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Conserved domains on  [gi|2462538516|ref|XP_054231207|]
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TBC1 domain family member 4 isoform X5 [Homo sapiens]

Protein Classification

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 ...
 193-437 2.89e-75

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: 245.28  E-value: 2.89e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  193 EDAFYNSQKFEVLYCGKVTVTHKKAPSSLIDDCMEKFSLHEQQRLKiqgeqrgpdpgedladlevvvpgspgdclpeead 272
Cdd:cd01269      1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEKSR---------------------------------- 46

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  273 gtdthlglpagasqpaltssrvcfperiledsgfdeqqefrsrcssvtgvqrrvhegsqksqprrrhaSAPSHVQPSDSE 352
Cdd:cd01269     47 --------------------------------------------------------------------SGPSSVQPTDSE 58

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  353 KNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESPEPGLSQYICYVFQCASESLVDEVMLT 432
Cdd:cd01269     59 ENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDHFGFICRESSEGGGFHFVCYVFKCQSESVVDEIMLT 138


                   ....*
gi 2462538516  433 LKQAF 437
Cdd:cd01269    139 IKQAF 143
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 818-1032 3.92e-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: 239.13  E-value: 3.92e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516   818 GVPKSRRGEIWQFLALQYRlRHRLPNKQQppdisYKELLKQ----LTAQQHAILVDLGRTFPTHPYFSVQLGPGQLSLFN 893
Cdd:smart00164    4 GVPPSLRGVVWKLLLNAQP-MDTSADKDL-----YSRLLKEtapdDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQESLRR 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516   894 LLKAYSLLDKEVGYCQGISFVAGVLLLHM-SEEQAFEMLKFLMYDLGfRKQYRPDMMSLQIQMYQLSRLLHDYHRDLYNH 972
Cdd:smart00164   78 VLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYG-PNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKH 156

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516   973 LEENEISPSLYAAPWFLTLFASQFSLGFVARVFDIIFLQGTEVIFKVALSLLSSQETLIM 1032
Cdd:smart00164  157 LKDLGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 701-764 4.29e-28

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: 107.63  E-value: 4.29e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462538516  701 ELLPLSPLSPTMEEEPlVVFLSGEDDPEKIEERKKSKELRSLWRKAIHQQILLLRMEKENQKLE 764
Cdd:pfam11830    1 ELLPLSPLAPGGEEDP-AGLLSSEDSPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 31-190 7.48e-21

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


:

Pssm-ID: 214675  Cd Length: 134  Bit Score: 89.68  E-value: 7.48e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516    31 PSDKRFRLWYVGGSCLDHRTTLPMLPWLMAEIRrrsqkpEAGGCGAPAAREVILVLSAPFLRCVPAPGAGVsggtspsat 110
Cdd:smart00462    1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLR------AAQGSEKKEPQKVILSISSRGVKLIDEDTKAV--------- 65

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516   111 qpnpavfIFEHKAQHISRFIHNSHDLTYFAYLIKaqpDDPESQMACHVFRATDPSqvPDVISSIRQLSKAAMKEDAKPSK 190
Cdd:smart00462   66 -------LHEHPLRRISFCAVGPDDLDVFGYIAR---DPGSSRFACHVFRCEKAA--EDIALAIGQAFQLAYELKLKARS 133
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1061-1167 1.16e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516 1061 TQVFEMDISKQLHAYEVEYHVLQDELQEssYSCEDSETLEKLERANSQLKRQNmdllEKLQVAHTKIQALESNLENLLTR 1140
Cdd:COG4372     22 TGILIAALSEQLRKALFELDKLQEELEQ--LREELEQAREELEQLEEELEQAR----SELEQLEEELEELNEQLQAAQAE 95

                           90       100
                   ....*....|....*....|....*..
gi 2462538516 1141 ETKMKSLIRTLEQEKMAYQKTVEQLRK 1167
Cdd:COG4372     96 LAQAQEELESLQEEAEELQEELEELQK 122
 
