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Conserved domains on  [gi|568927520|ref|XP_006538385|]
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clavesin-1 isoform X4 [Mus musculus]

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

CATH:  1.20.5.1200|3.40.525.10|1.10.8.20
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 ...
 7-124 4.66e-37

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: 126.29  E-value: 4.66e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927520   7 DILRAILLSLEVLIEDPELQINGFILIIDWSNFSFKQASklTPSILKLAIEGLQDSFPARFGGVHFVNQPWYIHALYTLI 86
Cdd:cd00170   41 ELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLS--DLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIV 118

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568927520  87 KPFLKDKTRKRIFLHGNNLNSLHQLIHPEFLPSEFGGT 124
Cdd:cd00170  119 KPFLSEKTRKKIVFLGSDLEELLEYIDPDQLPKELGGT 156
 
Name Accession Description Interval E-value
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 7-124 4.66e-37

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: 126.29  E-value: 4.66e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927520   7 DILRAILLSLEVLIEDPELQINGFILIIDWSNFSFKQASklTPSILKLAIEGLQDSFPARFGGVHFVNQPWYIHALYTLI 86
Cdd:cd00170   41 ELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLS--DLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIV 118

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568927520  87 KPFLKDKTRKRIFLHGNNLNSLHQLIHPEFLPSEFGGT 124
Cdd:cd00170  119 KPFLSEKTRKKIVFLGSDLEELLEYIDPDQLPKELGGT 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
4-123 1.96e-31

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 111.58  E-value: 1.96e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927520    4 SFTDILRAILLSLEVLI-EDPELQINGFILIIDWSNFSFKQASKLTPSILKLAIEGLQDSFPARFGGVHFVNQPWYIHAL 82
Cdd:pfam00650  30 SEEELVRFLVLVLERALlLMPEGQVEGLTVIIDLKGLSLSNMDWWSISLLKKIIKILQDNYPERLGKILIVNAPWIFNTI 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568927520   83 YTLIKPFLKDKTRKRIFLHGN-NLNSLHQLIHPEFLPSEFGG 123
Cdd:pfam00650 110 WKLIKPFLDPKTREKIVFLKNsNEEELEKYIPPEQLPKEYGG 151
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 2-126 4.78e-30

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: 108.54  E-value: 4.78e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927520     2 MNSFT--DILRAILLSLE--VLIEDPELQINGFILIIDWSNFSFkqaSKLTPSILKLAIEGLQDSFPARFGGVHFVNQPW 77
Cdd:smart00516  32 LKSVTleELLRYLVYVLEkiLQEEKKTGGIEGFTVIFDLKGLSM---SNPDLSVLRKILKILQDHYPERLGKVYIINPPW 108

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 568927520    78 YIHALYTLIKPFLKDKTRKRIFLHGNN-LNSLHQLIHPEFLPSEFGGTLP 126
Cdd:smart00516 109 FFRVLWKIIKPFLDEKTREKIRFVGNDsKEELLEYIDKEQLPEELGGTLD 158
 
Name Accession Description Interval E-value
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 7-124 4.66e-37

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: 126.29  E-value: 4.66e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927520   7 DILRAILLSLEVLIEDPELQINGFILIIDWSNFSFKQASklTPSILKLAIEGLQDSFPARFGGVHFVNQPWYIHALYTLI 86
Cdd:cd00170   41 ELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLS--DLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIV 118

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568927520  87 KPFLKDKTRKRIFLHGNNLNSLHQLIHPEFLPSEFGGT 124
Cdd:cd00170  119 KPFLSEKTRKKIVFLGSDLEELLEYIDPDQLPKELGGT 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
4-123 1.96e-31

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 111.58  E-value: 1.96e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927520    4 SFTDILRAILLSLEVLI-EDPELQINGFILIIDWSNFSFKQASKLTPSILKLAIEGLQDSFPARFGGVHFVNQPWYIHAL 82
Cdd:pfam00650  30 SEEELVRFLVLVLERALlLMPEGQVEGLTVIIDLKGLSLSNMDWWSISLLKKIIKILQDNYPERLGKILIVNAPWIFNTI 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568927520   83 YTLIKPFLKDKTRKRIFLHGN-NLNSLHQLIHPEFLPSEFGG 123
Cdd:pfam00650 110 WKLIKPFLDPKTREKIVFLKNsNEEELEKYIPPEQLPKEYGG 151
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 2-126 4.78e-30

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: 108.54  E-value: 4.78e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927520     2 MNSFT--DILRAILLSLE--VLIEDPELQINGFILIIDWSNFSFkqaSKLTPSILKLAIEGLQDSFPARFGGVHFVNQPW 77
Cdd:smart00516  32 LKSVTleELLRYLVYVLEkiLQEEKKTGGIEGFTVIFDLKGLSM---SNPDLSVLRKILKILQDHYPERLGKVYIINPPW 108

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 568927520    78 YIHALYTLIKPFLKDKTRKRIFLHGNN-LNSLHQLIHPEFLPSEFGGTLP 126
Cdd:smart00516 109 FFRVLWKIIKPFLDEKTREKIRFVGNDsKEELLEYIDKEQLPEELGGTLD 158
 
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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