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Conserved domains on  [gi|79546079|ref|NP_201111|]
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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

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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 ...
120-261 1.15e-26

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: 101.26  E-value: 1.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79546079 120 GKAYVHGFLDVKGRPVVIVAPAKHIPGLLDPIEDEKLCVFLLEKALSKLPAGQHKILGIFDLRGFG-SQNADLKFLTFLF 198
Cdd:cd00170   9 GGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSlSNLSDLSLLKKLL 88
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79546079 199 DVFYYYYPSRLDEVLFVDAPFIFQPIWQFTKPLVKQY-ASLVKFC-SAETVRKEYFTEETLPSNF 261
Cdd:cd00170  89 KILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKtRKKIVFLgSDLEELLEYIDPDQLPKEL 153
 
Name Accession Description Interval E-value
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
120-261 1.15e-26

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: 101.26  E-value: 1.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79546079 120 GKAYVHGFLDVKGRPVVIVAPAKHIPGLLDPIEDEKLCVFLLEKALSKLPAGQHKILGIFDLRGFG-SQNADLKFLTFLF 198
Cdd:cd00170   9 GGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSlSNLSDLSLLKKLL 88
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79546079 199 DVFYYYYPSRLDEVLFVDAPFIFQPIWQFTKPLVKQY-ASLVKFC-SAETVRKEYFTEETLPSNF 261
Cdd:cd00170  89 KILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKtRKKIVFLgSDLEELLEYIDPDQLPKEL 153
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
118-261 4.12e-23

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: 91.98  E-value: 4.12e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79546079    118 DTGKAYVHGFL--DVKGRPVVIVAPAKHIPGLLDPIEDEKLCVFLLEKALS--KLPAGQHKILGIFDLRGFGSQNADLKF 193
Cdd:smart00516   3 ELLKAYIPGGRgyDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILQeeKKTGGIEGFTVIFDLKGLSMSNPDLSV 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79546079    194 LTFLFDVFYYYYPSRLDEVLFVDAPFIFQPIWQFTKPLVK-QYASLVKFCSAETVRK--EYFTEETLPSNF 261
Cdd:smart00516  83 LRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDeKTREKIRFVGNDSKEEllEYIDKEQLPEEL 153
CRAL_TRIO pfam00650
CRAL/TRIO domain;
119-261 2.12e-20

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 84.62  E-value: 2.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79546079   119 TGKAYVHGFlDVKGRPVVIVAPAKHIPGLLDPIEDEKLCVFLLEKALSKLP-AGQHKILGIFDLRGFGSQNAD---LKFL 194
Cdd:pfam00650   1 GGKVYLHGR-DKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALLLMPeGQVEGLTVIIDLKGLSLSNMDwwsISLL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79546079   195 TFLFDVFYYYYPSRLDEVLFVDAPFIFQPIWQFTKPLVKQY-ASLVKFCSAETVR--KEYFTEETLPSNF 261
Cdd:pfam00650  80 KKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKtREKIVFLKNSNEEelEKYIPPEQLPKEY 149
 
Name Accession Description Interval E-value
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
120-261 1.15e-26

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: 101.26  E-value: 1.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79546079 120 GKAYVHGFLDVKGRPVVIVAPAKHIPGLLDPIEDEKLCVFLLEKALSKLPAGQHKILGIFDLRGFG-SQNADLKFLTFLF 198
Cdd:cd00170   9 GGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSlSNLSDLSLLKKLL 88
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79546079 199 DVFYYYYPSRLDEVLFVDAPFIFQPIWQFTKPLVKQY-ASLVKFC-SAETVRKEYFTEETLPSNF 261
Cdd:cd00170  89 KILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKtRKKIVFLgSDLEELLEYIDPDQLPKEL 153
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
118-261 4.12e-23

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: 91.98  E-value: 4.12e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79546079    118 DTGKAYVHGFL--DVKGRPVVIVAPAKHIPGLLDPIEDEKLCVFLLEKALS--KLPAGQHKILGIFDLRGFGSQNADLKF 193
Cdd:smart00516   3 ELLKAYIPGGRgyDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILQeeKKTGGIEGFTVIFDLKGLSMSNPDLSV 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79546079    194 LTFLFDVFYYYYPSRLDEVLFVDAPFIFQPIWQFTKPLVK-QYASLVKFCSAETVRK--EYFTEETLPSNF 261
Cdd:smart00516  83 LRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDeKTREKIRFVGNDSKEEllEYIDKEQLPEEL 153
CRAL_TRIO pfam00650
CRAL/TRIO domain;
119-261 2.12e-20

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 84.62  E-value: 2.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79546079   119 TGKAYVHGFlDVKGRPVVIVAPAKHIPGLLDPIEDEKLCVFLLEKALSKLP-AGQHKILGIFDLRGFGSQNAD---LKFL 194
Cdd:pfam00650   1 GGKVYLHGR-DKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALLLMPeGQVEGLTVIIDLKGLSLSNMDwwsISLL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79546079   195 TFLFDVFYYYYPSRLDEVLFVDAPFIFQPIWQFTKPLVKQY-ASLVKFCSAETVR--KEYFTEETLPSNF 261
Cdd:pfam00650  80 KKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKtREKIVFLKNSNEEelEKYIPPEQLPKEY 149
 
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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