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Conserved domains on  [gi|1958682065|ref|XP_038949897|]
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TBC1 domain family member 4 isoform X1 [Rattus norvegicus]

Protein Classification

PTB domain-containing protein( domain architecture ID 10648786)

PTB (phosphotyrosine-binding) domain-containing protein similar to Caenorhabditis elegans PID domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
 193-446 1.13e-72

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: 237.96  E-value: 1.13e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  193 EDAFYNSQKFEVLYCGRVIVTHKKAPSSLIDDCKDKFSLHEQQRLKlqgerggdpgdgdemgvleaespvspddglpekp 272
Cdd:cd01269      1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEKSR---------------------------------- 46

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  273 dglvncpralpslaslpalasqpalassrvcfperiledcgfdeqqefrsrcssvtgvmqkkvhennqktqprrrhaSAP 352
Cdd:cd01269     47 -----------------------------------------------------------------------------SGP 49

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  353 SHVQPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESLEPGLSQYICYVFQCANE 432
Cdd:cd01269     50 SSVQPTDSEENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDHFGFICRESSEGGGFHFVCYVFKCQSE 129

                          250
                   ....*....|....
gi 1958682065  433 SLVDEVMLTLKQAF 446
Cdd:cd01269    130 SVVDEIMLTIKQAF 143
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 873-1083 7.44e-70

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: 232.97  E-value: 7.44e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065   873 GVPKSRRGEIWQFLALQYrlrhrlPNKHQPPDTSYKELLKQ----LTAQQHAILVDLGRTFPTQPYFSVQLGAGQLSLFN 948
Cdd:smart00164    4 GVPPSLRGVVWKLLLNAQ------PMDTSADKDLYSRLLKEtapdDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQESLRR 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065   949 LLKAYSLLDKEVGYCQGISFVAGVLLLHM-SEEQAFEMLKFLMYDLGfRKQYRPDMMSLQIQMYQLSRLLHDYHRDLYNH 1027
Cdd:smart00164   78 VLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYG-PNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKH 156

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958682065  1028 LEENEISPSLYAAPWFLTLFASQFPLGFVARVFDIIFLQGTEVIFKVALSLLSSQE 1083
Cdd:smart00164  157 LKDLGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHR 212
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 31-190 5.31e-19

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: 84.29  E-value: 5.31e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065    31 PGDKRFRLWYVGGSCLDRRTTLPMLPWLMAEIRrrslkpEAGGCGAPAAREVLLVLSAPFLRCVpapgvgvgggagsgav 110
Cdd:smart00462    1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLR------AAQGSEKKEPQKVILSISSRGVKLI---------------- 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065   111 QPNTGVFIFEHKAQHISRFIHNSHDLTYFAYLIKaqpDDPESQMACHVFRATDPNqvPDVISSIRQLSKAAMKEDAKPSK 190
Cdd:smart00462   59 DEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIAR---DPGSSRFACHVFRCEKAA--EDIALAIGQAFQLAYELKLKARS 133
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 756-819 5.88e-19

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: 81.82  E-value: 5.88e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958682065  756 ELLPLSPLSPTMEEEPlVIFLSGDEDTEKVEEKKKSKEIKSLWKKAIHQQILLLRMEKENQKLE 819
Cdd:pfam11830    1 ELLPLSPLAPGGEEDP-AGLLSSEDSPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63
PTZ00440 super family cl36566
reticulocyte binding protein 2-like protein; Provisional
 1087-1218 7.85e-04

reticulocyte binding protein 2-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00440:

Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 44.05  E-value: 7.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065 1087 MECENFENIVEFLKSTLPDMNTTE--MEKIITQVFEMDISKQLHAYEVEYHVLQDELleSSYAcEDNESLEKLEraNNQL 1164
Cdd:PTZ00440   681 MKSDNIDNIIKNLKKELQNLLSLKenIIKKQLNNIEQDISNSLNQYTIKYNDLKSSI--EEYK-EEEEKLEVYK--HQII 755

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065 1165 KRQNMDLL------EKLQVAHAKIQALESNLETLLTRETKMKALIRTLEQDKMAYQKTVE 1218
Cdd:PTZ00440   756 NRKNEFILhlyendKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLN 815
 
Name Accession Description Interval E-value
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
 193-446 1.13e-72

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: 237.96  E-value: 1.13e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  193 EDAFYNSQKFEVLYCGRVIVTHKKAPSSLIDDCKDKFSLHEQQRLKlqgerggdpgdgdemgvleaespvspddglpekp 272
Cdd:cd01269      1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEKSR---------------------------------- 46

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  273 dglvncpralpslaslpalasqpalassrvcfperiledcgfdeqqefrsrcssvtgvmqkkvhennqktqprrrhaSAP 352
Cdd:cd01269     47 -----------------------------------------------------------------------------SGP 49

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  353 SHVQPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESLEPGLSQYICYVFQCANE 432
Cdd:cd01269     50 SSVQPTDSEENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDHFGFICRESSEGGGFHFVCYVFKCQSE 129

                          250
                   ....*....|....
gi 1958682065  433 SLVDEVMLTLKQAF 446
Cdd:cd01269    130 SVVDEIMLTIKQAF 143
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 873-1083 7.44e-70

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: 232.97  E-value: 7.44e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065   873 GVPKSRRGEIWQFLALQYrlrhrlPNKHQPPDTSYKELLKQ----LTAQQHAILVDLGRTFPTQPYFSVQLGAGQLSLFN 948
Cdd:smart00164    4 GVPPSLRGVVWKLLLNAQ------PMDTSADKDLYSRLLKEtapdDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQESLRR 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065   949 LLKAYSLLDKEVGYCQGISFVAGVLLLHM-SEEQAFEMLKFLMYDLGfRKQYRPDMMSLQIQMYQLSRLLHDYHRDLYNH 1027
Cdd:smart00164   78 VLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYG-PNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKH 156

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958682065  1028 LEENEISPSLYAAPWFLTLFASQFPLGFVARVFDIIFLQGTEVIFKVALSLLSSQE 1083
Cdd:smart00164  157 LKDLGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHR 212
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 918-1083 5.16e-55

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: 189.00  E-value: 5.16e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  918 QHAILVDLGRTFPTQPYFsvQLGAGQLSLFNLLKAYSLLDKEVGYCQGISFVAGVLLL-HMSEEQAFEMLKFLMYDLGFR 996
Cdd:pfam00566    9 PEQIEKDVPRTFPHSFFF--DNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLR 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  997 KQYRPDMMSLQIQMYQLSRLLHDYHRDLYNHLEENEISPSLYAAPWFLTLFASQFPLGFVARVFDIIFLQGTEV-IFKVA 1075
Cdd:pfam00566   87 DFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVA 166


                   ....*...
gi 1958682065 1076 LSLLSSQE 1083
Cdd:pfam00566  167 LAILKRFR 174
COG5210 COG5210
GTPase-activating protein [General function prediction only];
870-1128 2.47e-45

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 171.52  E-value: 2.47e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  870 LKEGVPKSRRGEIWQFLALQYRLRHRLPNKHqPPDTSYKELLKQLTAQQ-HAILVDLGRTFPTQPYFSVQLGAGQLSLFN 948
Cdd:COG5210    209 IRKGIPNELRGDVWEFLLGIGFDLDKNPGLY-ERLLNLHREAKIPTQEIiSQIEKDLSRTFPDNSLFQTEISIRAENLRR 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  949 LLKAYSLLDKEVGYCQGISFVAGVLLLHM-SEEQAFEMLKFLMYDLGFRKQYRPDMMSLQIQMYQLSRLLHDYHRDLYNH 1027
Cdd:COG5210    288 VLKAYSLYNPEVGYVQGMNFLAAPLLLVLeSEEQAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPELYEH 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065 1028 LEENEISPSLYAAPWFLTLFASQFPLGFVARVFDIIFLQGTEVIFKVALSLLSSQEALVMECeNFENIVEFLKSTLPDMN 1107
Cdd:COG5210    368 LLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL-DSDELLDLLLKQLFLHS 446

                          250       260
                   ....*....|....*....|.
gi 1958682065 1108 TTEMEKIITQVFEMDISKQLH 1128
Cdd:COG5210    447 GKEAWSSILKFRHGTDRDILL 467
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 356-459 6.66e-23

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: 95.46  E-value: 6.66e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065   356 QPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICReslEPGLSQYICYVFQCANESlv 435
Cdd:smart00462   36 QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIAR---DPGSSRFACHVFRCEKAA-- 110

                            90       100
                    ....*....|....*....|....
gi 1958682065   436 DEVMLTLKQAFSTAAALQSAKTQI 459
Cdd:smart00462  111 EDIALAIGQAFQLAYELKLKARSE 134
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 31-190 5.31e-19

