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Conserved domains on  [gi|1486857881|ref|NP_001353377|]
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rab GTPase-activating protein 1-like isoform I [Homo sapiens]

Protein Classification

PTB_Rab6GAP and TBC domain-containing protein( domain architecture ID 10100584)

protein containing domains PTB_Rab6GAP, DUF3694, TBC, and SMC_prok_B

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 129-257 5.59e-75

GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a centrosome-associated GTPase activating protein (GAP) for Rab 6. It consists of an N-terminal PTB domain and a C-terminal TBC 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 is part of the Dab-like subgroup.


:

Pssm-ID: 269922  Cd Length: 129  Bit Score: 242.15  E-value: 5.59e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 129 VLFNKLTYLGCMKVSSPRNEVEALRAMATMKSSSQYPFPVTLYVPNVPEGSVRIIDQSSNVEIASFPIYKVLFCARGHDG 208
Cdd:cd01211     1 TIFNGVTYLGCAKVNAPRSETEALRIMAILREQSAQPIKVTLSVPNSSEGSVRLYDPTSNTEIASYPIYRILFCARGPDG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1486857881 209 TTESNCFAFTESSHGSEEFQIHVFSCEIKEAVSRILYSFCTAFKRSSRQ 257
Cdd:cd01211    81 TSESDCFAFTWSHGETAIFQCHVFRCEIPEAVSKVLYSFAKAFRRVPKS 129
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 535-744 6.03e-70

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


:

Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 231.81  E-value: 6.03e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881  535 VKSGVPEALRAEVWQLLAGCH--DNQAMLDRYRILIT----KDSAQESVITRDIHRTFPAHDYFKDTGGDGQESLYKICK 608
Cdd:smart00164   1 VRKGVPPSLRGVVWKLLLNAQpmDTSADKDLYSRLLKetapDDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881  609 AYSVYDEDIGYCQGQSFLAAVLLLHMP-EEQAFCVLVKIMYDYGLRdLYRNNFEDLHCKFYQLERLMQEQLPDLHSHFSD 687
Cdd:smart00164  81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1486857881  688 LNLEAHMYASQWFLTLFTAKFPLCMVFHIIDLLLCEGLNIIFHVALALLKTSKEDLL 744
Cdd:smart00164 160 LGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 290-421 1.84e-41

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


:

Pssm-ID: 463599  Cd Length: 149  Bit Score: 148.89  E-value: 1.84e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 290 NFSPVPKDR----DKFYFKLKQGIEKKVVITVQQLSNKELAIERCfgmllspgRNVKNSDMHLLDMesMGKSYDGRA--- 362
Cdd:pfam12473   1 EYVPVPVDQrselDPGTFQLHQGLQRRIVITLTHSSGDELPWERV--------RNVRVGDVRLLDM--KGRVPDSDStpd 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1486857881 363 --------------------YVITGMWNPNAPVFLALNEETPKDKQVYMTVAVDMVVTEVVEPVRFLLETVVRVYPANE 421
Cdd:pfam12473  71 vslkllskpvvrfnadgtssYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEKCAEPVRFSMDTAVQIYPRDE 149
 
Name Accession Description Interval E-value
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 129-257 5.59e-75

GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a centrosome-associated GTPase activating protein (GAP) for Rab 6. It consists of an N-terminal PTB domain and a C-terminal TBC 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 is part of the Dab-like subgroup.


Pssm-ID: 269922  Cd Length: 129  Bit Score: 242.15  E-value: 5.59e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 129 VLFNKLTYLGCMKVSSPRNEVEALRAMATMKSSSQYPFPVTLYVPNVPEGSVRIIDQSSNVEIASFPIYKVLFCARGHDG 208
Cdd:cd01211     1 TIFNGVTYLGCAKVNAPRSETEALRIMAILREQSAQPIKVTLSVPNSSEGSVRLYDPTSNTEIASYPIYRILFCARGPDG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1486857881 209 TTESNCFAFTESSHGSEEFQIHVFSCEIKEAVSRILYSFCTAFKRSSRQ 257
Cdd:cd01211    81 TSESDCFAFTWSHGETAIFQCHVFRCEIPEAVSKVLYSFAKAFRRVPKS 129
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 535-744 6.03e-70

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 231.81  E-value: 6.03e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881  535 VKSGVPEALRAEVWQLLAGCH--DNQAMLDRYRILIT----KDSAQESVITRDIHRTFPAHDYFKDTGGDGQESLYKICK 608
Cdd:smart00164   1 VRKGVPPSLRGVVWKLLLNAQpmDTSADKDLYSRLLKetapDDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881  609 AYSVYDEDIGYCQGQSFLAAVLLLHMP-EEQAFCVLVKIMYDYGLRdLYRNNFEDLHCKFYQLERLMQEQLPDLHSHFSD 687
Cdd:smart00164  81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1486857881  688 LNLEAHMYASQWFLTLFTAKFPLCMVFHIIDLLLCEGLNIIFHVALALLKTSKEDLL 744
Cdd:smart00164 160 LGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 541-744 1.43e-67

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: 223.67  E-value: 1.43e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 541 EALRAEVWQllagchdnqamldryrilitkdsaqeSVITRDIHRTFPAHDYFKDtgGDGQESLYKICKAYSVYDEDIGYC 620
Cdd:pfam00566   1 DELRGQVWP--------------------------EQIEKDVPRTFPHSFFFDN--GPGQNSLRRILKAYSIYNPDVGYC 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 621 QGQSFLAAVLLL-HMPEEQAFCVLVKIMYDYGLRDLYRNNFEDLHCKFYQLERLMQEQLPDLHSHFSDLNLEAHMYASQW 699
Cdd:pfam00566  53 QGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLRDFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQW 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1486857881 700 FLTLFTAKFPLCMVFHIIDLLLCEGL-NIIFHVALALLKTSKEDLL 744
Cdd:pfam00566 133 FLTLFAREFPLSTVLRIWDYFFLEGEkFVLFRVALAILKRFREELL 178
COG5210 COG5210
GTPase-activating protein [General function prediction only];
531-752 1.50e-49

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 183.46  E-value: 1.50e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 531 LSTLVKSGVPEALRAEVWQLLAGCH-DNQAMLDRYRILI-----TKDSAQESV--ITRDIHRTFPAHDYFKDTGGDGQES 602
Cdd:COG5210   205 LRELIRKGIPNELRGDVWEFLLGIGfDLDKNPGLYERLLnlhreAKIPTQEIIsqIEKDLSRTFPDNSLFQTEISIRAEN 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 603 LYKICKAYSVYDEDIGYCQGQSFLAAVLLLHMP-EEQAFCVLVKIMYDYGLRDLYRNNFEDLHCKFYQLERLMQEQLPDL 681
Cdd:COG5210   285 LRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLEsEEQAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPEL 364

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1486857881 682 HSHFSDLNLEAHMYASQWFLTLFTAKFPLCMVFHIIDLLLCEGLNIIFHVALALLKTSKEDLLQADFEGAL 752
Cdd:COG5210   365 YEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELL 435
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 290-421 1.84e-41

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


Pssm-ID: 463599  Cd Length: 149  Bit Score: 148.89  E-value: 1.84e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 290 NFSPVPKDR----DKFYFKLKQGIEKKVVITVQQLSNKELAIERCfgmllspgRNVKNSDMHLLDMesMGKSYDGRA--- 362
Cdd:pfam12473   1 EYVPVPVDQrselDPGTFQLHQGLQRRIVITLTHSSGDELPWERV--------RNVRVGDVRLLDM--KGRVPDSDStpd 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1486857881 363 --------------------YVITGMWNPNAPVFLALNEETPKDKQVYMTVAVDMVVTEVVEPVRFLLETVVRVYPANE 421
Cdd:pfam12473  71 vslkllskpvvrfnadgtssYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEKCAEPVRFSMDTAVQIYPRDE 149
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 126-257 7.63e-19

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


Pssm-ID: 214675  Cd Length: 134  Bit Score: 83.52  E-value: 7.63e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881  126 EDSVLFNkLTYLGCMKVSSPRNEVEALRAM----ATMKSSSQYPFPVTLyvpNVPEGSVRIIDQSSNVEIASFPIYKVLF 201
Cdd:smart00462   1 GSGVSFR-VKYLGSVEVPEARGLQVVQEAIrklrAAQGSEKKEPQKVIL---SISSRGVKLIDEDTKAVLHEHPLRRISF 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1486857881  202 CARGHDGtteSNCFAFTESSHGSEEFQIHVFSCEI--KEAVSRILYSFCTAFKRSSRQ 257
Cdd:smart00462  77 CAVGPDD---LDVFGYIARDPGSSRFACHVFRCEKaaEDIALAIGQAFQLAYELKLKA 131
 
Name Accession Description Interval E-value
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 129-257 5.59e-75

GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a centrosome-associated GTPase activating protein (GAP) for Rab 6. It consists of an N-terminal PTB domain and a C-terminal TBC 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 is part of the Dab-like subgroup.


