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Conserved domains on  [gi|442626331|ref|NP_001260132|]
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real-time, isoform B [Drosophila melanogaster]

Protein Classification

PRELI and SEC14 domain-containing protein( domain architecture ID 11152443)

protein containing domains PRELI, CRAL_TRIO_N, and SEC14

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRELI pfam04707
PRELI-like family; This family includes a conserved region found in the PRELI protein and ...
17-173 1.58e-66

PRELI-like family; This family includes a conserved region found in the PRELI protein and yeast YLR168C gene MSF1 product. The function of this protein is unknown, though it is thought to be involved in intra-mitochondrial protein sorting. This region is also found in a number of other eukaryotic proteins.


:

Pssm-ID: 398400  Cd Length: 156  Bit Score: 216.01  E-value: 1.58e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626331   17 ELVMKAYERRFPTcPQMPIVLDCEVIKDEsLEDGAKRNTSRRCKLAVDAPYIFKKLIGVDH-VYFLQHNFLDLANRTLSI 95
Cdd:pfam04707   1 EQVTAAFWRRYPN-PYSPHVISVDVLERE-LDDDGKLHTERLLTKQGRLPRWLKKLIGVAHtVYVVEVSVVDPKKRTLTL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626331   96 EAVNESFSSRIEIFERCRYYAHPDNSEWTCFDQSATLDIKNFFGFEHSMEKMGMKQYTQTTLKGKEIIEFFIGQLREE 173
Cdd:pfam04707  79 ETRNLTFSNRLSVDERCRYTPHPENPNWTIFDQEASISISGFFGFSSKVEKWSLKRFSQNAKKGREGMEYVLQKLEEE 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
293-456 1.06e-39

CRAL/TRIO domain;


:

Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 143.17  E-value: 1.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626331  293 HFPGGWHHLDKDGRPVYILRLGHMDVKgllkSLGMDGLLRLALHICEEGIQKINEsaerleKPVLNWSLLVDLEGLSMRH 372
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLGRHDPK----KSSEEELVRFLVLVLERALLLMPE------GQVEGLTVIIDLKGLSLSN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626331  373 LWRPGIKALLNIIETVERNYPETMGRVLVVRAPRVFPIAWTIVSAFIDEHTRSKFLFYGPdcaHMKDGLAQYLDEEIVPD 452
Cdd:pfam00650  71 MDWWSISLLKKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKN---SNEEELEKYIPPEQLPK 147

                  ....
gi 442626331  453 FLGG 456
Cdd:pfam00650 148 EYGG 151
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
222-268 4.31e-08

CRAL/TRIO, N-terminal domain;


:

Pssm-ID: 215024  Cd Length: 48  Bit Score: 49.86  E-value: 4.31e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 442626331   222 ESKLLELRKMLDGVDDL-ERVPSYQTILRFLAARDWHVSQAYAMLCDS 268
Cdd:smart01100   1 EEALEELRELLEKHPDLlPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
 
Name Accession Description Interval E-value
PRELI pfam04707
PRELI-like family; This family includes a conserved region found in the PRELI protein and ...
17-173 1.58e-66

PRELI-like family; This family includes a conserved region found in the PRELI protein and yeast YLR168C gene MSF1 product. The function of this protein is unknown, though it is thought to be involved in intra-mitochondrial protein sorting. This region is also found in a number of other eukaryotic proteins.


Pssm-ID: 398400  Cd Length: 156  Bit Score: 216.01  E-value: 1.58e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626331   17 ELVMKAYERRFPTcPQMPIVLDCEVIKDEsLEDGAKRNTSRRCKLAVDAPYIFKKLIGVDH-VYFLQHNFLDLANRTLSI 95
Cdd:pfam04707   1 EQVTAAFWRRYPN-PYSPHVISVDVLERE-LDDDGKLHTERLLTKQGRLPRWLKKLIGVAHtVYVVEVSVVDPKKRTLTL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626331   96 EAVNESFSSRIEIFERCRYYAHPDNSEWTCFDQSATLDIKNFFGFEHSMEKMGMKQYTQTTLKGKEIIEFFIGQLREE 173
Cdd:pfam04707  79 ETRNLTFSNRLSVDERCRYTPHPENPNWTIFDQEASISISGFFGFSSKVEKWSLKRFSQNAKKGREGMEYVLQKLEEE 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
293-456 1.06e-39

