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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930258  164 EFDDTFSKKFEVLFCGRVTVAHKKAPPALIDECIEKFNHVSGSRGSesprpnpphaaptgsqepvrrpmrksfsqpglrs 243
Cdd:cd01269     1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEKSR---------------------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930258  244 lafrkelqdgglrssgffssfeesdienhliSGHNIVQPTDIEENRTMLFTkdkskrlpatlcwlkyssetIGQSEVYLI 323
Cdd:cd01269    47 -------------------------------SGPSSVQPTDSEENRTMLFQ--------------------IGRSELRLI 75

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767930258  324 SPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRESSGGGGFHFVCYVFQCTNEALVDEIMMTLKQAF 391
Cdd:cd01269    76 SPDTKQVLLEKQFKDISSCSQGIKHVDHFGFICRESSEGGGFHFVCYVFKCQSESVVDEIMLTIKQAF 143

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.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767930258   723 ELPPRSPLEPVCEDGP-------FGPPPEEKKRTSRELRELWQKAILQQILLLRMEKENQKLQ 778
Cdd:pfam11830    1 ELLPLSPLAPGGEEDPagllsseDSPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767930258 1127 NLDLLEQL----QVANGRIQSLEATIEKLLSSESKLKQAMLTLELERSALLQTVEELRRRSAEPSDR 1189
Cdd:COG3074     2 SLELLEELeakvQQAVDTIELLQMEVEELKEKNEELEQENEELQSENEELQSENEQLKTENAEWQER 68

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930258  164 EFDDTFSKKFEVLFCGRVTVAHKKAPPALIDECIEKFNHVSGSRGSesprpnpphaaptgsqepvrrpmrksfsqpglrs 243
Cdd:cd01269     1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEKSR---------------------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930258  244 lafrkelqdgglrssgffssfeesdienhliSGHNIVQPTDIEENRTMLFTkdkskrlpatlcwlkyssetIGQSEVYLI 323
Cdd:cd01269    47 -------------------------------SGPSSVQPTDSEENRTMLFQ--------------------IGRSELRLI 75

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767930258  324 SPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRESSGGGGFHFVCYVFQCTNEALVDEIMMTLKQAF 391
Cdd:cd01269    76 SPDTKQVLLEKQFKDISSCSQGIKHVDHFGFICRESSEGGGFHFVCYVFKCQSESVVDEIMLTIKQAF 143

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930258   878 QHAILIDLGRTFPTHPYFsaQLGAGQLSLYNILKAYSLLDQEVGYCQGLSFVAGILLL-HMSEEEAFKMLKFLMFDMGLR 956
Cdd:pfam00566    9 PEQIEKDVPRTFPHSFFF--DNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLR 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930258   957 KQYRPDMIILQIQMYQLSRLLHDYHRDLYNHLEEHEIGPSLYAAPWFLTMFASQFPLGFVARVFDMIFLQGTEV-IFKVA 1035
Cdd:pfam00566   87 DFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVA 166

                          170
                   ....*....|..
gi 767930258  1036 LSLLGSHKPLIL 1047
Cdd:pfam00566  167 LAILKRFREELL 178

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.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767930258   723 ELPPRSPLEPVCEDGP-------FGPPPEEKKRTSRELRELWQKAILQQILLLRMEKENQKLQ 778
Cdd:pfam11830    1 ELLPLSPLAPGGEEDPagllsseDSPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930258   21 FGLQLVGSLPVHSLTTMPMlpwVVAEVRRLSRQSTRKEPVTKQVRLCVSPSGLRCEpEPGRSQQWDPLIYSSIFECkpqr 100
Cdd:cd00934     3 FQVKYLGSVEVGSSRGVDV---VEEALKALAAALKSSKRKPGPVLLEVSSKGVKLL-DLDTKELLLRHPLHRISYC---- 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767930258  101 vhklIHNSHDPSYFACLIKEDAVhRQSICYVFKADDQTKVPEIISSIRQA 150
Cdd:cd00934    75 ----GRDPDNPNVFAFIAGEEGG-SGFRCHVFQCEDEEEAEEILQAIGQA 119

Phosphotyrosine interaction domain (PTB/PID);

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767930258   322 LISPDTKKIALEKNFKEISFCSQG-IRHVDHFGFICRessGGGGFHFVCYVFQCtnEALVDEIMMTLKQAFTVA 394
Cdd:pfam00640   65 LLNPDTQELIHDHPLVSISFCADGdPDLMRYFAYIAR---DKATNKFACHVFES--EDGAQDIAQSIGQAFALA 133

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930258  164 EFDDTFSKKFEVLFCGRVTVAHKKAPPALIDECIEKFNHVSGSRGSesprpnpphaaptgsqepvrrpmrksfsqpglrs 243
Cdd:cd01269     1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEKSR---------------------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930258  244 lafrkelqdgglrssgffssfeesdienhliSGHNIVQPTDIEENRTMLFTkdkskrlpatlcwlkyssetIGQSEVYLI 323
Cdd:cd01269    47 -------------------------------SGPSSVQPTDSEENRTMLFQ--------------------IGRSELRLI 75

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767930258  324 SPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRESSGGGGFHFVCYVFQCTNEALVDEIMMTLKQAF 391
Cdd:cd01269    76 SPDTKQVLLEKQFKDISSCSQGIKHVDHFGFICRESSEGGGFHFVCYVFKCQSESVVDEIMLTIKQAF 143

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930258   878 QHAILIDLGRTFPTHPYFsaQLGAGQLSLYNILKAYSLLDQEVGYCQGLSFVAGILLL-HMSEEEAFKMLKFLMFDMGLR 956
Cdd:pfam00566    9 PEQIEKDVPRTFPHSFFF--DNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLR 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930258   957 KQYRPDMIILQIQMYQLSRLLHDYHRDLYNHLEEHEIGPSLYAAPWFLTMFASQFPLGFVARVFDMIFLQGTEV-IFKVA 1035
Cdd:pfam00566   87 DFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVA 166

                          170
                   ....*....|..
gi 767930258  1036 LSLLGSHKPLIL 1047
Cdd:pfam00566  167 LAILKRFREELL 178

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.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767930258   723 ELPPRSPLEPVCEDGP-------FGPPPEEKKRTSRELRELWQKAILQQILLLRMEKENQKLQ 778
Cdd:pfam11830    1 ELLPLSPLAPGGEEDPagllsseDSPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930258  285 IEENRTMLFTKDKSKRLPATLCWLkysseTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRESsggGG 364
Cdd:cd00934    22 VEEALKALAAALKSSKRKPGPVLL-----EVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDNPNVFAFIAGEE---GG 93

                          90       100
                  ....*....|....*....|....*..
gi 767930258  365 FHFVCYVFQCTNEALVDEIMMTLKQAF 391
Cdd:cd00934    94 SGFRCHVFQCEDEEEAEEILQAIGQAF 120

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767930258  320 VYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRESSGGggfHFVCYVFQCTNEALVDEIMMTLKQAFTVA 394
Cdd:cd01274    65 VKFIDATTKNLICEHEIRNISCACQDPEDLNTFAYITKDLKTD---HHYCHVFCVLTVDLATEIILTLGQAFEVA 136

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930258   21 FGLQLVGSLPVHSLTTMPMlpwVVAEVRRLSRQSTRKEPVTKQVRLCVSPSGLRCEpEPGRSQQWDPLIYSSIFECkpqr 100
Cdd:cd00934     3 FQVKYLGSVEVGSSRGVDV---VEEALKALAAALKSSKRKPGPVLLEVSSKGVKLL-DLDTKELLLRHPLHRISYC---- 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767930258  101 vhklIHNSHDPSYFACLIKEDAVhRQSICYVFKADDQTKVPEIISSIRQA 150
Cdd:cd00934    75 ----GRDPDNPNVFAFIAGEEGG-SGFRCHVFQCEDEEEAEEILQAIGQA 119

Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also known as GULP1: engulfment adaptor PTB domain containing 1) is an adaptor protein involved in the specific recognition and engulfment of apoptotic cells. CED6 has been shown to interact with the cytoplasmic tail of another protein involved in the engulfment of apoptotic cells, CED1. CED6 has a C-terminal PTB domain, which can bind to NPXY motifs. 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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767930258  320 VYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRESSGGGgfHFvCYVFQCtnEALVDEIMMTLKQAFTVA 394
Cdd:cd01273    66 VKIQDPKTKVIMHQFPLHRISFCADDKTDKRIFSFIAKDSESEK--HL-CFVFDS--EKLAEEITLTIGQAFDLA 135

Phosphotyrosine interaction domain (PTB/PID);

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767930258   322 LISPDTKKIALEKNFKEISFCSQG-IRHVDHFGFICRessGGGGFHFVCYVFQCtnEALVDEIMMTLKQAFTVA 394
Cdd:pfam00640   65 LLNPDTQELIHDHPLVSISFCADGdPDLMRYFAYIAR---DKATNKFACHVFES--EDGAQDIAQSIGQAFALA 133