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Conserved domains on  [gi|528467846|ref|XP_005168426|]
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TBC1 domain family member 1 isoform X1 [Danio rerio]

Protein Classification

PTB_TBC1D1_like and TBC domain-containing protein( domain architecture ID 10351146)

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
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 901-1119 2.98e-76

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: 251.46  E-value: 2.98e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846    901 VGQGVPRQHRGEIWKFLSEQYllrqevpSAKPPNNDTPYKELLKQ----LTSQQHAILIDLGRTFPTHPYFSAQLGAGQL 976
Cdd:smart00164    1 VRKGVPPSLRGVVWKLLLNAQ-------PMDTSADKDLYSRLLKEtapdDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQE 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846    977 SLYNLLKAYSLLDPEVGYCQGLSFVAGVLLLHM-SEEDAFHMLKFLMYDMGLRKqYRPDMIILQIQMYQLSRLLHDYHRE 1055
Cdd:smart00164   74 SLRRVLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYGPNF-YLPDMSGLQLDLLQLDRLVKEYDPD 152

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528467846   1056 LYSHLELYEIGPSLYAAPWFLTAFASHFPLGFVARVFDMLFLQGSEVIFKVALSLLGSHKPLIL 1119
Cdd:smart00164  153 LYKHLKDLGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
 217-410 1.78e-74

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: 243.36  E-value: 1.78e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  217 FAKKFEVLFCGRVVVAHKKAPPALIDECIEKFGRVSVTgslaagirrafslnqvvngtnegdgggkrplffkrdqsfpfl 296
Cdd:cd01269     6 NSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELE------------------------------------------ 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  297 qaldenglspelqrRAADGATGVQPTSLQENRTMLFTIGRSQIFLVSPDTKKVAIEKSFREISFCSQGIRHVDHFGFICR 376
Cdd:cd01269    44 --------------KSRSGPSSVQPTDSEENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDHFGFICR 109

                         170       180       190
                  ....*....|....*....|....*....|....
gi 528467846  377 ESVECGGCQFVCYVFQCANEALVDEIMLTLKQAF 410
Cdd:cd01269   110 ESSEGGGFHFVCYVFKCQSESVVDEIMLTIKQAF 143
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 811-849 1.23e-16

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: 75.28  E-value: 1.23e-16
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 528467846   811 AVPEERRKRSGAELRKLWRKAILQQILLLRMEKENQKLQ 849
Cdd:pfam11830   25 SPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 40-182 5.30e-06

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member smart00462:

Pssm-ID: 473070  Cd Length: 134  Bit Score: 47.31  E-value: 5.30e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846     40 EEVIQYRPTLVGSLAIHPQTTMAILPWVVAEIRRPGVREKNRNlefngnyspeirdQPVVLQISASSVCCIldtagpgkp 119
Cdd:smart00462    1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEP-------------QKVILSISSRGVKLI--------- 58

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528467846    120 wNPLQHMVLFDHRPHHVTKLIHNSQEPSYFGCLLREE--KKAACYVFRCQDqlKVPEIISTLRQA 182
Cdd:smart00462   59 -DEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIARDPgsSRFACHVFRCEK--AAEDIALAIGQA 120
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1139-1259 1.64e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846 1139 GLVQMEKTINQVSemDISKQLQAYEVEYHVLQDELldgpstlshSQRAAQLEKTNGSLRQQNldllEELQVAHAKIRCLE 1218
Cdd:COG4372    36 ALFELDKLQEELE--QLREELEQAREELEQLEEEL---------EQARSELEQLEEELEELN----EQLQAAQAELAQAQ 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 528467846 1219 TRVDGLVNREAELQSQVKTLQQEQTDLQQTVCKLRDLLSSL 1259
Cdd:COG4372   101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141
 
Name Accession Description Interval E-value
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 901-1119 2.98e-76

