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Conserved domains on  [gi|575501701|ref|NP_001276443|]
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TBC1 domain family member 1 isoform 2 [Mus musculus]

Protein Classification

PTB_TBC1D1_like and TBC domain-containing protein( domain architecture ID 10101027)

protein containing domains PTB_TBC1D1_like, DUF3350, and TBC

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 ...
 662-879 2.40e-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: 252.61  E-value: 2.40e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701    662 VGQGVPRHHRGEIWKFLAEQFHLKHpfpskqQPKDVPYKELLK----KLTSQQHAILIDLGRTFPTHPYFSAQLGAGQLS 737
Cdd:smart00164    1 VRKGVPPSLRGVVWKLLLNAQPMDT------SADKDLYSRLLKetapDDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQES 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701    738 LYNILKAYSLLDQEVGYCQGLSFVAGILLLHM-SEEEAFKMLKFLMFDMGLRKqYRPDMIILQIQMYQLSRLLHDYHRDL 816
Cdd:smart00164   75 LRRVLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYGPNF-YLPDMSGLQLDLLQLDRLVKEYDPDL 153

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575501701    817 YNHLEEHEIGPSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEVIFKVALSLLGSHKPLIL 879
Cdd:smart00164  154 YKHLKDLGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
 35-236 2.72e-77

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: 249.52  E-value: 2.72e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701   35 EFDDTFAKKFEVLFCGRVTVAHKKAPPALIDECIEKFNHVSCGRrtdweaptgqpsapgprpmrksfsqpglrslafrke 114
Cdd:cd01269     1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEK------------------------------------ 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701  115 fqdasLRSstfssfdndienhligGHNVVQPTDMEENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDH 194
Cdd:cd01269    45 -----SRS----------------GPSSVQPTDSEENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDH 103

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 575501701  195 FGFICREcsGGGSGGFHFVCYVFQCTNEALVDEIMMTLKQAF 236
Cdd:cd01269   104 FGFICRE--SSEGGGFHFVCYVFKCQSESVVDEIMLTIKQAF 143
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 555-610 4.92e-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: 93.38  E-value: 4.92e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575501701   555 ELPPRSPLEPVCEDGP-------FGPVQEEKRKTSRELRELWKKAILQQILLLRMEKENQKLQ 610
Cdd:pfam11830    1 ELLPLSPLAPGGEEDPagllsseDSPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63
PRK12704 super family cl36166
phosphodiesterase; Provisional
 917-1017 5.27e-03

phosphodiesterase; Provisional


The actual alignment was detected with superfamily member PRK12704:

Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701  917 KQLQAYEvEYHVLQEELIESSPLSDN----------QRMEKLEKTNSSLRKQNLDLLEQLQVANARIQSLEATVEKLLTS 986
Cdd:PRK12704   58 ALLEAKE-EIHKLRNEFEKELRERRNelqklekrllQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL 136

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 575501701  987 ESKLKQ-----AALTLEVERSALLQMVE-ELRRQSAR 1017
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 ...
 662-879 2.40e-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: 252.61  E-value: 2.40e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701    662 VGQGVPRHHRGEIWKFLAEQFHLKHpfpskqQPKDVPYKELLK----KLTSQQHAILIDLGRTFPTHPYFSAQLGAGQLS 737
Cdd:smart00164    1 VRKGVPPSLRGVVWKLLLNAQPMDT------SADKDLYSRLLKetapDDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQES 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701    738 LYNILKAYSLLDQEVGYCQGLSFVAGILLLHM-SEEEAFKMLKFLMFDMGLRKqYRPDMIILQIQMYQLSRLLHDYHRDL 816
Cdd:smart00164   75 LRRVLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYGPNF-YLPDMSGLQLDLLQLDRLVKEYDPDL 153

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575501701    817 YNHLEEHEIGPSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEVIFKVALSLLGSHKPLIL 879
Cdd:smart00164  154 YKHLKDLGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
 35-236 2.72e-77

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: 249.52  E-value: 2.72e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701   35 EFDDTFAKKFEVLFCGRVTVAHKKAPPALIDECIEKFNHVSCGRrtdweaptgqpsapgprpmrksfsqpglrslafrke 114
Cdd:cd01269     1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEK------------------------------------ 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701  115 fqdasLRSstfssfdndienhligGHNVVQPTDMEENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDH 194
Cdd:cd01269    45 -----SRS----------------GPSSVQPTDSEENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDH 103

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 575501701  195 FGFICREcsGGGSGGFHFVCYVFQCTNEALVDEIMMTLKQAF 236
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 ...
 710-879 4.97e-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: 191.70  E-value: 4.97e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701   710 QHAILIDLGRTFPTHPYFsaQLGAGQLSLYNILKAYSLLDQEVGYCQGLSFVAGILLL-HMSEEEAFKMLKFLMFDMGLR 788
Cdd:pfam00566    9 PEQIEKDVPRTFPHSFFF--DNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLR 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701   789 KQYRPDMIILQIQMYQLSRLLHDYHRDLYNHLEEHEIGPSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEV-IFKVA 867
Cdd:pfam00566   87 DFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVA 166

                          170
                   ....*....|..
gi 575501701   868 LSLLGSHKPLIL 879
Cdd:pfam00566  167 LAILKRFREELL 178
COG5210 COG5210
GTPase-activating protein [General function prediction only];
593-893 7.92e-46

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 172.68  E-value: 7.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701  593 ILQQILLLRMEKENQKlqaseNDLLNKRLKLDYEEITPCLkevTTVWEKMLSTPGRSKIKFDMEKVHSAVGQGVPRHHRG 672
Cdd:COG5210   148 KGSSSLNSNPELNKEI-----NELSLKEEPQKLRYYELAA---DKLWISYLDPNPLSFLPVQLSKLRELIRKGIPNELRG 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701  673 EIWKFLaeqfhLKHPFPSKQQPKDVPYKELLKKLTSQQ-----HAILIDLGRTFPTHPYFSAQLGAGQLSLYNILKAYSL 747
Cdd:COG5210   220 DVWEFL-----LGIGFDLDKNPGLYERLLNLHREAKIPtqeiiSQIEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSL 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701  748 LDQEVGYCQGLSFVAGILLLHM-SEEEAFKMLKFLMFDMGLRKQYRPDMIILQIQMYQLSRLLHDYHRDLYNHLEEHEIG 826
Cdd:COG5210   295 YNPEVGYVQGMNFLAAPLLLVLeSEEQAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVV 374

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575501701  827 PSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEVIFKVALSLLGSHKPLILQHENLETIVDFIKN 893
Cdd:COG5210   375 LLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLDLLLKQ 441
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 555-610 4.92e-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: 93.38  E-value: 4.92e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575501701   555 ELPPRSPLEPVCEDGP-------FGPVQEEKRKTSRELRELWKKAILQQILLLRMEKENQKLQ 610
Cdd:pfam11830    1 ELLPLSPLAPGGEEDPagllsseDSPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 144-248 1.09e-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: 91.99  E-value: 1.09e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701    144 QPTDMEENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRECSGGgsggfHFVCYVFQCTNEA 223
Cdd:smart00462   36 QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIARDPGSS-----RFACHVFRCEKAA 110

                            90       100
                    ....*....|....*....|....*
gi 575501701    224 lvDEIMMTLKQAFTVAAVQQTAKAP 248
Cdd:smart00462  111 --EDIALAIGQAFQLAYELKLKARS 133
PRK12704 PRK12704
phosphodiesterase; Provisional
 917-1017 5.27e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701  917 KQLQAYEvEYHVLQEELIESSPLSDN----------QRMEKLEKTNSSLRKQNLDLLEQLQVANARIQSLEATVEKLLTS 986
Cdd:PRK12704   58 ALLEAKE-EIHKLRNEFEKELRERRNelqklekrllQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL 136

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 575501701  987 ESKLKQ-----AALTLEVERSALLQMVE-ELRRQSAR 1017
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 ...
 662-879 2.40e-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: 252.61  E-value: 2.40e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701    662 VGQGVPRHHRGEIWKFLAEQFHLKHpfpskqQPKDVPYKELLK----KLTSQQHAILIDLGRTFPTHPYFSAQLGAGQLS 737
Cdd:smart00164    1 VRKGVPPSLRGVVWKLLLNAQPMDT------SADKDLYSRLLKetapDDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQES 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701    738 LYNILKAYSLLDQEVGYCQGLSFVAGILLLHM-SEEEAFKMLKFLMFDMGLRKqYRPDMIILQIQMYQLSRLLHDYHRDL 816
Cdd:smart00164   75 LRRVLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYGPNF-YLPDMSGLQLDLLQLDRLVKEYDPDL 153

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575501701    817 YNHLEEHEIGPSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEVIFKVALSLLGSHKPLIL 879
Cdd:smart00164  154 YKHLKDLGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
 35-236 2.72e-77

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: 249.52  E-value: 2.72e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701   35 EFDDTFAKKFEVLFCGRVTVAHKKAPPALIDECIEKFNHVSCGRrtdweaptgqpsapgprpmrksfsqpglrslafrke 114
Cdd:cd01269     1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEK------------------------------------ 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701  115 fqdasLRSstfssfdndienhligGHNVVQPTDMEENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDH 194
Cdd:cd01269    45 -----SRS----------------GPSSVQPTDSEENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDH 103

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 575501701  195 FGFICREcsGGGSGGFHFVCYVFQCTNEALVDEIMMTLKQAF 236
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 ...
 710-879 4.97e-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: 191.70  E-value: 4.97e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701   710 QHAILIDLGRTFPTHPYFsaQLGAGQLSLYNILKAYSLLDQEVGYCQGLSFVAGILLL-HMSEEEAFKMLKFLMFDMGLR 788
Cdd:pfam00566    9 PEQIEKDVPRTFPHSFFF--DNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLR 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701   789 KQYRPDMIILQIQMYQLSRLLHDYHRDLYNHLEEHEIGPSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEV-IFKVA 867
Cdd:pfam00566   87 DFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVA 166