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 143.17  E-value: 1.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626331  293 HFPGGWHHLDKDGRPVYILRLGHMDVKgllkSLGMDGLLRLALHICEEGIQKINEsaerleKPVLNWSLLVDLEGLSMRH 372
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLGRHDPK----KSSEEELVRFLVLVLERALLLMPE------GQVEGLTVIIDLKGLSLSN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626331  373 LWRPGIKALLNIIETVERNYPETMGRVLVVRAPRVFPIAWTIVSAFIDEHTRSKFLFYGPdcaHMKDGLAQYLDEEIVPD 452
Cdd:pfam00650  71 MDWWSISLLKKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKN---SNEEELEKYIPPEQLPK 147

                  ....
gi 442626331  453 FLGG 456
Cdd:pfam00650 148 EYGG 151
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
294-459 3.18e-34

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: 127.80  E-value: 3.18e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626331   294 FPGGWHHlDKDGRPVYILRLGHMDvkglLKSLGMDGLLRLALHICEEGIQKinesaERLEKPVLNWSLLVDLEGLSMRHl 373
Cdd:smart00516   9 IPGGRGY-DKDGRPVLIERAGRFD----LKSVTLEELLRYLVYVLEKILQE-----EKKTGGIEGFTVIFDLKGLSMSN- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626331   374 wrPGIKALLNIIETVERNYPETMGRVLVVRAPRVFPIAWTIVSAFIDEHTRSKFLFYGPDCahmKDGLAQYLDEEIVPDF 453
Cdd:smart00516  78 --PDLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDS---KEELLEYIDKEQLPEE 152

                   ....*.
gi 442626331   454 LGGPCK 459
Cdd:smart00516 153 LGGTLD 158
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
294-456 5.69e-34

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: 127.07  E-value: 5.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626331 294 FPGGWHHLDKDGRPVYILRLGHmdvkGLLKSLGMDGLLRLALHICEEGIQKINESAERlekpvlnWSLLVDLEGLSMRHL 373
Cdd:cd00170   10 GIGYLGGRDKEGRPVLVFRAGW----DPPKLLDLEELLRYLVYLLEKALRELEEQVEG-------FVVIIDLKGFSLSNL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626331 374 WrpGIKALLNIIETVERNYPETMGRVLVVRAPRVFPIAWTIVSAFIDEHTRSKFLFYGPDcahmKDGLAQYLDEEIVPDF 453
Cdd:cd00170   79 S--DLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSD----LEELLEYIDPDQLPKE 152

                 ...
gi 442626331 454 LGG 456
Cdd:cd00170  153 LGG 155
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
222-268 4.31e-08

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 49.86  E-value: 4.31e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 442626331   222 ESKLLELRKMLDGVDDL-ERVPSYQTILRFLAARDWHVSQAYAMLCDS 268
Cdd:smart01100   1 EEALEELRELLEKHPDLlPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
CRAL_TRIO_N pfam03765
CRAL/TRIO, N-terminal domain; This all-alpha domain is found to the N-terminus of pfam00650.
246-267 2.53e-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: 39.18  E-value: 2.53e-04
                          10        20
                  ....*....|....*....|..
gi 442626331  246 TILRFLAARDWHVSQAYAMLCD 267
Cdd:pfam03765  32 CLLRFLRARKWDVEKAIKMLED 53
 
Name Accession Description Interval E-value
PRELI pfam04707
PRELI-like family; This family includes a conserved region found in the PRELI protein and ...
17-173 1.58e-66

PRELI-like family; This family includes a conserved region found in the PRELI protein and yeast YLR168C gene MSF1 product. The function of this protein is unknown, though it is thought to be involved in intra-mitochondrial protein sorting. This region is also found in a number of other eukaryotic proteins.


