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Conserved domains on  [gi|568987148|ref|XP_006518824|]
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TBC1 domain family member 4 isoform X3 [Mus musculus]

Protein Classification

PTB_TBC1D1_like and TBC domain-containing protein( domain architecture ID 10648786)

protein containing domains PTB, PTB_TBC1D1_like, DUF3350, and TBC

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 ...
 193-444 5.66e-73

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: 239.12  E-value: 5.66e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  193 EDAFYNSQKFEVLYCGRVIVTHKKAPSSLIDDCKDKFSLHEQQRLKlqgerggdpgdemgvlevespvspddslpekadg 272
Cdd:cd01269     1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEKSR---------------------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  273 tvnspralpslaslpalasqpalassrvcfperiledcgfdeqqefrsrcssvtgvmqkkvhennqktqprrrhaSAPSH 352
Cdd:cd01269    47 ---------------------------------------------------------------------------SGPSS 51

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  353 VQPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESPEPGLSQYICYVFQCANESL 432
Cdd:cd01269    52 VQPTDSEENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDHFGFICRESSEGGGFHFVCYVFKCQSESV 131

                         250
                  ....*....|..
gi 568987148  433 VDEVMLTLKQAF 444
Cdd:cd01269   132 VDEIMLTIKQAF 143
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 919-1133 3.83e-72

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: 239.90  E-value: 3.83e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148    919 GVPKSRRGEIWQFLALQYrlrhrlPNKHQPPDTSYKELLKQ----LTAQQHAILVDLGRTFPTHPYFSVQLGAGQLSLFN 994
Cdd:smart00164    4 GVPPSLRGVVWKLLLNAQ------PMDTSADKDLYSRLLKEtapdDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQESLRR 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148    995 LLKAYSLLDKEVGYCQGISFVAGVLLLHM-SEEQAFEMLKFLMYDLGfRKQYRPDMMSLQIQMYQLSRLLHDYHRELYNH 1073
Cdd:smart00164   78 VLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYG-PNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKH 156

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148   1074 LEENEISPSLYAAPWFLTLFASQFPLGFVARVFDIIFLQGTEVIFKVALSLLSSQEALIM 1133
Cdd:smart00164  157 LKDLGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 31-190 4.01e-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: 84.67  E-value: 4.01e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148     31 PGDKRFRLWYVGGSCLDRRTTLPMLPWLMAEIRRrsqkpdAGGCGAPAAREVILVLSAPFLRCVpapgagvgggagsgav 110
Cdd:smart00462    1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRA------AQGSEKKEPQKVILSISSRGVKLI---------------- 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148    111 QPNTGVFIFEHKAQHISRFIHNSHDLTYFAYLIKaqpDDPESQMACHVFRATDPNqvPDVISSIRQLSKAAMKEDSKPSK 190
Cdd:smart00462   59 DEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIAR---DPGSSRFACHVFRCEKAA--EDIALAIGQAFQLAYELKLKARS 133
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 801-864 9.64e-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: 81.44  E-value: 9.64e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568987148   801 ELLPLSPLSPTMEEEPlIIFLSGDEDTEKVEEKKKSKELKSLWKKAIHQQILLLRMEKENQKLE 864
Cdd:pfam11830    1 ELLPLSPLAPGGEEDP-AGLLSSEDSPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63
PTZ00440 super family cl36566
reticulocyte binding protein 2-like protein; Provisional
 1133-1264 6.41e-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: 44.44  E-value: 6.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148 1133 MECENFENIVEFLKSTLPDMNTTE--MEKIITQVFEMDISKQLHAYEVEYHVLQDELleSSYAcEDNESLEKLEraNNQL 1210
Cdd:PTZ00440  681 MKSDNIDNIIKNLKKELQNLLSLKenIIKKQLNNIEQDISNSLNQYTIKYNDLKSSI--EEYK-EEEEKLEVYK--HQII 755

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148 1211 KRQNMDLL------EKLQVAHAKIQALESNLETLLTRETKMKALIRTLEQDKMAYQKTVE 1264
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 ...
 193-444 5.66e-73

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: 239.12  E-value: 5.66e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  193 EDAFYNSQKFEVLYCGRVIVTHKKAPSSLIDDCKDKFSLHEQQRLKlqgerggdpgdemgvlevespvspddslpekadg 272
Cdd:cd01269     1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEKSR---------------------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  273 tvnspralpslaslpalasqpalassrvcfperiledcgfdeqqefrsrcssvtgvmqkkvhennqktqprrrhaSAPSH 352
Cdd:cd01269    47 ---------------------------------------------------------------------------SGPSS 51