Pssm-ID: 269922  Cd Length: 129  Bit Score: 242.15  E-value: 5.59e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 129 VLFNKLTYLGCMKVSSPRNEVEALRAMATMKSSSQYPFPVTLYVPNVPEGSVRIIDQSSNVEIASFPIYKVLFCARGHDG 208
Cdd:cd01211     1 TIFNGVTYLGCAKVNAPRSETEALRIMAILREQSAQPIKVTLSVPNSSEGSVRLYDPTSNTEIASYPIYRILFCARGPDG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1486857881 209 TTESNCFAFTESSHGSEEFQIHVFSCEIKEAVSRILYSFCTAFKRSSRQ 257
Cdd:cd01211    81 TSESDCFAFTWSHGETAIFQCHVFRCEIPEAVSKVLYSFAKAFRRVPKS 129
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 535-744 6.03e-70

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 231.81  E-value: 6.03e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881  535 VKSGVPEALRAEVWQLLAGCH--DNQAMLDRYRILIT----KDSAQESVITRDIHRTFPAHDYFKDTGGDGQESLYKICK 608
Cdd:smart00164   1 VRKGVPPSLRGVVWKLLLNAQpmDTSADKDLYSRLLKetapDDKSIVHQIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881  609 AYSVYDEDIGYCQGQSFLAAVLLLHMP-EEQAFCVLVKIMYDYGLRdLYRNNFEDLHCKFYQLERLMQEQLPDLHSHFSD 687
Cdd:smart00164  81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1486857881  688 LNLEAHMYASQWFLTLFTAKFPLCMVFHIIDLLLCEGLNIIFHVALALLKTSKEDLL 744
Cdd:smart00164 160 LGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 541-744 1.43e-67

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: 223.67  E-value: 1.43e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 541 EALRAEVWQllagchdnqamldryrilitkdsaqeSVITRDIHRTFPAHDYFKDtgGDGQESLYKICKAYSVYDEDIGYC 620
Cdd:pfam00566   1 DELRGQVWP--------------------------EQIEKDVPRTFPHSFFFDN--GPGQNSLRRILKAYSIYNPDVGYC 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 621 QGQSFLAAVLLL-HMPEEQAFCVLVKIMYDYGLRDLYRNNFEDLHCKFYQLERLMQEQLPDLHSHFSDLNLEAHMYASQW 699
Cdd:pfam00566  53 QGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLRDFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQW 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1486857881 700 FLTLFTAKFPLCMVFHIIDLLLCEGL-NIIFHVALALLKTSKEDLL 744
Cdd:pfam00566 133 FLTLFAREFPLSTVLRIWDYFFLEGEkFVLFRVALAILKRFREELL 178
COG5210 COG5210
GTPase-activating protein [General function prediction only];
531-752 1.50e-49

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 183.46  E-value: 1.50e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 531 LSTLVKSGVPEALRAEVWQLLAGCH-DNQAMLDRYRILI-----TKDSAQESV--ITRDIHRTFPAHDYFKDTGGDGQES 602
Cdd:COG5210   205 LRELIRKGIPNELRGDVWEFLLGIGfDLDKNPGLYERLLnlhreAKIPTQEIIsqIEKDLSRTFPDNSLFQTEISIRAEN 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 603 LYKICKAYSVYDEDIGYCQGQSFLAAVLLLHMP-EEQAFCVLVKIMYDYGLRDLYRNNFEDLHCKFYQLERLMQEQLPDL 681
Cdd:COG5210   285 LRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLEsEEQAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPEL 364

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1486857881 682 HSHFSDLNLEAHMYASQWFLTLFTAKFPLCMVFHIIDLLLCEGLNIIFHVALALLKTSKEDLLQADFEGAL 752
Cdd:COG5210   365 YEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELL 435
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 290-421 1.84e-41

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


Pssm-ID: 463599  Cd Length: 149  Bit Score: 148.89  E-value: 1.84e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 290 NFSPVPKDR----DKFYFKLKQGIEKKVVITVQQLSNKELAIERCfgmllspgRNVKNSDMHLLDMesMGKSYDGRA--- 362
Cdd:pfam12473   1 EYVPVPVDQrselDPGTFQLHQGLQRRIVITLTHSSGDELPWERV--------RNVRVGDVRLLDM--KGRVPDSDStpd 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1486857881 363 --------------------YVITGMWNPNAPVFLALNEETPKDKQVYMTVAVDMVVTEVVEPVRFLLETVVRVYPANE 421
Cdd:pfam12473  71 vslkllskpvvrfnadgtssYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEKCAEPVRFSMDTAVQIYPRDE 149
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 133-251 1.29e-20