Name Accession Description Interval E-value
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
 193-437 2.89e-75

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: 245.28  E-value: 2.89e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  193 EDAFYNSQKFEVLYCGKVTVTHKKAPSSLIDDCMEKFSLHEQQRLKiqgeqrgpdpgedladlevvvpgspgdclpeead 272
Cdd:cd01269      1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEKSR---------------------------------- 46

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  273 gtdthlglpagasqpaltssrvcfperiledsgfdeqqefrsrcssvtgvqrrvhegsqksqprrrhaSAPSHVQPSDSE 352
Cdd:cd01269     47 --------------------------------------------------------------------SGPSSVQPTDSE 58

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  353 KNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESPEPGLSQYICYVFQCASESLVDEVMLT 432
Cdd:cd01269     59 ENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDHFGFICRESSEGGGFHFVCYVFKCQSESVVDEIMLT 138


                   ....*
gi 2462538516  433 LKQAF 437
Cdd:cd01269    139 IKQAF 143
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 818-1032 3.92e-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: 239.13  E-value: 3.92e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516   818 GVPKSRRGEIWQFLALQYRlRHRLPNKQQppdisYKELLKQ----LTAQQHAILVDLGRTFPTHPYFSVQLGPGQLSLFN 893
Cdd:smart00164    4 GVPPSLRGVVWKLLLNAQP-MDTSADKDL-----YSRLLKEtapdDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQESLRR 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516   894 LLKAYSLLDKEVGYCQGISFVAGVLLLHM-SEEQAFEMLKFLMYDLGfRKQYRPDMMSLQIQMYQLSRLLHDYHRDLYNH 972
Cdd:smart00164   78 VLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYG-PNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKH 156

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516   973 LEENEISPSLYAAPWFLTLFASQFSLGFVARVFDIIFLQGTEVIFKVALSLLSSQETLIM 1032
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 ...
 863-1032 1.77e-56

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


Pssm-ID: 459855  Cd Length: 178  Bit Score: 193.24  E-value: 1.77e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  863 QHAILVDLGRTFPTHPYFsvQLGPGQLSLFNLLKAYSLLDKEVGYCQGISFVAGVLLL-HMSEEQAFEMLKFLMYDLGFR 941
Cdd:pfam00566    9 PEQIEKDVPRTFPHSFFF--DNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLR 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  942 KQYRPDMMSLQIQMYQLSRLLHDYHRDLYNHLEENEISPSLYAAPWFLTLFASQFSLGFVARVFDIIFLQGTEV-IFKVA 1020
Cdd:pfam00566   87 DFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVA 166

                          170
                   ....*....|..
gi 2462538516 1021 LSLLSSQETLIM 1032
Cdd:pfam00566  167 LAILKRFREELL 178
COG5210 COG5210
GTPase-activating protein [General function prediction only];
749-1068 7.38e-49

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 181.92  E-value: 7.38e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  749 QQILLLRMEKENQKLEASRDELQSRKVKLDYEEVGACQKEVLITWDKKLLNCRAKIRcdmedihTLLKEGVPKSRRGEIW 828
Cdd:COG5210    150 SSSLNSNPELNKEINELSLKEEPQKLRYYELAADKLWISYLDPNPLSFLPVQLSKLR-------ELIRKGIPNELRGDVW 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  829 QFLALQYRLRHRLPNKQqPPDISYKELLKQLTAQQ-HAILVDLGRTFPTHPYFSVQLGPGQLSLFNLLKAYSLLDKEVGY 907
Cdd:COG5210    223 EFLLGIGFDLDKNPGLY-ERLLNLHREAKIPTQEIiSQIEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSLYNPEVGY 301

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  908 CQGISFVAGVLLLHM-SEEQAFEMLKFLMYDLGFRKQYRPDMMSLQIQMYQLSRLLHDYHRDLYNHLEENEISPSLYAAP 986
Cdd:COG5210    302 VQGMNFLAAPLLLVLeSEEQAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVVLLMFAFR 381