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  353 VQPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESPEPGLSQYICYVFQCANESL 432
Cdd:cd01269    52 VQPTDSEENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDHFGFICRESSEGGGFHFVCYVFKCQSESV 131

                         250
                  ....*....|..
gi 568987148  433 VDEVMLTLKQAF 444
Cdd:cd01269   132 VDEIMLTIKQAF 143
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 919-1133 3.83e-72

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: 239.90  E-value: 3.83e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148    919 GVPKSRRGEIWQFLALQYrlrhrlPNKHQPPDTSYKELLKQ----LTAQQHAILVDLGRTFPTHPYFSVQLGAGQLSLFN 994
Cdd:smart00164    4 GVPPSLRGVVWKLLLNAQ------PMDTSADKDLYSRLLKEtapdDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQESLRR 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148    995 LLKAYSLLDKEVGYCQGISFVAGVLLLHM-SEEQAFEMLKFLMYDLGfRKQYRPDMMSLQIQMYQLSRLLHDYHRELYNH 1073
Cdd:smart00164   78 VLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYG-PNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKH 156

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148   1074 LEENEISPSLYAAPWFLTLFASQFPLGFVARVFDIIFLQGTEVIFKVALSLLSSQEALIM 1133
Cdd:smart00164  157 LKDLGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 964-1133 1.20e-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: 194.01  E-value: 1.20e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148   964 QHAILVDLGRTFPTHPYFsvQLGAGQLSLFNLLKAYSLLDKEVGYCQGISFVAGVLLL-HMSEEQAFEMLKFLMYDLGFR 1042
Cdd:pfam00566    9 PEQIEKDVPRTFPHSFFF--DNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLR 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  1043 KQYRPDMMSLQIQMYQLSRLLHDYHRELYNHLEENEISPSLYAAPWFLTLFASQFPLGFVARVFDIIFLQGTEV-IFKVA 1121
Cdd:pfam00566   87 DFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVA 166

                          170
                   ....*....|..
gi 568987148  1122 LSLLSSQEALIM 1133
Cdd:pfam00566  167 LAILKRFREELL 178
COG5210 COG5210
GTPase-activating protein [General function prediction only];
849-1174 1.68e-47

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 178.07  E-value: 1.68e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  849 QQILLLRMEKENQKLEEARRDELQSRKVKldyeevgtcQKEILIAWDKKLL-NCRTKIRCDMEDIHTSLKEGVPKSRRGE 927
Cdd:COG5210   150 SSSLNSNPELNKEINELSLKEEPQKLRYY---------ELAADKLWISYLDpNPLSFLPVQLSKLRELIRKGIPNELRGD 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  928 IWQFLALQYRLRHRLPNKHqPPDTSYKELLKQLTAQQ-HAILVDLGRTFPTHPYFSVQLGAGQLSLFNLLKAYSLLDKEV 1006
Cdd:COG5210   221 VWEFLLGIGFDLDKNPGLY-ERLLNLHREAKIPTQEIiSQIEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSLYNPEV 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148 1007 GYCQGISFVAGVLLLHM-SEEQAFEMLKFLMYDLGFRKQYRPDMMSLQIQMYQLSRLLHDYHRELYNHLEENEISPSLYA 1085
Cdd:COG5210   300 GYVQGMNFLAAPLLLVLeSEEQAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVVLLMFA 379

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148 1086 APWFLTLFASQFPLGFVARVFDIIFLQGTEVIFKVALSLLSSQEALIMECeNFENIVEFLKSTLPDMNTTEMEKIITQVF 1165
Cdd:COG5210   380 FRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL-DSDELLDLLLKQLFLHSGKEAWSSILKFR 458


                  ....*....
gi 568987148 1166 EMDISKQLH 1174
Cdd:COG5210   459 HGTDRDILL 467
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 354-457 5.33e-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: 95.84  E-value: 5.33e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148    354 QPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRespEPGLSQYICYVFQCANESlv 433
Cdd:smart00462   36 QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIAR---DPGSSRFACHVFRCEKAA-- 110

