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Conserved domains on  [gi|1370514164|ref|XP_024303244|]
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rab GTPase-activating protein 1 isoform X6 [Homo sapiens]

Protein Classification

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 ...
 145-273 2.03e-83

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: 256.79  E-value: 2.03e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514164 145 VVFSKLTYLGCASVNAPRSEVEALRMMSILRSQCQISLDVTLSVPNVSEGIVRLLDPQTNTEIANYPIYKILFCVRGHDG 224
Cdd:cd01211     1 TIFNGVTYLGCAKVNAPRSETEALRIMAILREQSAQPIKVTLSVPNSSEGSVRLYDPTSNTEIASYPIYRILFCARGPDG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1370514164 225 TPESDCFAFTESHYNAELFRIHVFRCEIQEAVSRILYSFATAFRRSAKQ 273
Cdd:cd01211    81 TSESDCFAFTWSHGETAIFQCHVFRCEIPEAVSKVLYSFAKAFRRVPKS 129
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 307-437 5.57e-35

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: 129.24  E-value: 5.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514164 307 FSAVPKDK----DRQCFKLRQGIDKKIVIYVQQTTNKELAIERCfglllspgKDVRNSDMHLLDleSMGKSSDGKS---- 378
Cdd:pfam12473   2 YVPVPVDQrselDPGTFQLHQGLQRRIVITLTHSSGDELPWERV--------RNVRVGDVRLLD--MKGRVPDSDStpdv 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370514164 379 -------------------YVITGSWNPKSPHFQVVNEETPKDKVLFMTTAVDLVITEVQEPVRFLLETKVRVCSPNE 437
Cdd:pfam12473  72 slkllskpvvrfnadgtssYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEKCAEPVRFSMDTAVQIYPRDE 149
TBC super family cl47029
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 563-597 7.08e-03

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.


The actual alignment was detected with superfamily member smart00164:

Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 38.44  E-value: 7.08e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1370514164  563 VRNGVPEALRGEVWQLLAGCHNNDH--LVEKYRILIT 597
Cdd:smart00164   1 VRKGVPPSLRGVVWKLLLNAQPMDTsaDKDLYSRLLK 37
 
Name Accession Description Interval E-value
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 145-273 2.03e-83

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: 256.79  E-value: 2.03e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514164 145 VVFSKLTYLGCASVNAPRSEVEALRMMSILRSQCQISLDVTLSVPNVSEGIVRLLDPQTNTEIANYPIYKILFCVRGHDG 224
Cdd:cd01211     1 TIFNGVTYLGCAKVNAPRSETEALRIMAILREQSAQPIKVTLSVPNSSEGSVRLYDPTSNTEIASYPIYRILFCARGPDG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1370514164 225 TPESDCFAFTESHYNAELFRIHVFRCEIQEAVSRILYSFATAFRRSAKQ 273
Cdd:cd01211    81 TSESDCFAFTWSHGETAIFQCHVFRCEIPEAVSKVLYSFAKAFRRVPKS 129
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 307-437 5.57e-35

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: 129.24  E-value: 5.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514164 307 FSAVPKDK----DRQCFKLRQGIDKKIVIYVQQTTNKELAIERCfglllspgKDVRNSDMHLLDleSMGKSSDGKS---- 378
Cdd:pfam12473   2 YVPVPVDQrselDPGTFQLHQGLQRRIVITLTHSSGDELPWERV--------RNVRVGDVRLLD--MKGRVPDSDStpdv 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370514164 379 -------------------YVITGSWNPKSPHFQVVNEETPKDKVLFMTTAVDLVITEVQEPVRFLLETKVRVCSPNE 437
Cdd:pfam12473  72 slkllskpvvrfnadgtssYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEKCAEPVRFSMDTAVQIYPRDE 149
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 143-276 3.87e-29

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: 112.41  E-value: 3.87e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514164  143 DSVVFSKLTYLGCASVNAPRSEVEALR-MMSILRSQCQISLDVTLSVPNVSEGIVRLLDPQTNTEIANYPIYKILFCVRG 221
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEaIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370514164  222 HDGtpeSDCFAFTESHYNAELFRIHVFRCEI--QEAVSRILYSFATAFRRSAKQTPL 276
Cdd:smart00462  81 PDD---LDVFGYIARDPGSSRFACHVFRCEKaaEDIALAIGQAFQLAYELKLKARSE 134
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
152-267 5.75e-06

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 46.20  E-value: 5.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514164 152 YLGCASVNAPRSEVEALRMM----SILR-SQCQISLDVTLSVP---------NVSEGIVRLLDPQTNTEIANYPIYKILF 217
Cdd:pfam00640   5 YLGSVEVPEERAPDKNTRMQqareAIRRvKAAKINKIRGLSGEtgpgtkvdlFISTDGLKLLNPDTQELIHDHPLVSISF 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370514164 218 CVRGHDGTpeSDCFAFTESHYNAELFRIHVFRCEiqEAVSRILYSFATAF 267
Cdd:pfam00640  85 CADGDPDL--MRYFAYIARDKATNKFACHVFESE--DGAQDIAQSIGQAF 130
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 563-597 7.08e-03

