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Conserved domains on  [gi|321400094|ref|NP_956025|]
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alpha-tocopherol transfer protein [Danio rerio]

Protein Classification

CRAL-TRIO domain-containing protein( domain architecture ID 10661233)

CRAL-TRIO domain-containing protein act as a lipid binding protein which may bind small lipophilic molecules such as retinal, inositol, and vitamin E

CATH:  3.40.525.10
Gene Ontology:  GO:1902936|GO:0008289
PubMed:  12767229|17428729

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CRAL_TRIO pfam00650
CRAL/TRIO domain;
96-245 9.59e-34

CRAL/TRIO domain;


:

Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 120.05  E-value: 9.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400094   96 NYHGVLRSRDDAGSRVLIYRIGKWNPKEFTAYEVFRVSLITSELIVQEW-ETQRNGLKAIFDLQDWCFAHALQINPSLAK 174
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALLLMpEGQVEGLTVIIDLKGLSLSNMDWWSISLLK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 321400094  175 KISSVLTDSFPLKVRGIHLINEPIFFRPVFAMIRPFLPDKIKQRIHMHGCSYARSLCNYFPKAVLPPVYGG 245
Cdd:pfam00650  81 KIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKNSNEEELEKYIPPEQLPKEYGG 151
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
26-70 3.39e-08

CRAL/TRIO, N-terminal domain;


:

Pssm-ID: 215024  Cd Length: 48  Bit Score: 48.70  E-value: 3.39e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 321400094    26 LSELKEKAEAELRIRDLDLSKTFLIRFLQARDFDVALALKLLINY 70
Cdd:smart01100   4 LEELRELLEKHPDLLPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
 
Name Accession Description Interval E-value
CRAL_TRIO pfam00650
CRAL/TRIO domain;
96-245 9.59e-34

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 120.05  E-value: 9.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400094   96 NYHGVLRSRDDAGSRVLIYRIGKWNPKEFTAYEVFRVSLITSELIVQEW-ETQRNGLKAIFDLQDWCFAHALQINPSLAK 174
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALLLMpEGQVEGLTVIIDLKGLSLSNMDWWSISLLK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 321400094  175 KISSVLTDSFPLKVRGIHLINEPIFFRPVFAMIRPFLPDKIKQRIHMHGCSYARSLCNYFPKAVLPPVYGG 245
Cdd:pfam00650  81 KIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKNSNEEELEKYIPPEQLPKEYGG 151
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
96-246 7.64e-33

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are 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: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 118.21  E-value: 7.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400094  96 NYHGVLRSRDDAGSRVLIYRIGKWNPKEFTAYEVFRVSLITSELIVQEWETQRNGLKAIFDLQDWCFAHALqiNPSLAKK 175
Cdd:cd00170    9 GGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLS--DLSLLKK 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 321400094 176 ISSVLTDSFPLKVRGIHLINEPIFFRPVFAMIRPFLPDKIKQRIHMHGCSYArSLCNYFPKAVLPPVYGGT 246
Cdd:cd00170   87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSDLE-ELLEYIDPDQLPKELGGT 156
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
102-248 1.39e-28

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 [Multi-domain]  Cd Length: 158  Bit Score: 107.00  E-value: 1.39e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400094   102 RSRDDAGSRVLIYRIGKWNPKEFTAYEVFRVSLITSELIVQEW--ETQRNGLKAIFDLQDWCFAHALqinPSLAKKISSV 179
Cdd:smart00516  13 RGYDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILQEEkkTGGIEGFTVIFDLKGLSMSNPD---LSVLRKILKI 89
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 321400094   180 LTDSFPLKVRGIHLINEPIFFRPVFAMIRPFLPDKIKQRIHMHGCSYARSLCNYFPKAVLPPVYGGTGP 248
Cdd:smart00516  90 LQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKEQLPEELGGTLD 158
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
26-70 3.39e-08

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 48.70  E-value: 3.39e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 321400094    26 LSELKEKAEAELRIRDLDLSKTFLIRFLQARDFDVALALKLLINY 70
Cdd:smart01100   4 LEELRELLEKHPDLLPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
CRAL_TRIO_N pfam03765
CRAL/TRIO, N-terminal domain; This all-alpha domain is found to the N-terminus of pfam00650.
25-69 6.84e-05