                            90       100
                    ....*....|....*....|....
gi 568987148    434 DEVMLTLKQAFSTAAALQSAKTQI 457
Cdd:smart00462  111 EDIALAIGQAFQLAYELKLKARSE 134
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 31-190 4.01e-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: 84.67  E-value: 4.01e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148     31 PGDKRFRLWYVGGSCLDRRTTLPMLPWLMAEIRRrsqkpdAGGCGAPAAREVILVLSAPFLRCVpapgagvgggagsgav 110
Cdd:smart00462    1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRA------AQGSEKKEPQKVILSISSRGVKLI---------------- 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148    111 QPNTGVFIFEHKAQHISRFIHNSHDLTYFAYLIKaqpDDPESQMACHVFRATDPNqvPDVISSIRQLSKAAMKEDSKPSK 190
Cdd:smart00462   59 DEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIAR---DPGSSRFACHVFRCEKAA--EDIALAIGQAFQLAYELKLKARS 133
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 801-864 9.64e-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: 81.44  E-value: 9.64e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568987148   801 ELLPLSPLSPTMEEEPlIIFLSGDEDTEKVEEKKKSKELKSLWKKAIHQQILLLRMEKENQKLE 864
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 9.35e-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: 9.35e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568987148  112 PNTGVFIFEHKAQHISRFIHNSHDLTYFAYLIKaqpDDPESQMACHVFRATDPNQVPDVISSIRQ 176
Cdd:cd00934    57 LDTKELLLRHPLHRISYCGRDPDNPNVFAFIAG---EEGGSGFRCHVFQCEDEEEAEEILQAIGQ 118
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 1133-1264 6.41e-04

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 44.44  E-value: 6.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148 1133 MECENFENIVEFLKSTLPDMNTTE--MEKIITQVFEMDISKQLHAYEVEYHVLQDELleSSYAcEDNESLEKLEraNNQL 1210
Cdd:PTZ00440  681 MKSDNIDNIIKNLKKELQNLLSLKenIIKKQLNNIEQDISNSLNQYTIKYNDLKSSI--EEYK-EEEEKLEVYK--HQII 755

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148 1211 KRQNMDLL------EKLQVAHAKIQALESNLETLLTRETKMKALIRTLEQDKMAYQKTVE 1264
Cdd:PTZ00440  756 NRKNEFILhlyendKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLN 815
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
112-176 1.25e-03

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 40.42  E-value: 1.25e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568987148   112 PNTGVFIFEHKAQHISrFIHNSH--DLTYFAYLIKaqpDDPESQMACHVFRATDPNQvpDVISSIRQ 176
Cdd:pfam00640   68 PDTQELIHDHPLVSIS-FCADGDpdLMRYFAYIAR---DKATNKFACHVFESEDGAQ--DIAQSIGQ 128
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
373-447 1.56e-03

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 40.04  E-value: 1.56e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568987148   373 INLISPDTKSVVLEKNFKDISSCSQG-IKHVDHFGFICRESPepgLSQYICYVFQCanESLVDEVMLTLKQAFSTA 447
Cdd:pfam00640   63 LKLLNPDTQELIHDHPLVSISFCADGdPDLMRYFAYIARDKA---TNKFACHVFES--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 ...
 193-444 5.66e-73

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: 239.12  E-value: 5.66e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  193 EDAFYNSQKFEVLYCGRVIVTHKKAPSSLIDDCKDKFSLHEQQRLKlqgerggdpgdemgvlevespvspddslpekadg 272
Cdd:cd01269     1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEKSR---------------------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  273 tvnspralpslaslpalasqpalassrvcfperiledcgfdeqqefrsrcssvtgvmqkkvhennqktqprrrhaSAPSH 352
Cdd:cd01269    47 ---------------------------------------------------------------------------SGPSS 51

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  353 VQPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESPEPGLSQYICYVFQCANESL 432
Cdd:cd01269    52 VQPTDSEENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDHFGFICRESSEGGGFHFVCYVFKCQSESV 131

                         250
                  ....*....|..
gi 568987148  433 VDEVMLTLKQAF 444
Cdd:cd01269   132 VDEIMLTIKQAF 143
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 919-1133 3.83e-72