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: 84.29  E-value: 5.31e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065    31 PGDKRFRLWYVGGSCLDRRTTLPMLPWLMAEIRrrslkpEAGGCGAPAAREVLLVLSAPFLRCVpapgvgvgggagsgav 110
Cdd:smart00462    1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLR------AAQGSEKKEPQKVILSISSRGVKLI---------------- 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065   111 QPNTGVFIFEHKAQHISRFIHNSHDLTYFAYLIKaqpDDPESQMACHVFRATDPNqvPDVISSIRQLSKAAMKEDAKPSK 190
Cdd:smart00462   59 DEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIAR---DPGSSRFACHVFRCEKAA--EDIALAIGQAFQLAYELKLKARS 133
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 756-819 5.88e-19

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: 81.82  E-value: 5.88e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958682065  756 ELLPLSPLSPTMEEEPlVIFLSGDEDTEKVEEKKKSKEIKSLWKKAIHQQILLLRMEKENQKLE 819
Cdd:pfam11830    1 ELLPLSPLAPGGEEDP-AGLLSSEDSPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 112-176 9.91e-05

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: 43.27  E-value: 9.91e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958682065  112 PNTGVFIFEHKAQHISRFIHNSHDLTYFAYLIKaqpDDPESQMACHVFRATDPNQVPDVISSIRQ 176
Cdd:cd00934     57 LDTKELLLRHPLHRISYCGRDPDNPNVFAFIAG---EEGGSGFRCHVFQCEDEEEAEEILQAIGQ 118
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 1087-1218 7.85e-04

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 44.05  E-value: 7.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065 1087 MECENFENIVEFLKSTLPDMNTTE--MEKIITQVFEMDISKQLHAYEVEYHVLQDELleSSYAcEDNESLEKLEraNNQL 1164
Cdd:PTZ00440   681 MKSDNIDNIIKNLKKELQNLLSLKenIIKKQLNNIEQDISNSLNQYTIKYNDLKSSI--EEYK-EEEEKLEVYK--HQII 755

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065 1165 KRQNMDLL------EKLQVAHAKIQALESNLETLLTRETKMKALIRTLEQDKMAYQKTVE 1218
Cdd:PTZ00440   756 NRKNEFILhlyendKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLN 815
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
112-176 1.37e-03

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 40.04  E-value: 1.37e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958682065  112 PNTGVFIFEHKAQHISrFIHNSH--DLTYFAYLIKaqpDDPESQMACHVFRATDPNQvpDVISSIRQ 176
Cdd:pfam00640   68 PDTQELIHDHPLVSIS-FCADGDpdLMRYFAYIAR---DKATNKFACHVFESEDGAQ--DIAQSIGQ 128
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
375-449 2.44e-03

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 39.65  E-value: 2.44e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958682065  375 INLISPDTKSVVLEKNFKDISSCSQG-IKHVDHFGFICReslEPGLSQYICYVFQCanESLVDEVMLTLKQAFSTA 449
Cdd:pfam00640   63 LKLLNPDTQELIHDHPLVSISFCADGdPDLMRYFAYIAR---DKATNKFACHVFES--EDGAQDIAQSIGQAFALA 133
 
Name Accession Description Interval E-value
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
 193-446 1.13e-72

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: 237.96  E-value: 1.13e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  193 EDAFYNSQKFEVLYCGRVIVTHKKAPSSLIDDCKDKFSLHEQQRLKlqgerggdpgdgdemgvleaespvspddglpekp 272
Cdd:cd01269      1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEKSR---------------------------------- 46

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  273 dglvncpralpslaslpalasqpalassrvcfperiledcgfdeqqefrsrcssvtgvmqkkvhennqktqprrrhaSAP 352
Cdd:cd01269     47 -----------------------------------------------------------------------------SGP 49

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  353 SHVQPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESLEPGLSQYICYVFQCANE 432
Cdd:cd01269     50 SSVQPTDSEENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDHFGFICRESSEGGGFHFVCYVFKCQSE 129

                          250
                   ....*....|....
gi 1958682065  433 SLVDEVMLTLKQAF 446
Cdd:cd01269    130 SVVDEIMLTIKQAF 143
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 873-1083 7.44e-70

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: 232.97  E-value: 7.44e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065   873 GVPKSRRGEIWQFLALQYrlrhrlPNKHQPPDTSYKELLKQ----LTAQQHAILVDLGRTFPTQPYFSVQLGAGQLSLFN 948
Cdd:smart00164    4 GVPPSLRGVVWKLLLNAQ------PMDTSADKDLYSRLLKEtapdDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQESLRR 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065   949 LLKAYSLLDKEVGYCQGISFVAGVLLLHM-SEEQAFEMLKFLMYDLGfRKQYRPDMMSLQIQMYQLSRLLHDYHRDLYNH 1027
Cdd:smart00164   78 VLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYG-PNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKH 156

