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Conserved domains on  [gi|28574921|ref|NP_648579|]
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uncharacterized protein Dmel_CG10657 [Drosophila melanogaster]

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

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
CRAL_TRIO pfam00650
CRAL/TRIO domain;
126-273 6.58e-29

CRAL/TRIO domain;


:

Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 108.88  E-value: 6.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574921   126 GYLVPLPQRDSTGRQVIFSVAAKFDPYKFTSVQMARVHSLVCEALLDDEDS-QVAGYVYINDESGMNMGFVSLWSLTDLR 204
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALLLMPEgQVEGLTVIIDLKGLSLSNMDWWSISLLK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574921   205 SIVKCIQNSTPMRHKETHFVNIPHYANRIIELGVSMLSDKLKKRIIVHKNVDI--LKTKIDPAILPKEYGG 273
Cdd:pfam00650  81 KIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKNSNEeeLEKYIPPEQLPKEYGG 151
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
52-98 1.74e-18

CRAL/TRIO, N-terminal domain;


:

Pssm-ID: 215024  Cd Length: 48  Bit Score: 77.59  E-value: 1.74e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 28574921     52 QALAQFREWIEKHPHIRKCRTDTVFLLRFLRTKKFSVPSACEMLERY 98
Cdd:smart01100   2 EALEELRELLEKHPDLLPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
 
Name Accession Description Interval E-value
CRAL_TRIO pfam00650
CRAL/TRIO domain;
126-273 6.58e-29

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 108.88  E-value: 6.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574921   126 GYLVPLPQRDSTGRQVIFSVAAKFDPYKFTSVQMARVHSLVCEALLDDEDS-QVAGYVYINDESGMNMGFVSLWSLTDLR 204
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALLLMPEgQVEGLTVIIDLKGLSLSNMDWWSISLLK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574921   205 SIVKCIQNSTPMRHKETHFVNIPHYANRIIELGVSMLSDKLKKRIIVHKNVDI--LKTKIDPAILPKEYGG 273
Cdd:pfam00650  81 KIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKNSNEeeLEKYIPPEQLPKEYGG 151
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
119-274 6.88e-22

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: 90.09  E-value: 6.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574921 119 INEIFEN-GYLVPLPQRDSTGRQVIFSVAAKFDPYKFTSVQMARVHSLVCEALLDDEDSQVAGYVYINDESGMNMGfvSL 197
Cdd:cd00170   1 LEELLELlGGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLS--NL 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574921 198 WSLTDLRSIVKCIQNSTPMRHKETHFVNIPHYANRIIELGVSMLSDKLKKRIIVHK-NVDILKTKIDPAILPKEYGGT 274
Cdd:cd00170  79 SDLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsDLEELLEYIDPDQLPKELGGT 156
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
52-98 1.74e-18

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 77.59  E-value: 1.74e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 28574921     52 QALAQFREWIEKHPHIRKCRTDTVFLLRFLRTKKFSVPSACEMLERY 98
Cdd:smart01100   2 EALEELRELLEKHPDLLPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
135-276 2.32e-11

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: 61.16  E-value: 2.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574921    135 DSTGRQVIFSVAAKFDPYKFTSVQMARVHSLVCE--ALLDDEDSQVAGYVYINDESGMNMgfvSLWSLTDLRSIVKCIQN 212
Cdd:smart00516  16 DKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEkiLQEEKKTGGIEGFTVIFDLKGLSM---SNPDLSVLRKILKILQD 92
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574921    213 STPMRHKETHFVNIPHYANRIIELGVSMLSDKLKKRIIVHKNVDI--LKTKIDPAILPKEYGGTVP 276
Cdd:smart00516  93 HYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSKeeLLEYIDKEQLPEELGGTLD 158
CRAL_TRIO_N pfam03765
CRAL/TRIO, N-terminal domain; This all-alpha domain is found to the N-terminus of pfam00650.
54-96 6.20e-04

