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Conserved domains on  [gi|578815703|ref|XP_006716531.1|]
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alpha-tocopherol transfer protein isoform X1 [Homo sapiens]

Protein Classification

CRAL_TRIO_N and SEC14 domain-containing protein (domain architecture ID 10661233)

CRAL_TRIO_N and SEC14 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CRAL_TRIO pfam00650
CRAL/TRIO domain;
69-132 1.15e-17

CRAL/TRIO domain;


:

Pssm-ID: 306996  Cd Length: 152  Bit Score: 76.15  E-value: 1.15e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578815703   69 DSFPLKVRGIHLINEPVIFHAVFSMIKPFLTEKIKERIHMHGNNYKQSLLQHFP-DILPLEYGGE 132
Cdd:pfam00650  88 DNYPERLGKILIVNAPWIFNVIWKLIKPFLDPKTREKIKFHKSSNLEELKKHIPpEQLPKEYGGT 152
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
40-67 1.73e-06

CRAL/TRIO, N-terminal domain;


:

Pssm-ID: 215024  Cd Length: 48  Bit Score: 42.92  E-value: 1.73e-06
                           10        20
                   ....*....|....*....|....*...
gi 578815703    40 VPLAPLPLTDSFLLRFLRARDFDLDLAW 67
Cdd:smart01100  15 PDLLPPRLDDAFLLRFLRARKFDVEKAK 42
 
Name Accession Description Interval E-value
CRAL_TRIO pfam00650
CRAL/TRIO domain;
69-132 1.15e-17

CRAL/TRIO domain;


Pssm-ID: 306996  Cd Length: 152  Bit Score: 76.15  E-value: 1.15e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578815703   69 DSFPLKVRGIHLINEPVIFHAVFSMIKPFLTEKIKERIHMHGNNYKQSLLQHFP-DILPLEYGGE 132
Cdd:pfam00650  88 DNYPERLGKILIVNAPWIFNVIWKLIKPFLDPKTREKIKFHKSSNLEELKKHIPpEQLPKEYGGT 152
SEC14 cd00170
Sec14p-like lipid-binding domain. Found in secretory proteins, such as S. cerevisiae ...
39-132 9.31e-17

Sec14p-like lipid-binding domain. Found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 238099  Cd Length: 157  Bit Score: 73.96  E-value: 9.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815703  39 GVPLAPLPLTDSFLLRFLRARDfdldlawrDSFPLKVRGIHLINEPVIFHAVFSMIKPFLTEKIKERIHMHGNNyKQSLL 118
Cdd:cd00170   72 GLSLSHLLPDPSLLKKILKILQ--------DNYPERLKAVYIINPPWFFKVLWKIVKPFLSEKTRKKIVFLGSD-KEELL 142
                         90
                 ....*....|....*
gi 578815703 119 QHFP-DILPLEYGGE 132
Cdd:cd00170  143 KYIDkEQLPEEYGGT 157
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
69-132 2.20e-16

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706  Cd Length: 158  Bit Score: 72.72  E-value: 2.20e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578815703    69 DSFPLKVRGIHLINEPVIFHAVFSMIKPFLTEKIKERIHMHGNNYKQSLLQHF-PDILPLEYGGE 132
Cdd:smart00516  92 DHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIdKEQLPEELGGT 156
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
40-67 1.73e-06

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 42.92  E-value: 1.73e-06
                           10        20
                   ....*....|....*....|....*...
gi 578815703    40 VPLAPLPLTDSFLLRFLRARDFDLDLAW 67
Cdd:smart01100  15 PDLLPPRLDDAFLLRFLRARKFDVEKAK 42
CRAL_TRIO_N pfam03765
CRAL/TRIO, N-terminal domain; This all-alpha domain is found to the N-terminus of pfam00650.
49-67 2.02e-04

CRAL/TRIO, N-terminal domain; This all-alpha domain is found to the N-terminus of pfam00650.


Pssm-ID: 309041  Cd Length: 52  Bit Score: 37.54  E-value: 2.02e-04
                          10
                  ....*....|....*....
gi 578815703   49 DSFLLRFLRARDFDLDLAW 67
Cdd:pfam03765  30 DACLLRFLRARKWDVEKAI 48
 
Name Accession Description Interval E-value
CRAL_TRIO pfam00650
CRAL/TRIO domain;
69-132 1.15e-17

CRAL/TRIO domain;


Pssm-ID: 306996  Cd Length: 152  Bit Score: 76.15  E-value: 1.15e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578815703   69 DSFPLKVRGIHLINEPVIFHAVFSMIKPFLTEKIKERIHMHGNNYKQSLLQHFP-DILPLEYGGE 132
Cdd:pfam00650  88 DNYPERLGKILIVNAPWIFNVIWKLIKPFLDPKTREKIKFHKSSNLEELKKHIPpEQLPKEYGGT 152
SEC14 cd00170
Sec14p-like lipid-binding domain. Found in secretory proteins, such as S. cerevisiae ...
39-132 9.31e-17

Sec14p-like lipid-binding domain. Found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 238099  Cd Length: 157  Bit Score: 73.96  E-value: 9.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815703  39 GVPLAPLPLTDSFLLRFLRARDfdldlawrDSFPLKVRGIHLINEPVIFHAVFSMIKPFLTEKIKERIHMHGNNyKQSLL 118
Cdd:cd00170   72 GLSLSHLLPDPSLLKKILKILQ--------DNYPERLKAVYIINPPWFFKVLWKIVKPFLSEKTRKKIVFLGSD-KEELL 142
                         90
                 ....*....|....*
gi 578815703 119 QHFP-DILPLEYGGE 132
Cdd:cd00170  143 KYIDkEQLPEEYGGT 157
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
69-132 2.20e-16

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706  Cd Length: 158  Bit Score: 72.72  E-value: 2.20e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578815703    69 DSFPLKVRGIHLINEPVIFHAVFSMIKPFLTEKIKERIHMHGNNYKQSLLQHF-PDILPLEYGGE 132
Cdd:smart00516  92 DHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIdKEQLPEELGGT 156
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
40-67 1.73e-06

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 42.92  E-value: 1.73e-06
                           10        20
                   ....*....|....*....|....*...
gi 578815703    40 VPLAPLPLTDSFLLRFLRARDFDLDLAW 67
Cdd:smart01100  15 PDLLPPRLDDAFLLRFLRARKFDVEKAK 42
CRAL_TRIO_N pfam03765
CRAL/TRIO, N-terminal domain; This all-alpha domain is found to the N-terminus of pfam00650.
49-67 2.02e-04

CRAL/TRIO, N-terminal domain; This all-alpha domain is found to the N-terminus of pfam00650.


Pssm-ID: 309041  Cd Length: 52  Bit Score: 37.54  E-value: 2.02e-04
                          10
                  ....*....|....*....
gi 578815703   49 DSFLLRFLRARDFDLDLAW 67
Cdd:pfam03765  30 DACLLRFLRARKWDVEKAI 48
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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