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  987 WFLTLFASQFSLGFVARVFDIIFLQGTEVIFKVALSLLSSQETLIMECESFENIVEFLK--NTLPDMNTSEMEKIITQVF 1064
Cdd:COG5210    382 WFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLDLLLKqlFLHSGKEAWSSILKFRHGT 461


                   ....
gi 2462538516 1065 EMDI 1068
Cdd:COG5210    462 DRDI 465
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 701-764 4.29e-28

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: 107.63  E-value: 4.29e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462538516  701 ELLPLSPLSPTMEEEPlVVFLSGEDDPEKIEERKKSKELRSLWRKAIHQQILLLRMEKENQKLE 764
Cdd:pfam11830    1 ELLPLSPLAPGGEEDP-AGLLSSEDSPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 347-450 3.62e-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: 96.23  E-value: 3.62e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516   347 QPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRespEPGLSQYICYVFQCASESlv 426
Cdd:smart00462   36 QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIAR---DPGSSRFACHVFRCEKAA-- 110

                            90       100
                    ....*....|....*....|....
gi 2462538516   427 DEVMLTLKQAFSTAAALQSAKTQI 450
Cdd:smart00462  111 EDIALAIGQAFQLAYELKLKARSE 134
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 31-190 7.48e-21

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 89.68  E-value: 7.48e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516    31 PSDKRFRLWYVGGSCLDHRTTLPMLPWLMAEIRrrsqkpEAGGCGAPAAREVILVLSAPFLRCVPAPGAGVsggtspsat 110
Cdd:smart00462    1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLR------AAQGSEKKEPQKVILSISSRGVKLIDEDTKAV--------- 65

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516   111 qpnpavfIFEHKAQHISRFIHNSHDLTYFAYLIKaqpDDPESQMACHVFRATDPSqvPDVISSIRQLSKAAMKEDAKPSK 190
Cdd:smart00462   66 -------LHEHPLRRISFCAVGPDDLDVFGYIAR---DPGSSRFACHVFRCEKAA--EDIALAIGQAFQLAYELKLKARS 133
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
118-176 4.39e-04

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 41.58  E-value: 4.39e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462538516  118 IFEHKAQHISrFIHNSH--DLTYFAYLIKaqpDDPESQMACHVFRATDPSQvpDVISSIRQ 176
Cdd:pfam00640   74 IHDHPLVSIS-FCADGDpdLMRYFAYIAR---DKATNKFACHVFESEDGAQ--DIAQSIGQ 128
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 110-176 6.22e-04

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: 40.96  E-value: 6.22e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462538516  110 TQPNPAVFIFEHKAQHISRFIHNSHDLTYFAYLIKaqpDDPESQMACHVFRATDPSQVPDVISSIRQ 176
Cdd:cd00934     55 LDLDTKELLLRHPLHRISYCGRDPDNPNVFAFIAG---EEGGSGFRCHVFQCEDEEEAEEILQAIGQ 118
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1061-1167 1.16e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516 1061 TQVFEMDISKQLHAYEVEYHVLQDELQEssYSCEDSETLEKLERANSQLKRQNmdllEKLQVAHTKIQALESNLENLLTR 1140
Cdd:COG4372     22 TGILIAALSEQLRKALFELDKLQEELEQ--LREELEQAREELEQLEEELEQAR----SELEQLEEELEELNEQLQAAQAE 95

                           90       100
                   ....*....|....*....|....*..
gi 2462538516 1141 ETKMKSLIRTLEQEKMAYQKTVEQLRK 1167
Cdd:COG4372     96 LAQAQEELESLQEEAEELQEELEELQK 122
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
324-440 1.35e-03

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 40.04  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  324 RRVHEgsqksQPRRRHASAPSHVQPSDSeknrtMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQG-IKHVDHFGFIC 402
Cdd:pfam00640   31 RRVKA-----AKINKIRGLSGETGPGTK-----VDLFISTDGLKLLNPDTQELIHDHPLVSISFCADGdPDLMRYFAYIA 100