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: 37.25  E-value: 6.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 28574921    54 LAQFREWIEKHPHIR----KCRTDTVFLLRFLRTKKFSVPSACEMLE 96
Cdd:pfam03765   6 LELLKDEDEETDREKfwltREDHDDVCLLRFLRARKWDVEKAIKMLE 52
 
Name Accession Description Interval E-value
CRAL_TRIO pfam00650
CRAL/TRIO domain;
126-273 6.58e-29

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 108.88  E-value: 6.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574921   126 GYLVPLPQRDSTGRQVIFSVAAKFDPYKFTSVQMARVHSLVCEALLDDEDS-QVAGYVYINDESGMNMGFVSLWSLTDLR 204
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALLLMPEgQVEGLTVIIDLKGLSLSNMDWWSISLLK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574921   205 SIVKCIQNSTPMRHKETHFVNIPHYANRIIELGVSMLSDKLKKRIIVHKNVDI--LKTKIDPAILPKEYGG 273
Cdd:pfam00650  81 KIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKNSNEeeLEKYIPPEQLPKEYGG 151
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
119-274 6.88e-22

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: 90.09  E-value: 6.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574921 119 INEIFEN-GYLVPLPQRDSTGRQVIFSVAAKFDPYKFTSVQMARVHSLVCEALLDDEDSQVAGYVYINDESGMNMGfvSL 197
Cdd:cd00170   1 LEELLELlGGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLS--NL 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574921 198 WSLTDLRSIVKCIQNSTPMRHKETHFVNIPHYANRIIELGVSMLSDKLKKRIIVHK-NVDILKTKIDPAILPKEYGGT 274
Cdd:cd00170  79 SDLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsDLEELLEYIDPDQLPKELGGT 156
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
52-98 1.74e-18

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 77.59  E-value: 1.74e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 28574921     52 QALAQFREWIEKHPHIRKCRTDTVFLLRFLRTKKFSVPSACEMLERY 98
Cdd:smart01100   2 EALEELRELLEKHPDLLPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
135-276 2.32e-11

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: 61.16  E-value: 2.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574921    135 DSTGRQVIFSVAAKFDPYKFTSVQMARVHSLVCE--ALLDDEDSQVAGYVYINDESGMNMgfvSLWSLTDLRSIVKCIQN 212
Cdd:smart00516  16 DKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEkiLQEEKKTGGIEGFTVIFDLKGLSM---SNPDLSVLRKILKILQD 92
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574921    213 STPMRHKETHFVNIPHYANRIIELGVSMLSDKLKKRIIVHKNVDI--LKTKIDPAILPKEYGGTVP 276
Cdd:smart00516  93 HYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSKeeLLEYIDKEQLPEELGGTLD 158
CRAL_TRIO_N pfam03765
CRAL/TRIO, N-terminal domain; This all-alpha domain is found to the N-terminus of pfam00650.
54-96 6.20e-04

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: 37.25  E-value: 6.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 28574921    54 LAQFREWIEKHPHIR----KCRTDTVFLLRFLRTKKFSVPSACEMLE 96
Cdd:pfam03765   6 LELLKDEDEETDREKfwltREDHDDVCLLRFLRARKWDVEKAIKMLE 52
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
138-275 2.23e-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: 37.69  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574921   138 GRQVIFSVAAKFDPYKFTSVQMARVHSLVCEALLDDEDSQvaGYVYINDESGMNMGFVSLWSLtdLRSIVKCIQNSTPMR 217
Cdd:pfam13716   1 GRPVLVFISKLLPSRPASLDDLDRLLFYLLKTLSEKLKGK--PFVVVVDHTGVTSENFPSLSF--LKKAYDLLPRAFKKN 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 28574921   218 HKETHFVNIPHYANRII-ELGVSMLSDKLKKRIIVHKNVDILKTKIDPAILPKEYGGTV 275
Cdd:pfam13716  77 LKAVYVVHPSTFLRTFLkTLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPTELPGVL 135
 
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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