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


Pssm-ID: 461043  Cd Length: 53  Bit Score: 39.56  E-value: 6.84e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 321400094   25 YLSELKEKAEAE-LRIRDLDLSKTFLIRFLQARDFDVALALKLLIN 69
Cdd:pfam03765   8 LLKDEDEETDREkFWLTREDHDDVCLLRFLRARKWDVEKAIKMLED 53
 
Name Accession Description Interval E-value
CRAL_TRIO pfam00650
CRAL/TRIO domain;
96-245 9.59e-34

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 120.05  E-value: 9.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400094   96 NYHGVLRSRDDAGSRVLIYRIGKWNPKEFTAYEVFRVSLITSELIVQEW-ETQRNGLKAIFDLQDWCFAHALQINPSLAK 174
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALLLMpEGQVEGLTVIIDLKGLSLSNMDWWSISLLK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 321400094  175 KISSVLTDSFPLKVRGIHLINEPIFFRPVFAMIRPFLPDKIKQRIHMHGCSYARSLCNYFPKAVLPPVYGG 245
Cdd:pfam00650  81 KIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKNSNEEELEKYIPPEQLPKEYGG 151
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
96-246 7.64e-33

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are 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: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 118.21  E-value: 7.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400094  96 NYHGVLRSRDDAGSRVLIYRIGKWNPKEFTAYEVFRVSLITSELIVQEWETQRNGLKAIFDLQDWCFAHALqiNPSLAKK 175
Cdd:cd00170    9 GGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLS--DLSLLKK 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 321400094 176 ISSVLTDSFPLKVRGIHLINEPIFFRPVFAMIRPFLPDKIKQRIHMHGCSYArSLCNYFPKAVLPPVYGGT 246
Cdd:cd00170   87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSDLE-ELLEYIDPDQLPKELGGT 156
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
102-248 1.39e-28

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 [Multi-domain]  Cd Length: 158  Bit Score: 107.00  E-value: 1.39e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400094   102 RSRDDAGSRVLIYRIGKWNPKEFTAYEVFRVSLITSELIVQEW--ETQRNGLKAIFDLQDWCFAHALqinPSLAKKISSV 179
Cdd:smart00516  13 RGYDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILQEEkkTGGIEGFTVIFDLKGLSMSNPD---LSVLRKILKI 89
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 321400094   180 LTDSFPLKVRGIHLINEPIFFRPVFAMIRPFLPDKIKQRIHMHGCSYARSLCNYFPKAVLPPVYGGTGP 248
Cdd:smart00516  90 LQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKEQLPEELGGTLD 158
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
26-70 3.39e-08

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 48.70  E-value: 3.39e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 321400094    26 LSELKEKAEAELRIRDLDLSKTFLIRFLQARDFDVALALKLLINY 70
Cdd:smart01100   4 LEELRELLEKHPDLLPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
CRAL_TRIO_N pfam03765
CRAL/TRIO, N-terminal domain; This all-alpha domain is found to the N-terminus of pfam00650.
25-69 6.84e-05

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


Pssm-ID: 461043  Cd Length: 53  Bit Score: 39.56  E-value: 6.84e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 321400094   25 YLSELKEKAEAE-LRIRDLDLSKTFLIRFLQARDFDVALALKLLIN 69
Cdd:pfam03765   8 LLKDEDEETDREkFWLTREDHDDVCLLRFLRARKWDVEKAIKMLED 53
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
169-246 5.79e-03

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 36.54  E-value: 5.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400094  169 NPSLA--KKISSVLTDSFPLKVRGIHLINEPIFFRPVFAMI-RPFLPDKIKQRIHMhgCSYARSLCNYFPKAVLPPVYGG 245
Cdd:pfam13716  56 FPSLSflKKAYDLLPRAFKKNLKAVYVVHPSTFLRTFLKTLgSLLGSKKLRKKVHY--VSSLSELWEGIDREQLPTELPG 133

                  .
gi 321400094  246 T 246
Cdd:pfam13716 134 V 134
 
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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