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462538516  403 RESPepgLSQYICYVFQCasESLVDEVMLTLKQAFSTA 440
Cdd:pfam00640  101 RDKA---TNKFACHVFES--EDGAQDIAQSIGQAFALA 133
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 1032-1163 5.82e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 40.97  E-value: 5.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516 1032 MECESFENIVEFLKNTLPDMNT--SEMEKIITQVFEMDISKQLHAYEVEYHVLQDELQESSyscEDSETLEKLEraNSQL 1109
Cdd:PTZ00440   681 MKSDNIDNIIKNLKKELQNLLSlkENIIKKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYK---EEEEKLEVYK--HQII 755

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516 1110 KRQNMDLL------EKLQVAHTKIQALESNLENLLTRETKMKSLIRTLEQEKMAYQKTVE 1163
Cdd:PTZ00440   756 NRKNEFILhlyendKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLN 815
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1022-1166 7.24e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.39  E-value: 7.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516 1022 SLLSSQETLIMECESFENIVEFLKNTLPDMNT--SEMEKIITQV--FEMDISKQLHAYEVEYHVLQDELQESSYSCEDSE 1097
Cdd:TIGR04523  416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdSVKELIIKNLdnTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE 495

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516 1098 T-LEKLERANSQLKRQNMDLLEKLQVAHTKIQALESnleNLLTRETKMKSLIR------------TLEQEKMAYQKTVEQ 1164
Cdd:TIGR04523  496 KeLKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES---EKKEKESKISDLEDelnkddfelkkeNLEKEIDEKNKEIEE 572


                   ..
gi 2462538516 1165 LR 1166
Cdd:TIGR04523  573 LK 574
 
Name Accession Description Interval E-value
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
 193-437 2.89e-75

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: 245.28  E-value: 2.89e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  193 EDAFYNSQKFEVLYCGKVTVTHKKAPSSLIDDCMEKFSLHEQQRLKiqgeqrgpdpgedladlevvvpgspgdclpeead 272
Cdd:cd01269      1 DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEKSR---------------------------------- 46

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  273 gtdthlglpagasqpaltssrvcfperiledsgfdeqqefrsrcssvtgvqrrvhegsqksqprrrhaSAPSHVQPSDSE 352
Cdd:cd01269     47 --------------------------------------------------------------------SGPSSVQPTDSE 58

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  353 KNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESPEPGLSQYICYVFQCASESLVDEVMLT 432
Cdd:cd01269     59 ENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDHFGFICRESSEGGGFHFVCYVFKCQSESVVDEIMLT 138


                   ....*
gi 2462538516  433 LKQAF 437
Cdd:cd01269    139 IKQAF 143
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 818-1032 3.92e-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: 239.13  E-value: 3.92e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516   818 GVPKSRRGEIWQFLALQYRlRHRLPNKQQppdisYKELLKQ----LTAQQHAILVDLGRTFPTHPYFSVQLGPGQLSLFN 893
Cdd:smart00164    4 GVPPSLRGVVWKLLLNAQP-MDTSADKDL-----YSRLLKEtapdDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQESLRR 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516   894 LLKAYSLLDKEVGYCQGISFVAGVLLLHM-SEEQAFEMLKFLMYDLGfRKQYRPDMMSLQIQMYQLSRLLHDYHRDLYNH 972
Cdd:smart00164   78 VLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYG-PNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKH 156

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516   973 LEENEISPSLYAAPWFLTLFASQFSLGFVARVFDIIFLQGTEVIFKVALSLLSSQETLIM 1032
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 ...
 863-1032 1.77e-56

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


Pssm-ID: 459855  Cd Length: 178  Bit Score: 193.24  E-value: 1.77e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  863 QHAILVDLGRTFPTHPYFsvQLGPGQLSLFNLLKAYSLLDKEVGYCQGISFVAGVLLL-HMSEEQAFEMLKFLMYDLGFR 941
Cdd:pfam00566    9 PEQIEKDVPRTFPHSFFF--DNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLR 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  942 KQYRPDMMSLQIQMYQLSRLLHDYHRDLYNHLEENEISPSLYAAPWFLTLFASQFSLGFVARVFDIIFLQGTEV-IFKVA 1020
Cdd:pfam00566   87 DFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVA 166