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: 251.46  E-value: 2.98e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846    901 VGQGVPRQHRGEIWKFLSEQYllrqevpSAKPPNNDTPYKELLKQ----LTSQQHAILIDLGRTFPTHPYFSAQLGAGQL 976
Cdd:smart00164    1 VRKGVPPSLRGVVWKLLLNAQ-------PMDTSADKDLYSRLLKEtapdDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQE 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846    977 SLYNLLKAYSLLDPEVGYCQGLSFVAGVLLLHM-SEEDAFHMLKFLMYDMGLRKqYRPDMIILQIQMYQLSRLLHDYHRE 1055
Cdd:smart00164   74 SLRRVLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYGPNF-YLPDMSGLQLDLLQLDRLVKEYDPD 152

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528467846   1056 LYSHLELYEIGPSLYAAPWFLTAFASHFPLGFVARVFDMLFLQGSEVIFKVALSLLGSHKPLIL 1119
Cdd:smart00164  153 LYKHLKDLGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
 217-410 1.78e-74

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: 243.36  E-value: 1.78e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  217 FAKKFEVLFCGRVVVAHKKAPPALIDECIEKFGRVSVTgslaagirrafslnqvvngtnegdgggkrplffkrdqsfpfl 296
Cdd:cd01269     6 NSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELE------------------------------------------ 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  297 qaldenglspelqrRAADGATGVQPTSLQENRTMLFTIGRSQIFLVSPDTKKVAIEKSFREISFCSQGIRHVDHFGFICR 376
Cdd:cd01269    44 --------------KSRSGPSSVQPTDSEENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDHFGFICR 109

                         170       180       190
                  ....*....|....*....|....*....|....
gi 528467846  377 ESVECGGCQFVCYVFQCANEALVDEIMLTLKQAF 410
Cdd:cd01269   110 ESSEGGGFHFVCYVFKCQSESVVDEIMLTIKQAF 143
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 950-1119 2.52e-55

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


Pssm-ID: 459855  Cd Length: 178  Bit Score: 190.16  E-value: 2.52e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846   950 QHAILIDLGRTFPTHPYFsaQLGAGQLSLYNLLKAYSLLDPEVGYCQGLSFVAGVLLL-HMSEEDAFHMLKFLMYDMGLR 1028
Cdd:pfam00566    9 PEQIEKDVPRTFPHSFFF--DNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLR 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  1029 KQYRPDMIILQIQMYQLSRLLHDYHRELYSHLELYEIGPSLYAAPWFLTAFASHFPLGFVARVFDMLFLQGSEV-IFKVA 1107
Cdd:pfam00566   87 DFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVA 166

                          170
                   ....*....|..
gi 528467846  1108 LSLLGSHKPLIL 1119
Cdd:pfam00566  167 LAILKRFREELL 178
COG5210 COG5210
GTPase-activating protein [General function prediction only];
832-1127 1.17e-49

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 184.62  E-value: 1.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  832 ILQQILLLRMEKENQKLqasESDLQCKRQKLDYEEitPCLkdvTLVWERMLGTAGRAKVRFDMDEIHGAVGQGVPRQHRG 911
Cdd:COG5210   148 KGSSSLNSNPELNKEIN---ELSLKEEPQKLRYYE--LAA---DKLWISYLDPNPLSFLPVQLSKLRELIRKGIPNELRG 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  912 EIWKFLSEQYLLRQEVPSAKPPNNDtpYKELLKQLTSQQ-HAILIDLGRTFPTHPYFSAQLGAGQLSLYNLLKAYSLLDP 990
Cdd:COG5210   220 DVWEFLLGIGFDLDKNPGLYERLLN--LHREAKIPTQEIiSQIEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSLYNP 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  991 EVGYCQGLSFVAGVLLLHM-SEEDAFHMLKFLMYDMGLRKQYRPDMIILQIQMYQLSRLLHDYHRELYSHLELYEIGPSL 1069
Cdd:COG5210   298 EVGYVQGMNFLAAPLLLVLeSEEQAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVVLLM 377