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958682065  1028 LEENEISPSLYAAPWFLTLFASQFPLGFVARVFDIIFLQGTEVIFKVALSLLSSQE 1083
Cdd:smart00164  157 LKDLGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHR 212
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 918-1083 5.16e-55

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: 189.00  E-value: 5.16e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  918 QHAILVDLGRTFPTQPYFsvQLGAGQLSLFNLLKAYSLLDKEVGYCQGISFVAGVLLL-HMSEEQAFEMLKFLMYDLGFR 996
Cdd:pfam00566    9 PEQIEKDVPRTFPHSFFF--DNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLR 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  997 KQYRPDMMSLQIQMYQLSRLLHDYHRDLYNHLEENEISPSLYAAPWFLTLFASQFPLGFVARVFDIIFLQGTEV-IFKVA 1075
Cdd:pfam00566   87 DFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVA 166


                   ....*...
gi 1958682065 1076 LSLLSSQE 1083
Cdd:pfam00566  167 LAILKRFR 174
COG5210 COG5210
GTPase-activating protein [General function prediction only];
870-1128 2.47e-45

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 171.52  E-value: 2.47e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  870 LKEGVPKSRRGEIWQFLALQYRLRHRLPNKHqPPDTSYKELLKQLTAQQ-HAILVDLGRTFPTQPYFSVQLGAGQLSLFN 948
Cdd:COG5210    209 IRKGIPNELRGDVWEFLLGIGFDLDKNPGLY-ERLLNLHREAKIPTQEIiSQIEKDLSRTFPDNSLFQTEISIRAENLRR 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  949 LLKAYSLLDKEVGYCQGISFVAGVLLLHM-SEEQAFEMLKFLMYDLGFRKQYRPDMMSLQIQMYQLSRLLHDYHRDLYNH 1027
Cdd:COG5210    288 VLKAYSLYNPEVGYVQGMNFLAAPLLLVLeSEEQAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPELYEH 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065 1028 LEENEISPSLYAAPWFLTLFASQFPLGFVARVFDIIFLQGTEVIFKVALSLLSSQEALVMECeNFENIVEFLKSTLPDMN 1107
Cdd:COG5210    368 LLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL-DSDELLDLLLKQLFLHS 446

                          250       260
                   ....*....|....*....|.
gi 1958682065 1108 TTEMEKIITQVFEMDISKQLH 1128
Cdd:COG5210    447 GKEAWSSILKFRHGTDRDILL 467
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 356-459 6.66e-23

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: 95.46  E-value: 6.66e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065   356 QPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICReslEPGLSQYICYVFQCANESlv 435
Cdd:smart00462   36 QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIAR---DPGSSRFACHVFRCEKAA-- 110

                            90       100
                    ....*....|....*....|....
gi 1958682065   436 DEVMLTLKQAFSTAAALQSAKTQI 459
Cdd:smart00462  111 EDIALAIGQAFQLAYELKLKARSE 134
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 31-190 5.31e-19

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: 84.29  E-value: 5.31e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065    31 PGDKRFRLWYVGGSCLDRRTTLPMLPWLMAEIRrrslkpEAGGCGAPAAREVLLVLSAPFLRCVpapgvgvgggagsgav 110
Cdd:smart00462    1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLR------AAQGSEKKEPQKVILSISSRGVKLI---------------- 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065   111 QPNTGVFIFEHKAQHISRFIHNSHDLTYFAYLIKaqpDDPESQMACHVFRATDPNqvPDVISSIRQLSKAAMKEDAKPSK 190
Cdd:smart00462   59 DEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIAR---DPGSSRFACHVFRCEKAA--EDIALAIGQAFQLAYELKLKARS 133
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 756-819 5.88e-19

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: 81.82  E-value: 5.88e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958682065  756 ELLPLSPLSPTMEEEPlVIFLSGDEDTEKVEEKKKSKEIKSLWKKAIHQQILLLRMEKENQKLE 819
Cdd:pfam11830    1 ELLPLSPLAPGGEEDP-AGLLSSEDSPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 349-446 7.19e-18

Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269911  Cd Length: 120  Bit Score: 80.63  E-value: 7.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  349 ASAPSHVQPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICReslEPGLSQYICYVFQ 428
Cdd:cd00934     26 LKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDNPNVFAFIAG---EEGGSGFRCHVFQ 102