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: 38.44  E-value: 7.08e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1370514164  563 VRNGVPEALRGEVWQLLAGCHNNDH--LVEKYRILIT 597
Cdd:smart00164   1 VRKGVPPSLRGVVWKLLLNAQPMDTsaDKDLYSRLLK 37
 
Name Accession Description Interval E-value
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 145-273 2.03e-83

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: 256.79  E-value: 2.03e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514164 145 VVFSKLTYLGCASVNAPRSEVEALRMMSILRSQCQISLDVTLSVPNVSEGIVRLLDPQTNTEIANYPIYKILFCVRGHDG 224
Cdd:cd01211     1 TIFNGVTYLGCAKVNAPRSETEALRIMAILREQSAQPIKVTLSVPNSSEGSVRLYDPTSNTEIASYPIYRILFCARGPDG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1370514164 225 TPESDCFAFTESHYNAELFRIHVFRCEIQEAVSRILYSFATAFRRSAKQ 273
Cdd:cd01211    81 TSESDCFAFTWSHGETAIFQCHVFRCEIPEAVSKVLYSFAKAFRRVPKS 129
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 307-437 5.57e-35

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: 129.24  E-value: 5.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514164 307 FSAVPKDK----DRQCFKLRQGIDKKIVIYVQQTTNKELAIERCfglllspgKDVRNSDMHLLDleSMGKSSDGKS---- 378
Cdd:pfam12473   2 YVPVPVDQrselDPGTFQLHQGLQRRIVITLTHSSGDELPWERV--------RNVRVGDVRLLD--MKGRVPDSDStpdv 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370514164 379 -------------------YVITGSWNPKSPHFQVVNEETPKDKVLFMTTAVDLVITEVQEPVRFLLETKVRVCSPNE 437
Cdd:pfam12473  72 slkllskpvvrfnadgtssYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEKCAEPVRFSMDTAVQIYPRDE 149
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 143-276 3.87e-29

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: 112.41  E-value: 3.87e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514164  143 DSVVFSKLTYLGCASVNAPRSEVEALR-MMSILRSQCQISLDVTLSVPNVSEGIVRLLDPQTNTEIANYPIYKILFCVRG 221
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEaIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370514164  222 HDGtpeSDCFAFTESHYNAELFRIHVFRCEI--QEAVSRILYSFATAFRRSAKQTPL 276
Cdd:smart00462  81 PDD---LDVFGYIARDPGSSRFACHVFRCEKaaEDIALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 149-267 3.05e-18

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


Pssm-ID: 269911  Cd Length: 120  Bit Score: 81.02  E-value: 3.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514164 149 KLTYLGCASVNAPR----SEVEALRMMSILRSQCQISLDVTLsvpNVSEGIVRLLDPQTNTEIANYPIYKILFCVRGHDg 224
Cdd:cd00934     4 QVKYLGSVEVGSSRgvdvVEEALKALAAALKSSKRKPGPVLL---EVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPD- 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1370514164 225 tpESDCFAFTESHYNAELFRIHVFRCEIQEAVSRILYSFATAF 267
Cdd:cd00934    80 --NPNVFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQAF 120
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
152-267 5.75e-06

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 46.20  E-value: 5.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514164 152 YLGCASVNAPRSEVEALRMM----SILR-SQCQISLDVTLSVP---------NVSEGIVRLLDPQTNTEIANYPIYKILF 217
Cdd:pfam00640   5 YLGSVEVPEERAPDKNTRMQqareAIRRvKAAKINKIRGLSGEtgpgtkvdlFISTDGLKLLNPDTQELIHDHPLVSISF 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370514164 218 CVRGHDGTpeSDCFAFTESHYNAELFRIHVFRCEiqEAVSRILYSFATAF 267
Cdd:pfam00640  85 CADGDPDL--MRYFAYIARDKATNKFACHVFESE--DGAQDIAQSIGQAF 130
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 143-250 1.61e-04

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: 41.55  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514164 143 DSVVFSkLTYLGCASVNAPRSE---VEALRmmSIL-------RSQCQISLDVTLsvpnvsEGIvRLLDPQTNTEIANYPI 212
Cdd:cd13159     1 DGVTFY-LKYLGSTLVEKPKGEgatAEAVK--TIIamakasgKKLQKVTLTVSP------KGI-KVTDSATNETILEVSI 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1370514164 213 YKILFCV--RGHDgtpesDCFAFTESHYNAELFRIHVFRC 250
Cdd:cd13159    71 YRISYCTadANHD-----KVFAFIATNQDNEKLECHAFLC 105
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 563-597 7.08e-03

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: 38.44  E-value: 7.08e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1370514164  563 VRNGVPEALRGEVWQLLAGCHNNDH--LVEKYRILIT 597
Cdd:smart00164   1 VRKGVPPSLRGVVWKLLLNAQPMDTsaDKDLYSRLLK 37
 
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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