                          170
                   ....*....|..
gi 575501701   868 LSLLGSHKPLIL 879
Cdd:pfam00566  167 LAILKRFREELL 178
COG5210 COG5210
GTPase-activating protein [General function prediction only];
593-893 7.92e-46

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 172.68  E-value: 7.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701  593 ILQQILLLRMEKENQKlqaseNDLLNKRLKLDYEEITPCLkevTTVWEKMLSTPGRSKIKFDMEKVHSAVGQGVPRHHRG 672
Cdd:COG5210   148 KGSSSLNSNPELNKEI-----NELSLKEEPQKLRYYELAA---DKLWISYLDPNPLSFLPVQLSKLRELIRKGIPNELRG 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701  673 EIWKFLaeqfhLKHPFPSKQQPKDVPYKELLKKLTSQQ-----HAILIDLGRTFPTHPYFSAQLGAGQLSLYNILKAYSL 747
Cdd:COG5210   220 DVWEFL-----LGIGFDLDKNPGLYERLLNLHREAKIPtqeiiSQIEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSL 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701  748 LDQEVGYCQGLSFVAGILLLHM-SEEEAFKMLKFLMFDMGLRKQYRPDMIILQIQMYQLSRLLHDYHRDLYNHLEEHEIG 826
Cdd:COG5210   295 YNPEVGYVQGMNFLAAPLLLVLeSEEQAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVV 374

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575501701  827 PSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEVIFKVALSLLGSHKPLILQHENLETIVDFIKN 893
Cdd:COG5210   375 LLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLDLLLKQ 441
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 555-610 4.92e-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: 93.38  E-value: 4.92e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575501701   555 ELPPRSPLEPVCEDGP-------FGPVQEEKRKTSRELRELWKKAILQQILLLRMEKENQKLQ 610
Cdd:pfam11830    1 ELLPLSPLAPGGEEDPagllsseDSPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 144-248 1.09e-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: 91.99  E-value: 1.09e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701    144 QPTDMEENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRECSGGgsggfHFVCYVFQCTNEA 223
Cdd:smart00462   36 QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIARDPGSS-----RFACHVFRCEKAA 110

                            90       100
                    ....*....|....*....|....*
gi 575501701    224 lvDEIMMTLKQAFTVAAVQQTAKAP 248
Cdd:smart00462  111 --EDIALAIGQAFQLAYELKLKARS 133
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 149-236 1.05e-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: 74.47  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701  149 EENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICREcsgggSGGFHFVCYVFQCTNEALVDEI 228
Cdd:cd00934    38 RKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDNPNVFAFIAGE-----EGGSGFRCHVFQCEDEEEAEEI 112


                  ....*...
gi 575501701  229 MMTLKQAF 236
Cdd:cd00934   113 LQAIGQAF 120
PTB_LOC417372 cd13168
uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of ...
 150-236 2.47e-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: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701  150 ENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRE--CSGGGsggfHFVCYVFQCTNEALVDE 227
Cdd:cd13168    36 TPKEVLLELGEIGVTVWDKSTSEVLFKHSFPEISSCGRRVDDPNYFAYIAGDtpCSLAK----HFVCYVFEAADEEEAET 111


                  ....*....
gi 575501701  228 IMMTLKQAF 236
Cdd:cd13168   112 ILQGIAQGF 120
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 163-239 6.18e-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: 46.89  E-value: 6.18e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575501701  163 VYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRECSGGgsggfHFVCYVFQCTNEALVDEIMMTLKQAFTVA 239
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 ...
 163-240 2.27e-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: 2.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575501701  163 VYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRECSGGGSggfhfVCYVFQCTNEAlvDEIMMTLKQAFTVAA 240
Cdd:cd13161    49 IRVVERLTGEVLTNVPIKDISFVTVDPKDKKLFAFISHDPRLGRI-----TCHVFRCKRGA--QEICDTIAEAFKAAA 119
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 157-237 4.96e-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: 4.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701  157 TIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRECSGGGSggfhfVCYVFQCTNEALVDEIMMTLKQAF 236
Cdd:cd13159    48 TVSPKGIKVTDSATNETILEVSIYRISYCTADANHDKVFAFIATNQDNEKL-----ECHAFLCAKRKMAQAVTLTVAQAF 122


                  .
gi 575501701  237 T 237
Cdd:cd13159   123 N 123
PRK12704 PRK12704
phosphodiesterase; Provisional
 917-1017 5.27e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501701  917 KQLQAYEvEYHVLQEELIESSPLSDN----------QRMEKLEKTNSSLRKQNLDLLEQLQVANARIQSLEATVEKLLTS 986
Cdd:PRK12704   58 ALLEAKE-EIHKLRNEFEKELRERRNelqklekrllQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL 136

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 575501701  987 ESKLKQ-----AALTLEVERSALLQMVE-ELRRQSAR 1017
Cdd:PRK12704  137 IEEQLQeleriSGLTAEEAKEILLEKVEeEARHEAAV 173
 
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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