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Conserved domains on  [gi|392890892|ref|NP_001254156|]
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CRAL-TRIO domain-containing protein [Caenorhabditis elegans]

Protein Classification

SEC14 and EMP24_GP25L domain-containing protein( domain architecture ID 11271403)

SEC14 and EMP24_GP25L domain-containing protein

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 ...
 98-267 1.72e-35

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: 128.19  E-value: 1.72e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890892    98 DCSVPLRYLPGSLiGLDHENNVVSLQMIGHLDaaglMPATRNSDLYRMRIAESEGVMQIirkmEKEQGKPLGTSVIFDLD 177
Cdd:smart00516   1 ELELLKAYIPGGR-GYDKDGRPVLIERAGRFD----LKSVTLEELLRYLVYVLEKILQE----EKKTGGIEGFTVIFDLK 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890892   178 GLSMVQIDLaalKVVTTMLSQLQEMFPDVIRKIFIVNTPTFIQVLWSMISPCLAKQTQQKVKILGNDWKQHLKENIGEEV 257
Cdd:smart00516  72 GLSMSNPDL---SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKEQ 148

                          170
                   ....*....|
gi 392890892   258 LFERWGGTRK 267
Cdd:smart00516 149 LPEELGGTLD 158
EMP24_GP25L super family cl03099
emp24/gp25L/p24 family/GOLD; Members of this family are implicated in bringing cargo forward ...
 331-405 4.59e-03

emp24/gp25L/p24 family/GOLD; Members of this family are implicated in bringing cargo forward from the ER and binding to coat proteins by their cytoplasmic domains. This domain corresponds closely to the beta-strand rich GOLD domain described in. The GOLD domain is always found combined with lipid- or membrane-association domains.


The actual alignment was detected with superfamily member pfam01105:

Pssm-ID: 426051  Cd Length: 181  Bit Score: 38.05  E-value: 4.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392890892  331 ENNDINFSIlRAAEGEEKVAEHDDDYMVHPKFKLQtdfvpedgevcAAEPGVYKFVFDNTHSKLRSKTVKYFIEV 405
Cdd:pfam01105  34 GGLDVDFTV-TDPDGNGNVIYSKKDRKSGGDFSFT-----------ATESGEYKFCFDNSFSTFSSKTVSFDIKV 96
 
Name Accession Description Interval E-value
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 98-267 1.72e-35

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: 128.19  E-value: 1.72e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890892    98 DCSVPLRYLPGSLiGLDHENNVVSLQMIGHLDaaglMPATRNSDLYRMRIAESEGVMQIirkmEKEQGKPLGTSVIFDLD 177
Cdd:smart00516   1 ELELLKAYIPGGR-GYDKDGRPVLIERAGRFD----LKSVTLEELLRYLVYVLEKILQE----EKKTGGIEGFTVIFDLK 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890892   178 GLSMVQIDLaalKVVTTMLSQLQEMFPDVIRKIFIVNTPTFIQVLWSMISPCLAKQTQQKVKILGNDWKQHLKENIGEEV 257
Cdd:smart00516  72 GLSMSNPDL---SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKEQ 148

                          170
                   ....*....|
gi 392890892   258 LFERWGGTRK 267
Cdd:smart00516 149 LPEELGGTLD 158
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 112-265 4.29e-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: 92.01  E-value: 4.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890892 112 GLDHENNVVSLQMIGHldaaGLMPATRNSDLYRMRIAESEgvmQIIRKMEKEQGkplGTSVIFDLDGLSMVQidLAALKV 191
Cdd:cd00170   16 GRDKEGRPVLVFRAGW----DPPKLLDLEELLRYLVYLLE---KALRELEEQVE---GFVVIIDLKGFSLSN--LSDLSL 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392890892 192 VTTMLSQLQEMFPDVIRKIFIVNTPTFIQVLWSMISPCLAKQTQQKVKILGNDWKQhLKENIGEEVLFERWGGT 265
Cdd:cd00170   84 LKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSDLEE-LLEYIDPDQLPKELGGT 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
153-264 7.46e-15

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 71.52  E-value: 7.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890892  153 VMQIIRKMEKEQGKPlGTSVIFDLDGLSMVQIDLAALKVVTTMLSQLQEMFPDVIRKIFIVNTPTFIQVLWSMISPCLAK 232
Cdd:pfam00650  41 VLERALLLMPEGQVE-GLTVIIDLKGLSLSNMDWWSISLLKKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDP 119

                          90       100       110
                  ....*....|....*....|....*....|..
gi 392890892  233 QTQQKVKILGNDWKQHLKENIGEEVLFERWGG 264
Cdd:pfam00650 120 KTREKIVFLKNSNEEELEKYIPPEQLPKEYGG 151
EMP24_GP25L pfam01105
emp24/gp25L/p24 family/GOLD; Members of this family are implicated in bringing cargo forward ...
 331-405 4.59e-03

emp24/gp25L/p24 family/GOLD; Members of this family are implicated in bringing cargo forward from the ER and binding to coat proteins by their cytoplasmic domains. This domain corresponds closely to the beta-strand rich GOLD domain described in. The GOLD domain is always found combined with lipid- or membrane-association domains.