                          170
                   ....*....|..
gi 2462538516 1021 LSLLSSQETLIM 1032
Cdd:pfam00566  167 LAILKRFREELL 178
COG5210 COG5210
GTPase-activating protein [General function prediction only];
749-1068 7.38e-49

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 181.92  E-value: 7.38e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  749 QQILLLRMEKENQKLEASRDELQSRKVKLDYEEVGACQKEVLITWDKKLLNCRAKIRcdmedihTLLKEGVPKSRRGEIW 828
Cdd:COG5210    150 SSSLNSNPELNKEINELSLKEEPQKLRYYELAADKLWISYLDPNPLSFLPVQLSKLR-------ELIRKGIPNELRGDVW 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  829 QFLALQYRLRHRLPNKQqPPDISYKELLKQLTAQQ-HAILVDLGRTFPTHPYFSVQLGPGQLSLFNLLKAYSLLDKEVGY 907
Cdd:COG5210    223 EFLLGIGFDLDKNPGLY-ERLLNLHREAKIPTQEIiSQIEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSLYNPEVGY 301

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  908 CQGISFVAGVLLLHM-SEEQAFEMLKFLMYDLGFRKQYRPDMMSLQIQMYQLSRLLHDYHRDLYNHLEENEISPSLYAAP 986
Cdd:COG5210    302 VQGMNFLAAPLLLVLeSEEQAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVVLLMFAFR 381

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  987 WFLTLFASQFSLGFVARVFDIIFLQGTEVIFKVALSLLSSQETLIMECESFENIVEFLK--NTLPDMNTSEMEKIITQVF 1064
Cdd:COG5210    382 WFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLDLLLKqlFLHSGKEAWSSILKFRHGT 461


                   ....
gi 2462538516 1065 EMDI 1068
Cdd:COG5210    462 DRDI 465
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 701-764 4.29e-28

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: 107.63  E-value: 4.29e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462538516  701 ELLPLSPLSPTMEEEPlVVFLSGEDDPEKIEERKKSKELRSLWRKAIHQQILLLRMEKENQKLE 764
Cdd:pfam11830    1 ELLPLSPLAPGGEEDP-AGLLSSEDSPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 347-450 3.62e-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: 96.23  E-value: 3.62e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516   347 QPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRespEPGLSQYICYVFQCASESlv 426
Cdd:smart00462   36 QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIAR---DPGSSRFACHVFRCEKAA-- 110

                            90       100
                    ....*....|....*....|....
gi 2462538516   427 DEVMLTLKQAFSTAAALQSAKTQI 450
Cdd:smart00462  111 EDIALAIGQAFQLAYELKLKARSE 134
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 31-190 7.48e-21

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 89.68  E-value: 7.48e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516    31 PSDKRFRLWYVGGSCLDHRTTLPMLPWLMAEIRrrsqkpEAGGCGAPAAREVILVLSAPFLRCVPAPGAGVsggtspsat 110
Cdd:smart00462    1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLR------AAQGSEKKEPQKVILSISSRGVKLIDEDTKAV--------- 65

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516   111 qpnpavfIFEHKAQHISRFIHNSHDLTYFAYLIKaqpDDPESQMACHVFRATDPSqvPDVISSIRQLSKAAMKEDAKPSK 190
Cdd:smart00462   66 -------LHEHPLRRISFCAVGPDDLDVFGYIAR---DPGSSRFACHVFRCEKAA--EDIALAIGQAFQLAYELKLKARS 133
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 318-437 1.16e-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: 82.94  E-value: 1.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  318 SVTGVQRRVHEGSQKSQPRRRHASAPSHvqpsdsEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDH 397
Cdd:cd00934     10 SVEVGSSRGVDVVEEALKALAAALKSSK------RKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDNPNV 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2462538516  398 FGFICRespEPGLSQYICYVFQCASESLVDEVMLTLKQAF 437
Cdd:cd00934     84 FAFIAG---EEGGSGFRCHVFQCEDEEEAEEILQAIGQAF 120
PTB_LOC417372 cd13168
uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of ...
 353-437 4.98e-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: 4.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  353 KNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESPEPGLSQYICYVFQCASESLVDEVMLT 432
Cdd:cd13168     36 TPKEVLLELGEIGVTVWDKSTSEVLFKHSFPEISSCGRRVDDPNYFAYIAGDTPCSLAKHFVCYVFEAADEEEAETILQG 115