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: 88.33  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 133 KLTYLGCMKVSSPRN----EVEALRAMATMKSSSQYPFPVTLyvpNVPEGSVRIIDQSSNVEIASFPIYKVLFCARGHDg 208
Cdd:cd00934     4 QVKYLGSVEVGSSRGvdvvEEALKALAAALKSSKRKPGPVLL---EVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPD- 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1486857881 209 ttESNCFAFTESSHGSEEFQIHVFSCEIKEAVSRILYSFCTAF 251
Cdd:cd00934    80 --NPNVFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQAF 120
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 126-257 7.63e-19

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


Pssm-ID: 214675  Cd Length: 134  Bit Score: 83.52  E-value: 7.63e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881  126 EDSVLFNkLTYLGCMKVSSPRNEVEALRAM----ATMKSSSQYPFPVTLyvpNVPEGSVRIIDQSSNVEIASFPIYKVLF 201
Cdd:smart00462   1 GSGVSFR-VKYLGSVEVPEARGLQVVQEAIrklrAAQGSEKKEPQKVIL---SISSRGVKLIDEDTKAVLHEHPLRRISF 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1486857881  202 CARGHDGtteSNCFAFTESSHGSEEFQIHVFSCEI--KEAVSRILYSFCTAFKRSSRQ 257
Cdd:smart00462  77 CAVGPDD---LDVFGYIARDPGSSRFACHVFRCEKaaEDIALAIGQAFQLAYELKLKA 131
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 127-234 4.41e-08

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: 52.72  E-value: 4.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 127 DSVLFnKLTYLGCMKVSSPRNE---VEALR-AMATMKSSSQYPFPVTLYVPnvPEGsVRIIDQSSNVEIASFPIYKVLFC 202
Cdd:cd13159     1 DGVTF-YLKYLGSTLVEKPKGEgatAEAVKtIIAMAKASGKKLQKVTLTVS--PKG-IKVTDSATNETILEVSIYRISYC 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1486857881 203 A--RGHDgttesNCFAFTESSHGSEEFQIHVFSC 234
Cdd:cd13159    77 TadANHD-----KVFAFIATNQDNEKLECHAFLC 105
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 136-242 9.56e-04

Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which plays critical roles in cell fate determination. Numb proteins are involved in control of asymmetric cell division and cell fate choice, endocytosis, cell adhesion, cell migration, ubiquitination of specific substrates and a number of signaling pathways (Notch, Hedgehog, p53). Mutations in Numb plays a critical role in disease (cancer). Numb has an N-terminal PTB domain and a C-terminal NumbF 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 is part of the Dab-like subgroup.


Pssm-ID: 241298  Cd Length: 135  Bit Score: 40.37  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 136 YLGCMKVSSPRNEVEALRAMATMKSSSQYPFPVTLYVPnvPEGsVRIIDQSSNVEIASFPIYKVLFCA--RGH------- 206
Cdd:cd01268    21 YLGCVEVGESRGMQVCEEALKKLKASRKKPVRAVLWVS--GDG-LRVVDEKTKGLIVDQTIEKVSFCApdRNHerafsyi 97

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1486857881 207 --DGTTES-NCFAFTESSHGSEEFQiHVFSCEIKEAVSR 242
Cdd:cd01268    98 crDGTTRRwMCHCFLAVKDSGERLS-HAVGCAFAACLER 135
PTB_APPL cd13158
Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called ...
 125-239 4.58e-03

Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called DCC-interacting protein (DIP)-13alpha) Phosphotyrosine-binding (PTB) domain; APPL interacts with oncoprotein serine/threonine kinase AKT2, tumor suppressor protein DCC (deleted in colorectal cancer), Rab5, GIPC (GAIP-interacting protein, C terminus), human follicle-stimulating hormone receptor (FSHR), and the adiponectin receptors AdipoR1 and AdipoR2. There are two isoforms of human APPL: APPL1 and APPL2, which share about 50% sequence identity. APPL has a BAR and a PH domain near its N terminus, and the two domains are thought to function as a unit (BAR-PH domain). C-terminal to this is a PTB domain. Lipid binding assays show that the BAR, PH, and PTB domains can bind phospholipids. 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: 269980  Cd Length: 135  Bit Score: 38.48  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857881 125 EEDSVLFNKLT--YLGCMKVSSPRNEVEALRAM-----ATMKSSSqypFPVTLYVPNVPEGSVRIIDQSSNVEIASFPIY 197
Cdd:cd13158     4 DEDSLLQQLFIvrFLGSMEVKSDRTSEVIYEAMrqvlaARAIHNI---FRMTESHLLVTSDCLRLIDPQTQVTRARFPLA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1486857881 198 KVLFCARGHDGTtesNCFAFTESSHGSEEFQiHVFSCEIKEA 239
Cdd:cd13158    81 DVVQFAAHQENK---RLFGFVVRTPEGDGEE-PSFSCYVFES 118
 
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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