Pssm-ID: 426051  Cd Length: 181  Bit Score: 38.05  E-value: 4.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392890892  331 ENNDINFSIlRAAEGEEKVAEHDDDYMVHPKFKLQtdfvpedgevcAAEPGVYKFVFDNTHSKLRSKTVKYFIEV 405
Cdd:pfam01105  34 GGLDVDFTV-TDPDGNGNVIYSKKDRKSGGDFSFT-----------ATESGEYKFCFDNSFSTFSSKTVSFDIKV 96
 
Name Accession Description Interval E-value
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 98-267 1.72e-35

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: 128.19  E-value: 1.72e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890892    98 DCSVPLRYLPGSLiGLDHENNVVSLQMIGHLDaaglMPATRNSDLYRMRIAESEGVMQIirkmEKEQGKPLGTSVIFDLD 177
Cdd:smart00516   1 ELELLKAYIPGGR-GYDKDGRPVLIERAGRFD----LKSVTLEELLRYLVYVLEKILQE----EKKTGGIEGFTVIFDLK 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890892   178 GLSMVQIDLaalKVVTTMLSQLQEMFPDVIRKIFIVNTPTFIQVLWSMISPCLAKQTQQKVKILGNDWKQHLKENIGEEV 257
Cdd:smart00516  72 GLSMSNPDL---SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKEQ 148

                          170
                   ....*....|
gi 392890892   258 LFERWGGTRK 267
Cdd:smart00516 149 LPEELGGTLD 158
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 112-265 4.29e-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: 92.01  E-value: 4.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890892 112 GLDHENNVVSLQMIGHldaaGLMPATRNSDLYRMRIAESEgvmQIIRKMEKEQGkplGTSVIFDLDGLSMVQidLAALKV 191
Cdd:cd00170   16 GRDKEGRPVLVFRAGW----DPPKLLDLEELLRYLVYLLE---KALRELEEQVE---GFVVIIDLKGFSLSN--LSDLSL 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392890892 192 VTTMLSQLQEMFPDVIRKIFIVNTPTFIQVLWSMISPCLAKQTQQKVKILGNDWKQhLKENIGEEVLFERWGGT 265
Cdd:cd00170   84 LKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSDLEE-LLEYIDPDQLPKELGGT 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
153-264 7.46e-15

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 71.52  E-value: 7.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890892  153 VMQIIRKMEKEQGKPlGTSVIFDLDGLSMVQIDLAALKVVTTMLSQLQEMFPDVIRKIFIVNTPTFIQVLWSMISPCLAK 232
Cdd:pfam00650  41 VLERALLLMPEGQVE-GLTVIIDLKGLSLSNMDWWSISLLKKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDP 119

                          90       100       110
                  ....*....|....*....|....*....|..
gi 392890892  233 QTQQKVKILGNDWKQHLKENIGEEVLFERWGG 264
Cdd:pfam00650 120 KTREKIVFLKNSNEEELEKYIPPEQLPKEYGG 151
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 153-260 9.58e-04

Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial phospholipase which maintains mitochondrial integrity. PNPLA8 is also known as iPLA2-gamma. In humans, it is predominantly expressed in heart tissue. iPLA2-gamma can catalyze both phospholipase A1 and A2 reactions (PLA1 and PLA2 respectively). This family includes PNPLA8 (iPLA2-gamma) from Homo sapiens and iPLA2-2 from Mus musculus.


Pssm-ID: 132850 [Multi-domain]  Cd Length: 308  Bit Score: 40.70  E-value: 9.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890892 153 VMQIIRKMEKEQGKPLGTsvIFDLD-GLSMVQIDLAALKVVTTMLSQLQEMFPDVIRKIFIVNTPTF--IQVLWSmispc 229
Cdd:cd07211   23 ALEILRKIEKLTGKPIHE--LFDYIcGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVFSQNTYISgtSRLVLS----- 95

                         90       100       110
                 ....*....|....*....|....*....|.
gi 392890892 230 LAKQTQQKvkilgndWKQHLKENIGEEVLFE 260
Cdd:cd07211   96 HAYYDTET-------WEKILKEMMGSDELID 119
EMP24_GP25L pfam01105
emp24/gp25L/p24 family/GOLD; Members of this family are implicated in bringing cargo forward ...
 331-405 4.59e-03

emp24/gp25L/p24 family/GOLD; Members of this family are implicated in bringing cargo forward from the ER and binding to coat proteins by their cytoplasmic domains. This domain corresponds closely to the beta-strand rich GOLD domain described in. The GOLD domain is always found combined with lipid- or membrane-association domains.


Pssm-ID: 426051  Cd Length: 181  Bit Score: 38.05  E-value: 4.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392890892  331 ENNDINFSIlRAAEGEEKVAEHDDDYMVHPKFKLQtdfvpedgevcAAEPGVYKFVFDNTHSKLRSKTVKYFIEV 405
Cdd:pfam01105  34 GGLDVDFTV-TDPDGNGNVIYSKKDRKSGGDFSFT-----------ATESGEYKFCFDNSFSTFSSKTVSFDIKV 96
 
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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