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: 239.90  E-value: 3.83e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148    919 GVPKSRRGEIWQFLALQYrlrhrlPNKHQPPDTSYKELLKQ----LTAQQHAILVDLGRTFPTHPYFSVQLGAGQLSLFN 994
Cdd:smart00164    4 GVPPSLRGVVWKLLLNAQ------PMDTSADKDLYSRLLKEtapdDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQESLRR 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148    995 LLKAYSLLDKEVGYCQGISFVAGVLLLHM-SEEQAFEMLKFLMYDLGfRKQYRPDMMSLQIQMYQLSRLLHDYHRELYNH 1073
Cdd:smart00164   78 VLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYG-PNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKH 156

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148   1074 LEENEISPSLYAAPWFLTLFASQFPLGFVARVFDIIFLQGTEVIFKVALSLLSSQEALIM 1133
Cdd:smart00164  157 LKDLGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 964-1133 1.20e-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: 194.01  E-value: 1.20e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148   964 QHAILVDLGRTFPTHPYFsvQLGAGQLSLFNLLKAYSLLDKEVGYCQGISFVAGVLLL-HMSEEQAFEMLKFLMYDLGFR 1042
Cdd:pfam00566    9 PEQIEKDVPRTFPHSFFF--DNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLR 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  1043 KQYRPDMMSLQIQMYQLSRLLHDYHRELYNHLEENEISPSLYAAPWFLTLFASQFPLGFVARVFDIIFLQGTEV-IFKVA 1121
Cdd:pfam00566   87 DFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVA 166

                          170
                   ....*....|..
gi 568987148  1122 LSLLSSQEALIM 1133
Cdd:pfam00566  167 LAILKRFREELL 178
COG5210 COG5210
GTPase-activating protein [General function prediction only];
849-1174 1.68e-47

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 178.07  E-value: 1.68e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  849 QQILLLRMEKENQKLEEARRDELQSRKVKldyeevgtcQKEILIAWDKKLL-NCRTKIRCDMEDIHTSLKEGVPKSRRGE 927
Cdd:COG5210   150 SSSLNSNPELNKEINELSLKEEPQKLRYY---------ELAADKLWISYLDpNPLSFLPVQLSKLRELIRKGIPNELRGD 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  928 IWQFLALQYRLRHRLPNKHqPPDTSYKELLKQLTAQQ-HAILVDLGRTFPTHPYFSVQLGAGQLSLFNLLKAYSLLDKEV 1006
Cdd:COG5210   221 VWEFLLGIGFDLDKNPGLY-ERLLNLHREAKIPTQEIiSQIEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSLYNPEV 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148 1007 GYCQGISFVAGVLLLHM-SEEQAFEMLKFLMYDLGFRKQYRPDMMSLQIQMYQLSRLLHDYHRELYNHLEENEISPSLYA 1085
Cdd:COG5210   300 GYVQGMNFLAAPLLLVLeSEEQAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVVLLMFA 379

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148 1086 APWFLTLFASQFPLGFVARVFDIIFLQGTEVIFKVALSLLSSQEALIMECeNFENIVEFLKSTLPDMNTTEMEKIITQVF 1165
Cdd:COG5210   380 FRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL-DSDELLDLLLKQLFLHSGKEAWSSILKFR 458


                  ....*....
gi 568987148 1166 EMDISKQLH 1174
Cdd:COG5210   459 HGTDRDILL 467
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 354-457 5.33e-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: 95.84  E-value: 5.33e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148    354 QPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRespEPGLSQYICYVFQCANESlv 433
Cdd:smart00462   36 QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIAR---DPGSSRFACHVFRCEKAA-- 110

                            90       100
                    ....*....|....*....|....
gi 568987148    434 DEVMLTLKQAFSTAAALQSAKTQI 457
Cdd:smart00462  111 EDIALAIGQAFQLAYELKLKARSE 134
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 31-190 4.01e-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: 84.67  E-value: 4.01e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148     31 PGDKRFRLWYVGGSCLDRRTTLPMLPWLMAEIRRrsqkpdAGGCGAPAAREVILVLSAPFLRCVpapgagvgggagsgav 110
Cdd:smart00462    1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRA------AQGSEKKEPQKVILSISSRGVKLI---------------- 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148    111 QPNTGVFIFEHKAQHISRFIHNSHDLTYFAYLIKaqpDDPESQMACHVFRATDPNqvPDVISSIRQLSKAAMKEDSKPSK 190
Cdd:smart00462   59 DEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIAR---DPGSSRFACHVFRCEKAA--EDIALAIGQAFQLAYELKLKARS 133
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 801-864 9.64e-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: 81.44  E-value: 9.64e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568987148   801 ELLPLSPLSPTMEEEPlIIFLSGDEDTEKVEEKKKSKELKSLWKKAIHQQILLLRMEKENQKLE 864
Cdd:pfam11830    1 ELLPLSPLAPGGEEDP-AGLLSSEDSPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 347-444 6.46e-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: 81.02  E-value: 6.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  347 ASAPSHVQPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRespEPGLSQYICYVFQ 426
Cdd:cd00934    26 LKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDNPNVFAFIAG---EEGGSGFRCHVFQ 102

