....*
gi 755511627    353 lvDEIMMTLKQAFTVAAVQQTAKAP 377
Cdd:smart00462  111 --EDIALAIGQAFQLAYELKLKARS 133
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 278-365 1.53e-15

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: 74.08  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627  278 EENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICREcsgggSGGFHFVCYVFQCTNEALVDEI 357
Cdd:cd00934    38 RKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDNPNVFAFIAGE-----EGGSGFRCHVFQCEDEEEAEEI 112


                  ....*...
gi 755511627  358 MMTLKQAF 365
Cdd:cd00934   113 LQAIGQAF 120
PTB_LOC417372 cd13168
uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of ...
 279-365 3.13e-06

uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of LOC417372 and its related proteins are unknown to date. Members here contain a N-terminal RUN domain, followed by a PDZ domain, and a C-terminal PTB domain. The RUN domain is involved in Ras-like GTPase signaling. The PDZ domain (also called DHR/Dlg homologous region or GLGF after its conserved sequence motif) binds C-terminal polypeptides, internal (non-C-terminal) polypeptides, and lipids. 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: 269989  Cd Length: 125  Bit Score: 47.71  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627  279 ENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRE--CSGGGsggfHFVCYVFQCTNEALVDE 356
Cdd:cd13168    36 TPKEVLLELGEIGVTVWDKSTSEVLFKHSFPEISSCGRRVDDPNYFAYIAGDtpCSLAK----HFVCYVFEAADEEEAET 111


                  ....*....
gi 755511627  357 IMMTLKQAF 365
Cdd:cd13168   112 ILQGIAQGF 120
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 292-368 6.99e-06

Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family Phosphotyrosine-binding (PTB) domain; Both AIDA-1b (AbetaPP intracellular domain-associated protein 1b) and Odin (also known as ankyrin repeat and sterile alpha motif domain-containing 1A; ANKS1A) belong to the Anks protein family. Both of these family members interacts with the EphA8 receptor. Ank members consists of ankyrin repeats, a SAM domain and a C-terminal PTB domain which is crucial for interaction with the juxtamembrane (JM) region of EphA8. PTB domains are classified into three groups, namely, phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains of which the Anks PTB is a member. 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: 269972  Cd Length: 146  Bit Score: 47.27  E-value: 6.99e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511627  292 VYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRECSGGgsggfHFVCYVFQCTNEALVDEIMMTLKQAFTVA 368
Cdd:cd01274    65 VKFIDATTKNLICEHEIRNISCACQDPEDLNTFAYITKDLKTD-----HHYCHVFCVLTVDLATEIILTLGQAFEVA 136
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 292-369 2.92e-04

Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK kinases catalyzes the transfer of the terminal phosphate of ATP to a specific tyrosine residue on its target protein. TK kinases play significant roles in development and cell division. Tyrosine-protein kinases can be divided into two subfamilies: receptor tyrosine kinases, which have an intracellular tyrosine kinase domain, a transmembrane domain and an extracellular ligand-binding domain; and non-receptor (cytoplasmic) tyrosine kinases, which are soluble, cytoplasmic kinases. In HMTK the conserved His-Arg-Asp sequence within the catalytic loop is replaced by a His-Met sequence. TM/HMTK have are 2-3 N-terminal PTB domains. PTB domains in TKs are thought to function analogously to the membrane targeting (PH, myristoylation) and pTyr binding (SH2) domains of Src subgroup kinases. 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: 269983  Cd Length: 120  Bit Score: 41.85  E-value: 2.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755511627  292 VYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRECSGGGSggfhfVCYVFQCTNEAlvDEIMMTLKQAFTVAA 369
Cdd:cd13161    49 IRVVERLTGEVLTNVPIKDISFVTVDPKDKKLFAFISHDPRLGRI-----TCHVFRCKRGA--QEICDTIAEAFKAAA 119
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 21-150 1.54e-03

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: 39.80  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627   21 FGLQLVGSLPVHSLTTMPMLpwVVAEVRRLSGQCSKKEPRTKqVRLWVSPSGLRCEpDLEKSQPwdplicssIFECKPQR 100
Cdd:cd00934     3 FQVKYLGSVEVGSSRGVDVV--EEALKALAAALKSSKRKPGP-VLLEVSSKGVKLL-DLDTKEL--------LLRHPLHR 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 755511627  101 VHKLIHNSHDPSYFaCLIKEDAAHRQSLCYVFKADDQTKVPEIISSIRQA 150
Cdd:cd00934    71 ISYCGRDPDNPNVF-AFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQA 119
PRK12704 PRK12704
phosphodiesterase; Provisional
 1139-1239 3.38e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627 1139 KQLQAYEvEYHVLQEELIESSPLSDN----------QRMEKLEKTNSSLRKQNLDLLEQLQVANARIQSLEATVEKLLTS 1208
Cdd:PRK12704   58 ALLEAKE-EIHKLRNEFEKELRERRNelqklekrllQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL 136

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 755511627 1209 ESKLKQ-----AALTLEVERSALLQMVE-ELRRQSAR 1239
Cdd:PRK12704  137 IEEQLQeleriSGLTAEEAKEILLEKVEeEARHEAAV 173
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 286-366 6.16e-03

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: 38.08  E-value: 6.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627  286 TIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRECSGGGSggfhfVCYVFQCTNEALVDEIMMTLKQAF 365
Cdd:cd13159    48 TVSPKGIKVTDSATNETILEVSIYRISYCTADANHDKVFAFIATNQDNEKL-----ECHAFLCAKRKMAQAVTLTVAQAF 122


                  .
gi 755511627  366 T 366
Cdd:cd13159   123 N 123
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1121-1236 8.63e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 8.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511627 1121 GLVQMEKTISQVFemDIAKQLQAYEVEYHVLQEELIESSplSDNQRM-EKLEKTNSSLRKQNLDLL---EQLQVANARIQ 1196
Cdd:COG4372    36 ALFELDKLQEELE--QLREELEQAREELEQLEEELEQAR--SELEQLeEELEELNEQLQAAQAELAqaqEELESLQEEAE 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 755511627 1197 SLEATVEKLLTSESKLKQAALTLEVERSALLQMVEELRRQ 1236
Cdd:COG4372   112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
 
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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