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Conserved domains on  [gi|24586355|ref|NP_724598|]
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Gdap2, isoform B [Drosophila melanogaster]

Protein Classification

CRAL-TRIO domain-containing protein( domain architecture ID 10617167)

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_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
97-228 1.75e-33

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: 117.81  E-value: 1.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586355    97 GRPVIVFCGKWFPAQNI---DLEKALLYLI-KLLDPIVKGDYVISYFHTLTSTNNYPSLHWLREVYSVLPYKYKKNLKAF 172
Cdd:pfam13716   1 GRPVLVFISKLLPSRPAsldDLDRLLFYLLkTLSEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKAV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 24586355   173 YIVHPTFWTKMMTW-WFTTFMAPAIKAKVHSLPGVEHLYSAITKDQL--EIPaYITEYD 228
Cdd:pfam13716  81 YVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLptELP-GVLSYD 138
 
Name Accession Description Interval E-value
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
97-228 1.75e-33

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: 117.81  E-value: 1.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586355    97 GRPVIVFCGKWFPAQNI---DLEKALLYLI-KLLDPIVKGDYVISYFHTLTSTNNYPSLHWLREVYSVLPYKYKKNLKAF 172
Cdd:pfam13716   1 GRPVLVFISKLLPSRPAsldDLDRLLFYLLkTLSEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKAV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 24586355   173 YIVHPTFWTKMMTW-WFTTFMAPAIKAKVHSLPGVEHLYSAITKDQL--EIPaYITEYD 228
Cdd:pfam13716  81 YVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLptELP-GVLSYD 138
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
76-221 1.32e-27

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: 103.18  E-value: 1.32e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586355  76 VEDLTEVSGiGCLYQSGVDRLGRPVIVFCGKWFPAQNIDLEKALLYLIKLLDPIVKGDYVISYFHTL------TSTNNYP 149
Cdd:cd00170   1 LEELLELLG-GIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVViidlkgFSLSNLS 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24586355 150 SLHWLREVYSVLPYKYKKNLKAFYIVHPTFWTKMMTWWFTTFMAPAIKAKVHSLPG-VEHLYSAITKDQLEIP 221
Cdd:cd00170  80 DLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSdLEELLEYIDPDQLPKE 152
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
85-219 1.42e-20

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: 85.04  E-value: 1.42e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586355     85 IGCLYQSGVDRLGRPVIVFCGKWFPAQNIDLEKALLYLIKLLDPIV---KGDYVISYFHTLTSTNNYPSLH----WLREV 157
Cdd:smart00516   7 AYIPGGRGYDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILqeeKKTGGIEGFTVIFDLKGLSMSNpdlsVLRKI 86
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24586355    158 YSVLPYKYKKNLKAFYIVHPTFWTKMMTWWFTTFMAPAIKAKVH--SLPGVEHLYSAITKDQLE 219
Cdd:smart00516  87 LKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRfvGNDSKEELLEYIDKEQLP 150
 
Name Accession Description Interval E-value
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
97-228 1.75e-33

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: 117.81  E-value: 1.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586355    97 GRPVIVFCGKWFPAQNI---DLEKALLYLI-KLLDPIVKGDYVISYFHTLTSTNNYPSLHWLREVYSVLPYKYKKNLKAF 172
Cdd:pfam13716   1 GRPVLVFISKLLPSRPAsldDLDRLLFYLLkTLSEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKAV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 24586355   173 YIVHPTFWTKMMTW-WFTTFMAPAIKAKVHSLPGVEHLYSAITKDQL--EIPaYITEYD 228
Cdd:pfam13716  81 YVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLptELP-GVLSYD 138
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
76-221 1.32e-27

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: 103.18  E-value: 1.32e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586355  76 VEDLTEVSGiGCLYQSGVDRLGRPVIVFCGKWFPAQNIDLEKALLYLIKLLDPIVKGDYVISYFHTL------TSTNNYP 149
Cdd:cd00170   1 LEELLELLG-GIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVViidlkgFSLSNLS 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24586355 150 SLHWLREVYSVLPYKYKKNLKAFYIVHPTFWTKMMTWWFTTFMAPAIKAKVHSLPG-VEHLYSAITKDQLEIP 221
Cdd:cd00170  80 DLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSdLEELLEYIDPDQLPKE 152
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
85-219 1.42e-20

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: 85.04  E-value: 1.42e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586355     85 IGCLYQSGVDRLGRPVIVFCGKWFPAQNIDLEKALLYLIKLLDPIV---KGDYVISYFHTLTSTNNYPSLH----WLREV 157
Cdd:smart00516   7 AYIPGGRGYDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILqeeKKTGGIEGFTVIFDLKGLSMSNpdlsVLRKI 86
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24586355    158 YSVLPYKYKKNLKAFYIVHPTFWTKMMTWWFTTFMAPAIKAKVH--SLPGVEHLYSAITKDQLE 219
Cdd:smart00516  87 LKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRfvGNDSKEELLEYIDKEQLP 150
 
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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