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 528467846 1070 YAAPWFLTAFASHFPLGFVARVFDMLFLQGSEVIFKVALSLLGSHKPLILQHDNLEAI 1127
Cdd:COG5210   378 FAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELL 435
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 320-423 5.48e-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: 90.07  E-value: 5.48e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846    320 QPTSLQENRTMLFTIGRSQIFLVSPDTKKVAIEKSFREISFCSQGIRHVDHFGFICResvECGGCQFVCYVFQCANEAlv 399
Cdd:smart00462   36 QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIAR---DPGSSRFACHVFRCEKAA-- 110

                            90       100
                    ....*....|....*....|....
gi 528467846    400 DEIMLTLKQAFSVAALQQNSRTQS 423
Cdd:smart00462  111 EDIALAIGQAFQLAYELKLKARSE 134
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 811-849 1.23e-16

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: 75.28  E-value: 1.23e-16
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 528467846   811 AVPEERRKRSGAELRKLWRKAILQQILLLRMEKENQKLQ 849
Cdd:pfam11830   25 SPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 40-182 5.30e-06

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: 47.31  E-value: 5.30e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846     40 EEVIQYRPTLVGSLAIHPQTTMAILPWVVAEIRRPGVREKNRNlefngnyspeirdQPVVLQISASSVCCIldtagpgkp 119
Cdd:smart00462    1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEP-------------QKVILSISSRGVKLI--------- 58

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528467846    120 wNPLQHMVLFDHRPHHVTKLIHNSQEPSYFGCLLREE--KKAACYVFRCQDqlKVPEIISTLRQA 182
Cdd:smart00462   59 -DEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIARDPgsSRFACHVFRCEK--AAEDIALAIGQA 120
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 68-182 2.79e-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: 44.81  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846   68 VAEIRRPGVREKNRNLEFNGNYSPEIRDQPVVLQISASSVCCildtagpgkpWNPLQHMVLFDHRPHHVTKLIHNSQEPS 147
Cdd:cd00934    13 VGSSRGVDVVEEALKALAAALKSSKRKPGPVLLEVSSKGVKL----------LDLDTKELLLRHPLHRISYCGRDPDNPN 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 528467846  148 YFGCLLREE--KKAACYVFRCQDQLKVPEIISTLRQA 182
Cdd:cd00934    83 VFAFIAGEEggSGFRCHVFQCEDEEEAEEILQAIGQA 119
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
330-413 7.64e-05

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 43.89  E-value: 7.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846   330 MLFTIGRSQIFLVSPDTKKVAIEKSFREISFCSQG-IRHVDHFGFICRESVEcggCQFVCYVFQCANEAlvDEIMLTLKQ 408
Cdd:pfam00640   54 VDLFISTDGLKLLNPDTQELIHDHPLVSISFCADGdPDLMRYFAYIARDKAT---NKFACHVFESEDGA--QDIAQSIGQ 128


                   ....*
gi 528467846   409 AFSVA 413
Cdd:pfam00640  129 AFALA 133
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1139-1259 1.64e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846 1139 GLVQMEKTINQVSemDISKQLQAYEVEYHVLQDELldgpstlshSQRAAQLEKTNGSLRQQNldllEELQVAHAKIRCLE 1218
Cdd:COG4372    36 ALFELDKLQEELE--QLREELEQAREELEQLEEEL---------EQARSELEQLEEELEELN----EQLQAAQAELAQAQ 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 528467846 1219 TRVDGLVNREAELQSQVKTLQQEQTDLQQTVCKLRDLLSSL 1259
Cdd:COG4372   101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1140-1259 4.44e-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: 41.54  E-value: 4.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  1140 LVQMEKTINQVSEM--DISKQLQAYEVEYHVLQDELldgpstlshSQRAAQLEKtngsLRQQNLDLLEELQVAHAKIRCL 1217
Cdd:TIGR04523  330 ISQNNKIISQLNEQisQLKKELTNSESENSEKQREL---------EEKQNEIEK----LKKENQSYKQEIKNLESQINDL 396

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 528467846  1218 ETRVDGLVNREAELQSQVKTLQQ-------EQTDLQQTVCKLRDLLSSL 1259
Cdd:TIGR04523  397 ESKIQNQEKLNQQKDEQIKKLQQekellekEIERLKETIIKNNSEIKDL 445
 