Pssm-ID: 398400  Cd Length: 156  Bit Score: 216.01  E-value: 1.58e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626331   17 ELVMKAYERRFPTcPQMPIVLDCEVIKDEsLEDGAKRNTSRRCKLAVDAPYIFKKLIGVDH-VYFLQHNFLDLANRTLSI 95
Cdd:pfam04707   1 EQVTAAFWRRYPN-PYSPHVISVDVLERE-LDDDGKLHTERLLTKQGRLPRWLKKLIGVAHtVYVVEVSVVDPKKRTLTL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626331   96 EAVNESFSSRIEIFERCRYYAHPDNSEWTCFDQSATLDIKNFFGFEHSMEKMGMKQYTQTTLKGKEIIEFFIGQLREE 173
Cdd:pfam04707  79 ETRNLTFSNRLSVDERCRYTPHPENPNWTIFDQEASISISGFFGFSSKVEKWSLKRFSQNAKKGREGMEYVLQKLEEE 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
293-456 1.06e-39

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 143.17  E-value: 1.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626331  293 HFPGGWHHLDKDGRPVYILRLGHMDVKgllkSLGMDGLLRLALHICEEGIQKINEsaerleKPVLNWSLLVDLEGLSMRH 372
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLGRHDPK----KSSEEELVRFLVLVLERALLLMPE------GQVEGLTVIIDLKGLSLSN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626331  373 LWRPGIKALLNIIETVERNYPETMGRVLVVRAPRVFPIAWTIVSAFIDEHTRSKFLFYGPdcaHMKDGLAQYLDEEIVPD 452
Cdd:pfam00650  71 MDWWSISLLKKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKN---SNEEELEKYIPPEQLPK 147

                  ....
gi 442626331  453 FLGG 456
Cdd:pfam00650 148 EYGG 151
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
294-459 3.18e-34

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: 127.80  E-value: 3.18e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626331   294 FPGGWHHlDKDGRPVYILRLGHMDvkglLKSLGMDGLLRLALHICEEGIQKinesaERLEKPVLNWSLLVDLEGLSMRHl 373
Cdd:smart00516   9 IPGGRGY-DKDGRPVLIERAGRFD----LKSVTLEELLRYLVYVLEKILQE-----EKKTGGIEGFTVIFDLKGLSMSN- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626331   374 wrPGIKALLNIIETVERNYPETMGRVLVVRAPRVFPIAWTIVSAFIDEHTRSKFLFYGPDCahmKDGLAQYLDEEIVPDF 453
Cdd:smart00516  78 --PDLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDS---KEELLEYIDKEQLPEE 152

                   ....*.
gi 442626331   454 LGGPCK 459
Cdd:smart00516 153 LGGTLD 158
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
294-456 5.69e-34

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: 127.07  E-value: 5.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626331 294 FPGGWHHLDKDGRPVYILRLGHmdvkGLLKSLGMDGLLRLALHICEEGIQKINESAERlekpvlnWSLLVDLEGLSMRHL 373
Cdd:cd00170   10 GIGYLGGRDKEGRPVLVFRAGW----DPPKLLDLEELLRYLVYLLEKALRELEEQVEG-------FVVIIDLKGFSLSNL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626331 374 WrpGIKALLNIIETVERNYPETMGRVLVVRAPRVFPIAWTIVSAFIDEHTRSKFLFYGPDcahmKDGLAQYLDEEIVPDF 453
Cdd:cd00170   79 S--DLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSD----LEELLEYIDPDQLPKE 152

                 ...
gi 442626331 454 LGG 456
Cdd:cd00170  153 LGG 155
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
222-268 4.31e-08

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 49.86  E-value: 4.31e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 442626331   222 ESKLLELRKMLDGVDDL-ERVPSYQTILRFLAARDWHVSQAYAMLCDS 268
Cdd:smart01100   1 EEALEELRELLEKHPDLlPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
CRAL_TRIO_N pfam03765
CRAL/TRIO, N-terminal domain; This all-alpha domain is found to the N-terminus of pfam00650.
246-267 2.53e-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: 39.18  E-value: 2.53e-04
                          10        20
                  ....*....|....*....|..
gi 442626331  246 TILRFLAARDWHVSQAYAMLCD 267
Cdd:pfam03765  32 CLLRFLRARKWDVEKAIKMLED 53
 
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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