                          90
                  ....*....|....*...
gi 568987148  427 CANESLVDEVMLTLKQAF 444
Cdd:cd00934   103 CEDEEEAEEILQAIGQAF 120
PTB_LOC417372 cd13168
uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of ...
 360-444 4.74e-08

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: 52.71  E-value: 4.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  360 KNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESPEPGLSQYICYVFQCANESLVDEVMLT 439
Cdd:cd13168    36 TPKEVLLELGEIGVTVWDKSTSEVLFKHSFPEISSCGRRVDDPNYFAYIAGDTPCSLAKHFVCYVFEAADEEEAETILQG 115


                  ....*
gi 568987148  440 LKQAF 444
Cdd:cd13168   116 IAQGF 120
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 373-455 1.91e-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: 48.82  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148  373 INLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESPEpglSQYICYVFQCANESLVDEVMLTLKQAFSTA--AAL 450
Cdd:cd01274    65 VKFIDATTKNLICEHEIRNISCACQDPEDLNTFAYITKDLKT---DHHYCHVFCVLTVDLATEIILTLGQAFEVAyqLAL 141


                  ....*
gi 568987148  451 QSAKT 455
Cdd:cd01274   142 RAQKS 146
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 372-445 3.50e-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: 44.63  E-value: 3.50e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568987148  372 EINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESPEPGLSqyiCYVFQCANESLVDEVMLTLKQAFS 445
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 9.35e-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: 9.35e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568987148  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 ...
 373-449 3.97e-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: 3.97e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568987148  373 INLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRespEPGLSQYICYVFQCANESlvDEVMLTLKQAFSTAAA 449
Cdd:cd13161    49 IRVVERLTGEVLTNVPIKDISFVTVDPKDKKLFAFISH---DPRLGRITCHVFRCKRGA--QEICDTIAEAFKAAAE 120
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 112-176 4.81e-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: 4.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568987148  112 PNTGVFIFEHKAQHISRFIHNSHDLTYFAYLIKaqpDDPESQMACHVFRATDPNQVPDVISSIRQ 176
Cdd:cd01274    70 ATTKNLICEHEIRNISCACQDPEDLNTFAYITK---DLKTDHHYCHVFCVLTVDLATEIILTLGQ 131
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 1133-1264 6.41e-04

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 44.44  E-value: 6.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148 1133 MECENFENIVEFLKSTLPDMNTTE--MEKIITQVFEMDISKQLHAYEVEYHVLQDELleSSYAcEDNESLEKLEraNNQL 1210
Cdd:PTZ00440  681 MKSDNIDNIIKNLKKELQNLLSLKenIIKKQLNNIEQDISNSLNQYTIKYNDLKSSI--EEYK-EEEEKLEVYK--HQII 755

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987148 1211 KRQNMDLL------EKLQVAHAKIQALESNLETLLTRETKMKALIRTLEQDKMAYQKTVE 1264
Cdd:PTZ00440  756 NRKNEFILhlyendKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLN 815
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
112-176 1.25e-03

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 40.42  E-value: 1.25e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568987148   112 PNTGVFIFEHKAQHISrFIHNSH--DLTYFAYLIKaqpDDPESQMACHVFRATDPNQvpDVISSIRQ 176
Cdd:pfam00640   68 PDTQELIHDHPLVSIS-FCADGDpdLMRYFAYIAR---DKATNKFACHVFESEDGAQ--DIAQSIGQ 128
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
373-447 1.56e-03

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 40.04  E-value: 1.56e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568987148   373 INLISPDTKSVVLEKNFKDISSCSQG-IKHVDHFGFICRESPepgLSQYICYVFQCanESLVDEVMLTLKQAFSTA 447
Cdd:pfam00640   63 LKLLNPDTQELIHDHPLVSISFCADGdPDLMRYFAYIARDKA---TNKFACHVFES--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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