NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|79321295|ref|NP_001031284|]
View 

Sec14p-like phosphatidylinositol transfer family protein [Arabidopsis thaliana]

Protein Classification

SEC14 family lipid-binding protein( domain architecture ID 10074233)

SEC14 family lipid-binding protein contains a lipid-binding domain that is found in secretory proteins and in lipid regulated proteins; similar to Drosophila melanogaster retinol-binding protein pinta, a retinoid-binding protein which shows highest affinity for all-trans retinol

Gene Ontology:  GO:1902936|GO:0008289
PubMed:  12767229|17428729
SCOP:  4003560

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
7-158 7.03e-44

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: 144.01  E-value: 7.03e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79321295   7 ETGKVYKAGFHDRHGRTVLILRPGLQNTK--SLENQMKHLVYLIENAILNLPEDQEQMSWLIDFTGWSMSTSVPIKSARE 84
Cdd:cd00170   7 LLGGIGYLGGRDKEGRPVLVFRAGWDPPKllDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLSDLSLLKK 86
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79321295  85 TINILQNHYPERLAVAFLYNPPRLFEAFWKIVKYFIDAKTFVKVKFVypknSESVELMSTFFDEENLPTEFGGK 158
Cdd:cd00170  87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFL----GSDLEELLEYIDPDQLPKELGGT 156
 
Name Accession Description Interval E-value
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
7-158 7.03e-44

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: 144.01  E-value: 7.03e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79321295   7 ETGKVYKAGFHDRHGRTVLILRPGLQNTK--SLENQMKHLVYLIENAILNLPEDQEQMSWLIDFTGWSMSTSVPIKSARE 84
Cdd:cd00170   7 LLGGIGYLGGRDKEGRPVLVFRAGWDPPKllDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLSDLSLLKK 86
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79321295  85 TINILQNHYPERLAVAFLYNPPRLFEAFWKIVKYFIDAKTFVKVKFVypknSESVELMSTFFDEENLPTEFGGK 158
Cdd:cd00170  87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFL----GSDLEELLEYIDPDQLPKELGGT 156
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
5-158 1.44e-43

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: 143.21  E-value: 1.44e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79321295      5 EGETGKVYKAGF--HDRHGRTVLILRPGLQ--NTKSLENQMKHLVYLIENAILNLPED--QEQMSWLIDFTGWSMStSVP 78
Cdd:smart00516   1 ELELLKAYIPGGrgYDKDGRPVLIERAGRFdlKSVTLEELLRYLVYVLEKILQEEKKTggIEGFTVIFDLKGLSMS-NPD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79321295     79 IKSARETINILQNHYPERLAVAFLYNPPRLFEAFWKIVKYFIDAKTFVKVKFVYPKnseSVELMSTFFDEENLPTEFGGK 158
Cdd:smart00516  80 LSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGND---SKEELLEYIDKEQLPEELGGT 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
8-157 8.42e-41

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 135.85  E-value: 8.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79321295     8 TGKVYKAGFhDRHGRTVLILRPGLQNTK--SLENQMKHLVYLIENAILNLPEDQ-EQMSWLIDFTGWSMS--TSVPIKSA 82
Cdd:pfam00650   1 GGKVYLHGR-DKEGRPVLYLRLGRHDPKksSEEELVRFLVLVLERALLLMPEGQvEGLTVIIDLKGLSLSnmDWWSISLL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79321295    83 RETINILQNHYPERLAVAFLYNPPRLFEAFWKIVKYFIDAKTFVKVKFVYPKNSESvelMSTFFDEENLPTEFGG 157
Cdd:pfam00650  80 KKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKNSNEEE---LEKYIPPEQLPKEYGG 151
 
Name Accession Description Interval E-value
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
7-158 7.03e-44

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: 144.01  E-value: 7.03e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79321295   7 ETGKVYKAGFHDRHGRTVLILRPGLQNTK--SLENQMKHLVYLIENAILNLPEDQEQMSWLIDFTGWSMSTSVPIKSARE 84
Cdd:cd00170   7 LLGGIGYLGGRDKEGRPVLVFRAGWDPPKllDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLSDLSLLKK 86
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79321295  85 TINILQNHYPERLAVAFLYNPPRLFEAFWKIVKYFIDAKTFVKVKFVypknSESVELMSTFFDEENLPTEFGGK 158
Cdd:cd00170  87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFL----GSDLEELLEYIDPDQLPKELGGT 156
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
5-158 1.44e-43

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: 143.21  E-value: 1.44e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79321295      5 EGETGKVYKAGF--HDRHGRTVLILRPGLQ--NTKSLENQMKHLVYLIENAILNLPED--QEQMSWLIDFTGWSMStSVP 78
Cdd:smart00516   1 ELELLKAYIPGGrgYDKDGRPVLIERAGRFdlKSVTLEELLRYLVYVLEKILQEEKKTggIEGFTVIFDLKGLSMS-NPD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79321295     79 IKSARETINILQNHYPERLAVAFLYNPPRLFEAFWKIVKYFIDAKTFVKVKFVYPKnseSVELMSTFFDEENLPTEFGGK 158
Cdd:smart00516  80 LSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGND---SKEELLEYIDKEQLPEELGGT 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
8-157 8.42e-41

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 135.85  E-value: 8.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79321295     8 TGKVYKAGFhDRHGRTVLILRPGLQNTK--SLENQMKHLVYLIENAILNLPEDQ-EQMSWLIDFTGWSMS--TSVPIKSA 82
Cdd:pfam00650   1 GGKVYLHGR-DKEGRPVLYLRLGRHDPKksSEEELVRFLVLVLERALLLMPEGQvEGLTVIIDLKGLSLSnmDWWSISLL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79321295    83 RETINILQNHYPERLAVAFLYNPPRLFEAFWKIVKYFIDAKTFVKVKFVYPKNSESvelMSTFFDEENLPTEFGG 157
Cdd:pfam00650  80 KKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKNSNEEE---LEKYIPPEQLPKEYGG 151
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
21-166 2.12e-07

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: 48.48  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79321295    21 GRTVLIL--RPGLQNTKSLENQMKHLVYLIEnaILNLPEDQEQMSWLIDFTGWSMSTSVPIKSARETINILQNHYPERLA 98
Cdd:pfam13716   1 GRPVLVFisKLLPSRPASLDDLDRLLFYLLK--TLSEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLK 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79321295    99 VAFLYNPPRLFEAFWKIVKYFIDAKTFVKvKFVYpknSESVELMSTFFDEENLPTEFGGKalLQYNYE 166
Cdd:pfam13716  79 AVYVVHPSTFLRTFLKTLGSLLGSKKLRK-KVHY---VSSLSELWEGIDREQLPTELPGV--LSYDEE 140
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH