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Conserved domains on  [gi|17563812|ref|NP_505874|]
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CRAL-TRIO domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
85-254 1.83e-27

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: 105.84  E-value: 1.83e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563812     85 KDCFERFHISQLNYEvtSKNLHVFVQKMEGTDikeiLKVMPLSYVLHSYFMLQENfsraMAHTERKTGKTSSVVCILDLK 164
Cdd:smart00516   2 LELLKAYIPGGRGYD--KDGRPVLIERAGRFD----LKSVTLEELLRYLVYVLEK----ILQEEKKTGGIEGFTVIFDLK 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563812    165 GLNLMDFmnplsgPAQLARLVVQVWAEYFSEHLCKLLLINPPGIISVMWQVTKRLVDPNTVEKLAFLSN--VEDLKKYLE 242
Cdd:smart00516  72 GLSMSNP------DLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNdsKEELLEYID 145
                          170
                   ....*....|..
gi 17563812    243 PEAIPVEYGGTY 254
Cdd:smart00516 146 KEQLPEELGGTL 157
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
281-329 9.52e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd20950:

Pssm-ID: 472250  Cd Length: 97  Bit Score: 41.15  E-value: 9.52e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 17563812 281 PQEYIWVKNGILKAPKGKsySIKAFQTSEYIIKTTTeGKLVWNYTTSGD 329
Cdd:cd20950  27 PSEYTWFKDGVVMPTNPK--STRAFSNSSYSLDPTT-GELVFDPLSASD 72
 
Name Accession Description Interval E-value
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
85-254 1.83e-27

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: 105.84  E-value: 1.83e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563812     85 KDCFERFHISQLNYEvtSKNLHVFVQKMEGTDikeiLKVMPLSYVLHSYFMLQENfsraMAHTERKTGKTSSVVCILDLK 164
Cdd:smart00516   2 LELLKAYIPGGRGYD--KDGRPVLIERAGRFD----LKSVTLEELLRYLVYVLEK----ILQEEKKTGGIEGFTVIFDLK 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563812    165 GLNLMDFmnplsgPAQLARLVVQVWAEYFSEHLCKLLLINPPGIISVMWQVTKRLVDPNTVEKLAFLSN--VEDLKKYLE 242
Cdd:smart00516  72 GLSMSNP------DLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNdsKEELLEYID 145
                          170
                   ....*....|..
gi 17563812    243 PEAIPVEYGGTY 254
Cdd:smart00516 146 KEQLPEELGGTL 157
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
122-253 2.41e-19

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: 83.92  E-value: 2.41e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563812 122 KVMPLSYVLHSYFMLQENFSRAMAHTERKtgktssVVCILDLKGLNLMDFMNPlsgpaQLARLVVQVWAEYFSEHLCKLL 201
Cdd:cd00170  35 KLLDLEELLRYLVYLLEKALRELEEQVEG------FVVIIDLKGFSLSNLSDL-----SLLKKLLKILQDHYPERLKKIY 103
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 17563812 202 LINPPGIISVMWQVTKRLVDPNTVEKLAFL-SNVEDLKKYLEPEAIPVEYGGT 253
Cdd:cd00170 104 IVNAPWIFSALWKIVKPFLSEKTRKKIVFLgSDLEELLEYIDPDQLPKELGGT 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
151-252 1.71e-14

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 69.98  E-value: 1.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563812   151 TGKTSSVVCILDLKGLNLMDFmnpLSGPAQLARLVVQVWAEYFSEHLCKLLLINPPGIISVMWQVTKRLVDPNTVEKLAF 230
Cdd:pfam00650  51 EGQVEGLTVIIDLKGLSLSNM---DWWSISLLKKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVF 127
                          90       100
                  ....*....|....*....|....
gi 17563812   231 L--SNVEDLKKYLEPEAIPVEYGG 252
Cdd:pfam00650 128 LknSNEEELEKYIPPEQLPKEYGG 151
IgI_2_JAM1 cd20950
Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF ...
281-329 9.52e-05

Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF domains; The members here are composed of the second Ig-like domain of Junctional adhesion molecule-1 (JAM1). JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The second Ig-like domain of JAM1 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, the A strand of the I-set is discontinuous but lacks a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409542  Cd Length: 97  Bit Score: 41.15  E-value: 9.52e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 17563812 281 PQEYIWVKNGILKAPKGKsySIKAFQTSEYIIKTTTeGKLVWNYTTSGD 329
Cdd:cd20950  27 PSEYTWFKDGVVMPTNPK--STRAFSNSSYSLDPTT-GELVFDPLSASD 72
 
Name Accession Description Interval E-value
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
85-254 1.83e-27

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: 105.84  E-value: 1.83e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563812     85 KDCFERFHISQLNYEvtSKNLHVFVQKMEGTDikeiLKVMPLSYVLHSYFMLQENfsraMAHTERKTGKTSSVVCILDLK 164
Cdd:smart00516   2 LELLKAYIPGGRGYD--KDGRPVLIERAGRFD----LKSVTLEELLRYLVYVLEK----ILQEEKKTGGIEGFTVIFDLK 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563812    165 GLNLMDFmnplsgPAQLARLVVQVWAEYFSEHLCKLLLINPPGIISVMWQVTKRLVDPNTVEKLAFLSN--VEDLKKYLE 242
Cdd:smart00516  72 GLSMSNP------DLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNdsKEELLEYID 145
                          170
                   ....*....|..
gi 17563812    243 PEAIPVEYGGTY 254
Cdd:smart00516 146 KEQLPEELGGTL 157
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
122-253 2.41e-19

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: 83.92  E-value: 2.41e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563812 122 KVMPLSYVLHSYFMLQENFSRAMAHTERKtgktssVVCILDLKGLNLMDFMNPlsgpaQLARLVVQVWAEYFSEHLCKLL 201
Cdd:cd00170  35 KLLDLEELLRYLVYLLEKALRELEEQVEG------FVVIIDLKGFSLSNLSDL-----SLLKKLLKILQDHYPERLKKIY 103
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 17563812 202 LINPPGIISVMWQVTKRLVDPNTVEKLAFL-SNVEDLKKYLEPEAIPVEYGGT 253
Cdd:cd00170 104 IVNAPWIFSALWKIVKPFLSEKTRKKIVFLgSDLEELLEYIDPDQLPKELGGT 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
151-252 1.71e-14

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 69.98  E-value: 1.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563812   151 TGKTSSVVCILDLKGLNLMDFmnpLSGPAQLARLVVQVWAEYFSEHLCKLLLINPPGIISVMWQVTKRLVDPNTVEKLAF 230
Cdd:pfam00650  51 EGQVEGLTVIIDLKGLSLSNM---DWWSISLLKKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVF 127
                          90       100
                  ....*....|....*....|....
gi 17563812   231 L--SNVEDLKKYLEPEAIPVEYGG 252
Cdd:pfam00650 128 LknSNEEELEKYIPPEQLPKEYGG 151
IgI_2_JAM1 cd20950
Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF ...
281-329 9.52e-05

Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF domains; The members here are composed of the second Ig-like domain of Junctional adhesion molecule-1 (JAM1). JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The second Ig-like domain of JAM1 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, the A strand of the I-set is discontinuous but lacks a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409542  Cd Length: 97  Bit Score: 41.15  E-value: 9.52e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 17563812 281 PQEYIWVKNGILKAPKGKsySIKAFQTSEYIIKTTTeGKLVWNYTTSGD 329
Cdd:cd20950  27 PSEYTWFKDGVVMPTNPK--STRAFSNSSYSLDPTT-GELVFDPLSASD 72
 
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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