                   ....*
gi 2462538516  433 LKQAF 437
Cdd:cd13168    116 IAQGF 120
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 366-448 3.71e-07

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: 50.74  E-value: 3.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  366 INLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESPEpglSQYICYVFQCASESLVDEVMLTLKQAFSTA--AAL 443
Cdd:cd01274     65 VKFIDATTKNLICEHEIRNISCACQDPEDLNTFAYITKDLKT---DHHYCHVFCVLTVDLATEIILTLGQAFEVAyqLAL 141


                   ....*
gi 2462538516  444 QSAKT 448
Cdd:cd01274    142 RAQKS 146
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 365-438 3.24e-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: 3.24e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462538516  365 EINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESPEPGLSqyiCYVFQCASESLVDEVMLTLKQAFS 438
Cdd:cd13159     53 GIKVTDSATNETILEVSIYRISYCTADANHDKVFAFIATNQDNEKLE---CHAFLCAKRKMAQAVTLTVAQAFN 123
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
118-176 4.39e-04

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 41.58  E-value: 4.39e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462538516  118 IFEHKAQHISrFIHNSH--DLTYFAYLIKaqpDDPESQMACHVFRATDPSQvpDVISSIRQ 176
Cdd:pfam00640   74 IHDHPLVSIS-FCADGDpdLMRYFAYIAR---DKATNKFACHVFESEDGAQ--DIAQSIGQ 128
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 110-176 6.22e-04

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: 40.96  E-value: 6.22e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462538516  110 TQPNPAVFIFEHKAQHISRFIHNSHDLTYFAYLIKaqpDDPESQMACHVFRATDPSQVPDVISSIRQ 176
Cdd:cd00934     55 LDLDTKELLLRHPLHRISYCGRDPDNPNVFAFIAG---EEGGSGFRCHVFQCEDEEEAEEILQAIGQ 118
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 366-442 6.26e-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: 40.69  E-value: 6.26e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462538516  366 INLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRespEPGLSQYICYVFQCASESlvDEVMLTLKQAFSTAAA 442
Cdd:cd13161     49 IRVVERLTGEVLTNVPIKDISFVTVDPKDKKLFAFISH---DPRLGRITCHVFRCKRGA--QEICDTIAEAFKAAAE 120
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1061-1167 1.16e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516 1061 TQVFEMDISKQLHAYEVEYHVLQDELQEssYSCEDSETLEKLERANSQLKRQNmdllEKLQVAHTKIQALESNLENLLTR 1140
Cdd:COG4372     22 TGILIAALSEQLRKALFELDKLQEELEQ--LREELEQAREELEQLEEELEQAR----SELEQLEEELEELNEQLQAAQAE 95

                           90       100
                   ....*....|....*....|....*..
gi 2462538516 1141 ETKMKSLIRTLEQEKMAYQKTVEQLRK 1167
Cdd:COG4372     96 LAQAQEELESLQEEAEELQEELEELQK 122
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
324-440 1.35e-03

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 40.04  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  324 RRVHEgsqksQPRRRHASAPSHVQPSDSeknrtMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQG-IKHVDHFGFIC 402
Cdd:pfam00640   31 RRVKA-----AKINKIRGLSGETGPGTK-----VDLFISTDGLKLLNPDTQELIHDHPLVSISFCADGdPDLMRYFAYIA 100

