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Conserved domains on  [gi|19921536|ref|NP_609967|]
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uncharacterized protein Dmel_CG10237, isoform B [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

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List of domain hits

Name Accession Description Interval E-value
CRAL_TRIO pfam00650
CRAL/TRIO domain;
141-290 1.72e-43

CRAL/TRIO domain;


:

Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 146.63  E-value: 1.72e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921536   141 NILTVFPNRDQLGRRILVLELGkRWKHKQVTLDEVFKGAVLFLEAAMLE-PETQICGAVVIFDMDGLSLQQTWQFTPPFA 219
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLG-RHDPKKSSEEELVRFLVLVLERALLLmPEGQVEGLTVIIDLKGLSLSNMDWWSISLL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921536   220 KRIVDWLQDSVPLRIKAIHIVNQPKIFQVVFALFKPFLKEKLRSRIIFH-GTDRESLHKYMSPKCLPAAYGG 290
Cdd:pfam00650  80 KKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLkNSNEEELEKYIPPEQLPKEYGG 151
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
68-115 5.24e-06

CRAL/TRIO, N-terminal domain;


:

Pssm-ID: 215024  Cd Length: 48  Bit Score: 42.92  E-value: 5.24e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 19921536     68 KEASKELARLLEAETDLLYPKGNEEWLIRYLRPCKYYPESARDLIKRY 115
Cdd:smart01100   1 EEALEELRELLEKHPDLLPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
 
Name Accession Description Interval E-value
CRAL_TRIO pfam00650
CRAL/TRIO domain;
141-290 1.72e-43

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 146.63  E-value: 1.72e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921536   141 NILTVFPNRDQLGRRILVLELGkRWKHKQVTLDEVFKGAVLFLEAAMLE-PETQICGAVVIFDMDGLSLQQTWQFTPPFA 219
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLG-RHDPKKSSEEELVRFLVLVLERALLLmPEGQVEGLTVIIDLKGLSLSNMDWWSISLL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921536   220 KRIVDWLQDSVPLRIKAIHIVNQPKIFQVVFALFKPFLKEKLRSRIIFH-GTDRESLHKYMSPKCLPAAYGG 290
Cdd:pfam00650  80 KKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLkNSNEEELEKYIPPEQLPKEYGG 151
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
139-290 7.93e-42

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: 142.47  E-value: 7.93e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921536 139 KHNILTVFPNRDQLGRRILVLELGKrWKHKQVTLDEVFKGAVLFLEAAMLEPETQICGAVVIFDMDGLSLQQTWqfTPPF 218
Cdd:cd00170   7 LLGGIGYLGGRDKEGRPVLVFRAGW-DPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLS--DLSL 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921536 219 AKRIVDWLQDSVPLRIKAIHIVNQPKIFQVVFALFKPFLKEKLRSRIIFHGTDRESLHKYMSPKCLPAAYGG 290
Cdd:cd00170  84 LKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSDLEELLEYIDPDQLPKELGG 155
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
148-290 7.31e-29

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: 7.31e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921536    148 NRDQLGRRILVLELGkRWKHKQVTLDEVFKGAVLFLEAAMLE--PETQICGAVVIFDMDGLSLqqtWQFTPPFAKRIVDW 225
Cdd:smart00516  14 GYDKDGRPVLIERAG-RFDLKSVTLEELLRYLVYVLEKILQEekKTGGIEGFTVIFDLKGLSM---SNPDLSVLRKILKI 89
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19921536    226 LQDSVPLRIKAIHIVNQPKIFQVVFALFKPFLKEKLRSRIIFHGTD-RESLHKYMSPKCLPAAYGG 290
Cdd:smart00516  90 LQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDsKEELLEYIDKEQLPEELGG 155
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
68-115 5.24e-06

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 42.92  E-value: 5.24e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 19921536     68 KEASKELARLLEAETDLLYPKGNEEWLIRYLRPCKYYPESARDLIKRY 115
Cdd:smart01100   1 EEALEELRELLEKHPDLLPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
 
Name Accession Description Interval E-value
CRAL_TRIO pfam00650
CRAL/TRIO domain;
141-290 1.72e-43

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 146.63  E-value: 1.72e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921536   141 NILTVFPNRDQLGRRILVLELGkRWKHKQVTLDEVFKGAVLFLEAAMLE-PETQICGAVVIFDMDGLSLQQTWQFTPPFA 219
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLG-RHDPKKSSEEELVRFLVLVLERALLLmPEGQVEGLTVIIDLKGLSLSNMDWWSISLL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921536   220 KRIVDWLQDSVPLRIKAIHIVNQPKIFQVVFALFKPFLKEKLRSRIIFH-GTDRESLHKYMSPKCLPAAYGG 290
Cdd:pfam00650  80 KKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLkNSNEEELEKYIPPEQLPKEYGG 151
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
139-290 7.93e-42

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: 142.47  E-value: 7.93e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921536 139 KHNILTVFPNRDQLGRRILVLELGKrWKHKQVTLDEVFKGAVLFLEAAMLEPETQICGAVVIFDMDGLSLQQTWqfTPPF 218
Cdd:cd00170   7 LLGGIGYLGGRDKEGRPVLVFRAGW-DPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLS--DLSL 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921536 219 AKRIVDWLQDSVPLRIKAIHIVNQPKIFQVVFALFKPFLKEKLRSRIIFHGTDRESLHKYMSPKCLPAAYGG 290
Cdd:cd00170  84 LKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSDLEELLEYIDPDQLPKELGG 155
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
148-290 7.31e-29

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: 7.31e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921536    148 NRDQLGRRILVLELGkRWKHKQVTLDEVFKGAVLFLEAAMLE--PETQICGAVVIFDMDGLSLqqtWQFTPPFAKRIVDW 225
Cdd:smart00516  14 GYDKDGRPVLIERAG-RFDLKSVTLEELLRYLVYVLEKILQEekKTGGIEGFTVIFDLKGLSM---SNPDLSVLRKILKI 89
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19921536    226 LQDSVPLRIKAIHIVNQPKIFQVVFALFKPFLKEKLRSRIIFHGTD-RESLHKYMSPKCLPAAYGG 290
Cdd:smart00516  90 LQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDsKEELLEYIDKEQLPEELGG 155
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
68-115 5.24e-06

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 42.92  E-value: 5.24e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 19921536     68 KEASKELARLLEAETDLLYPKGNEEWLIRYLRPCKYYPESARDLIKRY 115
Cdd:smart01100   1 EEALEELRELLEKHPDLLPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
153-293 2.31e-04

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: 40.77  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921536   153 GRRILVLeLGKRWKHKQVTLDEVFKgaVLFLeaAMLEPETQICGA--VVIFDMDGLslqqTWQFTPP--FAKRIVDWLQD 228
Cdd:pfam13716   1 GRPVLVF-ISKLLPSRPASLDDLDR--LLFY--LLKTLSEKLKGKpfVVVVDHTGV----TSENFPSlsFLKKAYDLLPR 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19921536   229 SVPLRIKAIHIVNQPKIFQVVFA-LFKPFLKEKLRSRIIFHGTdRESLHKYMSPKCLPAAYGGFRE 293
Cdd:pfam13716  72 AFKKNLKAVYVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSS-LSELWEGIDREQLPTELPGVLS 136
 
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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