Name Accession Description Interval E-value
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 901-1119 2.98e-76

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: 251.46  E-value: 2.98e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846    901 VGQGVPRQHRGEIWKFLSEQYllrqevpSAKPPNNDTPYKELLKQ----LTSQQHAILIDLGRTFPTHPYFSAQLGAGQL 976
Cdd:smart00164    1 VRKGVPPSLRGVVWKLLLNAQ-------PMDTSADKDLYSRLLKEtapdDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQE 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846    977 SLYNLLKAYSLLDPEVGYCQGLSFVAGVLLLHM-SEEDAFHMLKFLMYDMGLRKqYRPDMIILQIQMYQLSRLLHDYHRE 1055
Cdd:smart00164   74 SLRRVLKAYALYNPEVGYCQGMNFLAAPLLLVMeDEEDAFWCLVKLMERYGPNF-YLPDMSGLQLDLLQLDRLVKEYDPD 152

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528467846   1056 LYSHLELYEIGPSLYAAPWFLTAFASHFPLGFVARVFDMLFLQGSEVIFKVALSLLGSHKPLIL 1119
Cdd:smart00164  153 LYKHLKDLGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
 217-410 1.78e-74

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: 243.36  E-value: 1.78e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  217 FAKKFEVLFCGRVVVAHKKAPPALIDECIEKFGRVSVTgslaagirrafslnqvvngtnegdgggkrplffkrdqsfpfl 296
Cdd:cd01269     6 NSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELE------------------------------------------ 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  297 qaldenglspelqrRAADGATGVQPTSLQENRTMLFTIGRSQIFLVSPDTKKVAIEKSFREISFCSQGIRHVDHFGFICR 376
Cdd:cd01269    44 --------------KSRSGPSSVQPTDSEENRTMLFQIGRSELRLISPDTKQVLLEKQFKDISSCSQGIKHVDHFGFICR 109

                         170       180       190
                  ....*....|....*....|....*....|....
gi 528467846  377 ESVECGGCQFVCYVFQCANEALVDEIMLTLKQAF 410
Cdd:cd01269   110 ESSEGGGFHFVCYVFKCQSESVVDEIMLTIKQAF 143
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 950-1119 2.52e-55

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


Pssm-ID: 459855  Cd Length: 178  Bit Score: 190.16  E-value: 2.52e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846   950 QHAILIDLGRTFPTHPYFsaQLGAGQLSLYNLLKAYSLLDPEVGYCQGLSFVAGVLLL-HMSEEDAFHMLKFLMYDMGLR 1028
Cdd:pfam00566    9 PEQIEKDVPRTFPHSFFF--DNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLR 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  1029 KQYRPDMIILQIQMYQLSRLLHDYHRELYSHLELYEIGPSLYAAPWFLTAFASHFPLGFVARVFDMLFLQGSEV-IFKVA 1107
Cdd:pfam00566   87 DFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVA 166

                          170
                   ....*....|..
gi 528467846  1108 LSLLGSHKPLIL 1119
Cdd:pfam00566  167 LAILKRFREELL 178
COG5210 COG5210
GTPase-activating protein [General function prediction only];
832-1127 1.17e-49

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 184.62  E-value: 1.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  832 ILQQILLLRMEKENQKLqasESDLQCKRQKLDYEEitPCLkdvTLVWERMLGTAGRAKVRFDMDEIHGAVGQGVPRQHRG 911
Cdd:COG5210   148 KGSSSLNSNPELNKEIN---ELSLKEEPQKLRYYE--LAA---DKLWISYLDPNPLSFLPVQLSKLRELIRKGIPNELRG 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  912 EIWKFLSEQYLLRQEVPSAKPPNNDtpYKELLKQLTSQQ-HAILIDLGRTFPTHPYFSAQLGAGQLSLYNLLKAYSLLDP 990
Cdd:COG5210   220 DVWEFLLGIGFDLDKNPGLYERLLN--LHREAKIPTQEIiSQIEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSLYNP 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  991 EVGYCQGLSFVAGVLLLHM-SEEDAFHMLKFLMYDMGLRKQYRPDMIILQIQMYQLSRLLHDYHRELYSHLELYEIGPSL 1069
Cdd:COG5210   298 EVGYVQGMNFLAAPLLLVLeSEEQAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVVLLM 377