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462538516  403 RESPepgLSQYICYVFQCasESLVDEVMLTLKQAFSTA 440
Cdd:pfam00640  101 RDKA---TNKFACHVFES--EDGAQDIAQSIGQAFALA 133
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 345-440 2.44e-03

Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also known as GULP1: engulfment adaptor PTB domain containing 1) is an adaptor protein involved in the specific recognition and engulfment of apoptotic cells. CED6 has been shown to interact with the cytoplasmic tail of another protein involved in the engulfment of apoptotic cells, CED1. CED6 has a C-terminal PTB domain, which can bind to NPXY motifs. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269971  Cd Length: 144  Bit Score: 39.57  E-value: 2.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516  345 HVQPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCS--QGIKHVdhFGFICRESPEpglSQYICYVFQcaS 422
Cdd:cd01273     45 QLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHRISFCAddKTDKRI--FSFIAKDSES---EKHLCFVFD--S 117

                           90
                   ....*....|....*...
gi 2462538516  423 ESLVDEVMLTLKQAFSTA 440
Cdd:cd01273    118 EKLAEEITLTIGQAFDLA 135
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 118-176 4.01e-03

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: 39.19  E-value: 4.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462538516  118 IFEHKAQHISRFIHNSHDLTYFAYLIKaqpDDPESQMACHVFRATDPSQVPDVISSIRQ 176
Cdd:cd01274     76 ICEHEIRNISCACQDPEDLNTFAYITK---DLKTDHHYCHVFCVLTVDLATEIILTLGQ 131
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1054-1169 4.54e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 4.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516 1054 SEMEKIITQVfeMDISKQLHAYEVEYHVLQDELQESSYSCED-SETLEKLERANSQLKRQNMDLLEKLQVAHTKIQALES 1132
Cdd:COG4372     73 SELEQLEEEL--EELNEQLQAAQAELAQAQEELESLQEEAEElQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREE 150

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462538516 1133 NLENLLTRETKMKSLIRTLEQEKMAY--QKTVEQLRKLL 1169
Cdd:COG4372    151 ELKELEEQLESLQEELAALEQELQALseAEAEQALDELL 189
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 1032-1163 5.82e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 40.97  E-value: 5.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516 1032 MECESFENIVEFLKNTLPDMNT--SEMEKIITQVFEMDISKQLHAYEVEYHVLQDELQESSyscEDSETLEKLEraNSQL 1109
Cdd:PTZ00440   681 MKSDNIDNIIKNLKKELQNLLSlkENIIKKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYK---EEEEKLEVYK--HQII 755

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516 1110 KRQNMDLL------EKLQVAHTKIQALESNLENLLTRETKMKSLIRTLEQEKMAYQKTVE 1163
Cdd:PTZ00440   756 NRKNEFILhlyendKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLN 815
PTB_LOC417372 cd13168
uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of ...
 118-176 5.99e-03

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: 38.08  E-value: 5.99e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462538516  118 IFEHKAQHISRFIHNSHDLTYFAYLIKAQPDDPESQMACHVFRATDPSQVPDVISSIRQ 176
Cdd:cd13168     60 LFKHSFPEISSCGRRVDDPNYFAYIAGDTPCSLAKHFVCYVFEAADEEEAETILQGIAQ 118
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1022-1166 7.24e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.39  E-value: 7.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516 1022 SLLSSQETLIMECESFENIVEFLKNTLPDMNT--SEMEKIITQV--FEMDISKQLHAYEVEYHVLQDELQESSYSCEDSE 1097
Cdd:TIGR04523  416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdSVKELIIKNLdnTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE 495

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538516 1098 T-LEKLERANSQLKRQNMDLLEKLQVAHTKIQALESnleNLLTRETKMKSLIR------------TLEQEKMAYQKTVEQ 1164
Cdd:TIGR04523  496 KeLKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES---EKKEKESKISDLEDelnkddfelkkeNLEKEIDEKNKEIEE 572


                   ..
gi 2462538516 1165 LR 1166
Cdd:TIGR04523  573 LK 574
 
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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