                           90
                   ....*....|....*...
gi 1958682065  429 CANESLVDEVMLTLKQAF 446
Cdd:cd00934    103 CEDEEEAEEILQAIGQAF 120
PTB_LOC417372 cd13168
uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of ...
 362-446 7.18e-07

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: 49.25  E-value: 7.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  362 KNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESLEPGLSQYICYVFQCANESLVDEVMLT 441
Cdd:cd13168     36 TPKEVLLELGEIGVTVWDKSTSEVLFKHSFPEISSCGRRVDDPNYFAYIAGDTPCSLAKHFVCYVFEAADEEEAETILQG 115


                   ....*
gi 1958682065  442 LKQAF 446
Cdd:cd13168    116 IAQGF 120
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 375-457 2.41e-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: 48.43  E-value: 2.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065  375 INLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESLEpglSQYICYVFQCANESLVDEVMLTLKQAFSTA--AAL 452
Cdd:cd01274     65 VKFIDATTKNLICEHEIRNISCACQDPEDLNTFAYITKDLKT---DHHYCHVFCVLTVDLATEIILTLGQAFEVAyqLAL 141


                   ....*
gi 1958682065  453 QSAKT 457
Cdd:cd01274    142 RAQKS 146
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 374-447 2.38e-05

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: 45.02  E-value: 2.38e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958682065  374 EINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESLEPGLSqyiCYVFQCANESLVDEVMLTLKQAFS 447
Cdd:cd13159     53 GIKVTDSATNETILEVSIYRISYCTADANHDKVFAFIATNQDNEKLE---CHAFLCAKRKMAQAVTLTVAQAFN 123
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 112-176 9.91e-05

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: 43.27  E-value: 9.91e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958682065  112 PNTGVFIFEHKAQHISRFIHNSHDLTYFAYLIKaqpDDPESQMACHVFRATDPNQVPDVISSIRQ 176
Cdd:cd00934     57 LDTKELLLRHPLHRISYCGRDPDNPNVFAFIAG---EEGGSGFRCHVFQCEDEEEAEEILQAIGQ 118
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 375-451 3.82e-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: 41.46  E-value: 3.82e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958682065  375 INLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICReslEPGLSQYICYVFQCANESlvDEVMLTLKQAFSTAAA 451
Cdd:cd13161     49 IRVVERLTGEVLTNVPIKDISFVTVDPKDKKLFAFISH---DPRLGRITCHVFRCKRGA--QEICDTIAEAFKAAAE 120
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 112-176 5.04e-04

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: 41.88  E-value: 5.04e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958682065  112 PNTGVFIFEHKAQHISRFIHNSHDLTYFAYLIKaqpDDPESQMACHVFRATDPNQVPDVISSIRQ 176
Cdd:cd01274     70 ATTKNLICEHEIRNISCACQDPEDLNTFAYITK---DLKTDHHYCHVFCVLTVDLATEIILTLGQ 131
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 1087-1218 7.85e-04

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 44.05  E-value: 7.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065 1087 MECENFENIVEFLKSTLPDMNTTE--MEKIITQVFEMDISKQLHAYEVEYHVLQDELleSSYAcEDNESLEKLEraNNQL 1164
Cdd:PTZ00440   681 MKSDNIDNIIKNLKKELQNLLSLKenIIKKQLNNIEQDISNSLNQYTIKYNDLKSSI--EEYK-EEEEKLEVYK--HQII 755

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682065 1165 KRQNMDLL------EKLQVAHAKIQALESNLETLLTRETKMKALIRTLEQDKMAYQKTVE 1218
Cdd:PTZ00440   756 NRKNEFILhlyendKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLN 815
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
112-176 1.37e-03

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 40.04  E-value: 1.37e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958682065  112 PNTGVFIFEHKAQHISrFIHNSH--DLTYFAYLIKaqpDDPESQMACHVFRATDPNQvpDVISSIRQ 176
Cdd:pfam00640   68 PDTQELIHDHPLVSIS-FCADGDpdLMRYFAYIAR---DKATNKFACHVFESEDGAQ--DIAQSIGQ 128
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
375-449 2.44e-03

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 39.65  E-value: 2.44e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958682065  375 INLISPDTKSVVLEKNFKDISSCSQG-IKHVDHFGFICReslEPGLSQYICYVFQCanESLVDEVMLTLKQAFSTA 449
Cdd:pfam00640   63 LKLLNPDTQELIHDHPLVSISFCADGdPDLMRYFAYIAR---DKATNKFACHVFES--EDGAQDIAQSIGQAFALA 133
 
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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