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 528467846 1070 YAAPWFLTAFASHFPLGFVARVFDMLFLQGSEVIFKVALSLLGSHKPLILQHDNLEAI 1127
Cdd:COG5210   378 FAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELL 435
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 320-423 5.48e-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: 90.07  E-value: 5.48e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846    320 QPTSLQENRTMLFTIGRSQIFLVSPDTKKVAIEKSFREISFCSQGIRHVDHFGFICResvECGGCQFVCYVFQCANEAlv 399
Cdd:smart00462   36 QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIAR---DPGSSRFACHVFRCEKAA-- 110

                            90       100
                    ....*....|....*....|....
gi 528467846    400 DEIMLTLKQAFSVAALQQNSRTQS 423
Cdd:smart00462  111 EDIALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 325-410 7.35e-19

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: 83.71  E-value: 7.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  325 QENRTMLFTIGRSQIFLVSPDTKKVAIEKSFREISFCSQGIRHVDHFGFICRESvecGGCQFVCYVFQCANEALVDEIML 404
Cdd:cd00934    38 RKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDNPNVFAFIAGEE---GGSGFRCHVFQCEDEEEAEEILQ 114


                  ....*.
gi 528467846  405 TLKQAF 410
Cdd:cd00934   115 AIGQAF 120
DUF3350 pfam11830
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ...
 811-849 1.23e-16

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: 75.28  E-value: 1.23e-16
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 528467846   811 AVPEERRKRSGAELRKLWRKAILQQILLLRMEKENQKLQ 849
Cdd:pfam11830   25 SPVGEKKKRTSEELRELWRKAIHQQILLLRMEKENQKLE 63
PTB_LOC417372 cd13168
uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of ...
 323-410 6.04e-07

uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of LOC417372 and its related proteins are unknown to date. Members here contain a N-terminal RUN domain, followed by a PDZ domain, and a C-terminal PTB domain. The RUN domain is involved in Ras-like GTPase signaling. The PDZ domain (also called DHR/Dlg homologous region or GLGF after its conserved sequence motif) binds C-terminal polypeptides, internal (non-C-terminal) polypeptides, and lipids. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269989  Cd Length: 125  Bit Score: 49.63  E-value: 6.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  323 SLQENRTMLFTIGRSQIFLVSPDTKKVAIEKSFREISFCSQGIRHVDHFGFICRESVECGGCQFVCYVFQCANEALVDEI 402
Cdd:cd13168    33 SDLTPKEVLLELGEIGVTVWDKSTSEVLFKHSFPEISSCGRRVDDPNYFAYIAGDTPCSLAKHFVCYVFEAADEEEAETI 112


                  ....*...
gi 528467846  403 MLTLKQAF 410
Cdd:cd13168   113 LQGIAQGF 120
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 40-182 5.30e-06

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: 47.31  E-value: 5.30e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846     40 EEVIQYRPTLVGSLAIHPQTTMAILPWVVAEIRRPGVREKNRNlefngnyspeirdQPVVLQISASSVCCIldtagpgkp 119
Cdd:smart00462    1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEP-------------QKVILSISSRGVKLI--------- 58

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528467846    120 wNPLQHMVLFDHRPHHVTKLIHNSQEPSYFGCLLREE--KKAACYVFRCQDqlKVPEIISTLRQA 182
Cdd:smart00462   59 -DEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIARDPgsSRFACHVFRCEK--AAEDIALAIGQA 120
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 342-417 1.42e-05

Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family Phosphotyrosine-binding (PTB) domain; Both AIDA-1b (AbetaPP intracellular domain-associated protein 1b) and Odin (also known as ankyrin repeat and sterile alpha motif domain-containing 1A; ANKS1A) belong to the Anks protein family. Both of these family members interacts with the EphA8 receptor. Ank members consists of ankyrin repeats, a SAM domain and a C-terminal PTB domain which is crucial for interaction with the juxtamembrane (JM) region of EphA8. PTB domains are classified into three groups, namely, phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains of which the Anks PTB is a member. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269972  Cd Length: 146  Bit Score: 46.12  E-value: 1.42e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528467846  342 VSPDTKKVAIEKSFREISFCSQGIRHVDHFGFICRESVecGGCQFvCYVFQCANEALVDEIMLTLKQAFSVA---ALQQ 417
Cdd:cd01274    68 IDATTKNLICEHEIRNISCACQDPEDLNTFAYITKDLK--TDHHY-CHVFCVLTVDLATEIILTLGQAFEVAyqlALRA 143
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 68-182 2.79e-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: 44.81  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846   68 VAEIRRPGVREKNRNLEFNGNYSPEIRDQPVVLQISASSVCCildtagpgkpWNPLQHMVLFDHRPHHVTKLIHNSQEPS 147
Cdd:cd00934    13 VGSSRGVDVVEEALKALAAALKSSKRKPGPVLLEVSSKGVKL----------LDLDTKELLLRHPLHRISYCGRDPDNPN 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 528467846  148 YFGCLLREE--KKAACYVFRCQDQLKVPEIISTLRQA 182
Cdd:cd00934    83 VFAFIAGEEggSGFRCHVFQCEDEEEAEEILQAIGQA 119
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
330-413 7.64e-05

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 43.89  E-value: 7.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846   330 MLFTIGRSQIFLVSPDTKKVAIEKSFREISFCSQG-IRHVDHFGFICRESVEcggCQFVCYVFQCANEAlvDEIMLTLKQ 408
Cdd:pfam00640   54 VDLFISTDGLKLLNPDTQELIHDHPLVSISFCADGdPDLMRYFAYIARDKAT---NKFACHVFESEDGA--QDIAQSIGQ 128


                   ....*
gi 528467846   409 AFSVA 413
Cdd:pfam00640  129 AFALA 133
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 337-414 4.05e-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: 4.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528467846  337 SQIFLVSPDTKKVAIEKSFREISFCSQGIRHVDHFGFICRESVECGGcqfVCYVFQCANEAlvDEIMLTLKQAFSVAA 414
Cdd:cd13161    47 EGIRVVERLTGEVLTNVPIKDISFVTVDPKDKKLFAFISHDPRLGRI---TCHVFRCKRGA--QEICDTIAEAFKAAA 119
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1139-1259 1.64e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846 1139 GLVQMEKTINQVSemDISKQLQAYEVEYHVLQDELldgpstlshSQRAAQLEKTNGSLRQQNldllEELQVAHAKIRCLE 1218
Cdd:COG4372    36 ALFELDKLQEELE--QLREELEQAREELEQLEEEL---------EQARSELEQLEEELEELN----EQLQAAQAELAQAQ 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 528467846 1219 TRVDGLVNREAELQSQVKTLQQEQTDLQQTVCKLRDLLSSL 1259
Cdd:COG4372   101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 339-411 1.72e-03

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins Phosphotyrosine-binding (PTB) PH-like fold; The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd contains mammals, insects, and sponges.


Pssm-ID: 269981  Cd Length: 123  Bit Score: 39.62  E-value: 1.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528467846  339 IFLVSPDTKKVAIEKSFREISFCSQGIRHVDHFGFICRESVECGgcqFVCYVFQCANEALVDEIMLTLKQAFS 411
Cdd:cd13159    54 IKVTDSATNETILEVSIYRISYCTADANHDKVFAFIATNQDNEK---LECHAFLCAKRKMAQAVTLTVAQAFN 123
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
 328-417 2.53e-03

Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal function, muscle regeneration, and cell migration. It binds to actin filaments and interacts with the cytoplasmic tails of beta-integrin via its PTB domain, allowing tensin to link actin filaments to integrin receptors. Tensin functions as a platform for assembly and disassembly of signaling complexes at focal adhesions by recruiting tyrosine-phosphorylated signaling molecules, and also by providing interaction sites for other proteins. In addition to its PTB domain, it contains a C-terminal SH2 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.


Pssm-ID: 269979  Cd Length: 129  Bit Score: 39.29  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  328 RTMLFTIGRSQIFLVSPDTKKVAIEKSFREISFCSqgIRHVDH-FGFICRESVECGGCQFvCYVFQCANEALVDEIMLTL 406
Cdd:cd13157    41 RPVILSVSLSGIKICSEDGKVVLMAHALRRVSYST--CRPAHAqFAFVARNPGGPTNRQY-CHVFVTRSPREAQELNLLL 117

                          90
                  ....*....|.
gi 528467846  407 KQAFSVAALQQ 417
Cdd:cd13157   118 CRAFQLAYLKQ 128
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1140-1259 4.44e-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: 41.54  E-value: 4.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  1140 LVQMEKTINQVSEM--DISKQLQAYEVEYHVLQDELldgpstlshSQRAAQLEKtngsLRQQNLDLLEELQVAHAKIRCL 1217
Cdd:TIGR04523  330 ISQNNKIISQLNEQisQLKKELTNSESENSEKQREL---------EEKQNEIEK----LKKENQSYKQEIKNLESQINDL 396

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 528467846  1218 ETRVDGLVNREAELQSQVKTLQQ-------EQTDLQQTVCKLRDLLSSL 1259
Cdd:TIGR04523  397 ESKIQNQEKLNQQKDEQIKKLQQekellekEIERLKETIIKNNSEIKDL 445
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1184-1257 4.92e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 4.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528467846 1184 QRAAQLEKTNGSLRQQNLDLLEELQVAHAKIRCLETRVDGLVNREAELQSQVKTLQQEQTDLQQTVCKLRDLLS 1257
Cdd:COG4717    53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 341-413 4.93e-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: 38.80  E-value: 4.93e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528467846  341 LVSPDTKKVAIEKSFREISFCSQGIRHVDHFGFICRESvecGGCQFVCYVFQCanEALVDEIMLTLKQAFSVA 413
Cdd:cd01273    68 IQDPKTKVIMHQFPLHRISFCADDKTDKRIFSFIAKDS---ESEKHLCFVFDS--EKLAEEITLTIGQAFDLA 135
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1142-1249 7.52e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 7.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846 1142 QMEKTINQVSEmdISKQLQAYEVEYHVLQDELldgpSTLShsQRAAQLEKTNGSLRQQNLDLLEELQVAHAKIRCLETRV 1221
Cdd:COG4372    74 ELEQLEEELEE--LNEQLQAAQAELAQAQEEL----ESLQ--EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145

                          90       100
                  ....*....|....*....|....*...
gi 528467846 1222 DGLVNREAELQSQVKTLQQEQTDLQQTV 1249
Cdd:COG4372   146 AEREEELKELEEQLESLQEELAALEQEL 173
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1117-1259 8.96e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 8.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846  1117 LILQHDNLEAIVEFIKTTLPNLGlvqmektiNQVSEMD-----ISKQLQAYEVEYHVLQDELLDGPSTLSHSQ-RAAQLE 1190
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALA--------NEISRLEqqkqiLRERLANLERQLEELEAQLEELESKLDELAeELAELE 343

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528467846  1191 KTNGSLRQQNLDLLEELQVAHAKIRCLETRVDGLVNREAELQSQVKTLQQEQTDLQQTVCKLRDLLSSL 1259
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1142-1259 9.57e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 9.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467846 1142 QMEKTINQVSEMDISKQLQAYEVEYHVLQDELLDGPSTLS--HSQRAA---QLEKTNGSLRQQNLDLLEELQvahAKIRC 1216
Cdd:COG3206   248 QLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTpnHPDVIAlraQIAALRAQLQQEAQRILASLE---AELEA 324

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 528467846 1217 LETRVDGLVNREAELQSQVKTL---QQEQTDLQQTVCKLRDLLSSL 1259
Cdd:COG3206   325 LQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESL 370
 
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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