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Conserved domains on  [gi|1676319525|ref|NP_002994|]
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SEC14-like protein 1 isoform a [Homo sapiens]

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 4.48e-67

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: 217.55  E-value: 4.48e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319525  17 ELIMAAYERRFPTcPLIPMFVGSDTVNEFKSEDGAIHViERRCKLDVDAPRLLKKIAGV-DYVYFVQKNSLNSRERTLHI 95
Cdd:pfam04707   1 EQVTAAFWRRYPN-PYSPHVISVDVLERELDDDGKLHT-ERLLTKQGRLPRWLKKLIGVaHTVYVVEVSVVDPKKRTLTL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1676319525  96 EAYNETFSNRVIINEHCCYTVHPENEDWTCFEQSASLDIKSFFGFESTVEKIAMKQYTSNIKKGKEIIEYYLRQLEEE 173
Cdd:pfam04707  79 ETRNLTFSNRLSVDERCRYTPHPENPNWTIFDQEASISISGFFGFSSKVEKWSLKRFSQNAKKGREGMEYVLQKLEEE 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
326-489 2.07e-39

CRAL/TRIO domain;


:

Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 142.40  E-value: 2.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319525 326 YYAGGWHHHDKDGRPLYVLRLGQMDTKglvrALGEEALLRYVLSINEEGLRRCEEntkvfgRPISSWTCLVDLEGLNMRH 405
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLGRHDPK----KSSEEELVRFLVLVLERALLLMPE------GQVEGLTVIIDLKGLSLSN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319525 406 LWRPGVKALLRIIEVVEANYPETLGRLLILRAPRVFPVLWTLVSPFIDDNTRRKFLIYAGNDYQgpgGLLDYIDKEIIPD 485
Cdd:pfam00650  71 MDWWSISLLKKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKNSNEE---ELEKYIPPEQLPK 147

                  ....
gi 1676319525 486 FLSG 489
Cdd:pfam00650 148 EYGG 151
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
256-301 1.01e-09

CRAL/TRIO, N-terminal domain;


:

Pssm-ID: 215024  Cd Length: 48  Bit Score: 54.48  E-value: 1.01e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1676319525  256 ESCLIRLRQWLQETHKGKIPK--DEHILRFLRARDFNIDKAREIMCQS 301
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 4.48e-67

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: 217.55  E-value: 4.48e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319525  17 ELIMAAYERRFPTcPLIPMFVGSDTVNEFKSEDGAIHViERRCKLDVDAPRLLKKIAGV-DYVYFVQKNSLNSRERTLHI 95
Cdd:pfam04707   1 EQVTAAFWRRYPN-PYSPHVISVDVLERELDDDGKLHT-ERLLTKQGRLPRWLKKLIGVaHTVYVVEVSVVDPKKRTLTL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1676319525  96 EAYNETFSNRVIINEHCCYTVHPENEDWTCFEQSASLDIKSFFGFESTVEKIAMKQYTSNIKKGKEIIEYYLRQLEEE 173
Cdd:pfam04707  79 ETRNLTFSNRLSVDERCRYTPHPENPNWTIFDQEASISISGFFGFSSKVEKWSLKRFSQNAKKGREGMEYVLQKLEEE 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
326-489 2.07e-39

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 142.40  E-value: 2.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319525 326 YYAGGWHHHDKDGRPLYVLRLGQMDTKglvrALGEEALLRYVLSINEEGLRRCEEntkvfgRPISSWTCLVDLEGLNMRH 405
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLGRHDPK----KSSEEELVRFLVLVLERALLLMPE------GQVEGLTVIIDLKGLSLSN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319525 406 LWRPGVKALLRIIEVVEANYPETLGRLLILRAPRVFPVLWTLVSPFIDDNTRRKFLIYAGNDYQgpgGLLDYIDKEIIPD 485
Cdd:pfam00650  71 MDWWSISLLKKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKNSNEE---ELEKYIPPEQLPK 147

                  ....
gi 1676319525 486 FLSG 489
Cdd:pfam00650 148 EYGG 151
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
319-491 2.01e-36

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: 134.35  E-value: 2.01e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319525  319 PPQVLQDYYAGGWHHhDKDGRPLYVLRLGQMDtkglVRALGEEALLRYVLSINEEGLRRceentKVFGRPISSWTCLVDL 398
Cdd:smart00516   1 ELELLKAYIPGGRGY-DKDGRPVLIERAGRFD----LKSVTLEELLRYLVYVLEKILQE-----EKKTGGIEGFTVIFDL 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319525  399 EGLNMRHlwrPGVKALLRIIEVVEANYPETLGRLLILRAPRVFPVLWTLVSPFIDDNTRRKFLIyAGNDYQgpGGLLDYI 478
Cdd:smart00516  71 KGLSMSN---PDLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRF-VGNDSK--EELLEYI 144
                          170
                   ....*....|...
gi 1676319525  479 DKEIIPDFLSGEC 491
Cdd:smart00516 145 DKEQLPEELGGTL 157
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
325-490 8.22e-36

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: 132.46  E-value: 8.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319525 325 DYYAGGWHHHDKDGRPLYVLRLGQMDTKglvrALGEEALLRYVLSINEEGLRRCEEntkvfgrPISSWTCLVDLEGLNMR 404
Cdd:cd00170     8 LGGIGYLGGRDKEGRPVLVFRAGWDPPK----LLDLEELLRYLVYLLEKALRELEE-------QVEGFVVIIDLKGFSLS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319525 405 HLWrpGVKALLRIIEVVEANYPETLGRLLILRAPRVFPVLWTLVSPFIDDNTRRKFLIYAGNdyqgPGGLLDYIDKEIIP 484
Cdd:cd00170    77 NLS--DLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSD----LEELLEYIDPDQLP 150

                  ....*.
gi 1676319525 485 DFLSGE 490
Cdd:cd00170   151 KELGGT 156
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
256-301 1.01e-09

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 54.48  E-value: 1.01e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1676319525  256 ESCLIRLRQWLQETHKGKIPK--DEHILRFLRARDFNIDKAREIMCQS 301
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.
262-296 2.50e-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: 2.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1676319525 262 LRQWLQETHKGKIPK----------DEHILRFLRARDFNIDKARE 296
Cdd:pfam03765   5 LLELLKDEDEETDREkfwltredhdDVCLLRFLRARKWDVEKAIK 49
 
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 4.48e-67

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: 217.55  E-value: 4.48e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319525  17 ELIMAAYERRFPTcPLIPMFVGSDTVNEFKSEDGAIHViERRCKLDVDAPRLLKKIAGV-DYVYFVQKNSLNSRERTLHI 95
Cdd:pfam04707   1 EQVTAAFWRRYPN-PYSPHVISVDVLERELDDDGKLHT-ERLLTKQGRLPRWLKKLIGVaHTVYVVEVSVVDPKKRTLTL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1676319525  96 EAYNETFSNRVIINEHCCYTVHPENEDWTCFEQSASLDIKSFFGFESTVEKIAMKQYTSNIKKGKEIIEYYLRQLEEE 173
Cdd:pfam04707  79 ETRNLTFSNRLSVDERCRYTPHPENPNWTIFDQEASISISGFFGFSSKVEKWSLKRFSQNAKKGREGMEYVLQKLEEE 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
326-489 2.07e-39

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 142.40  E-value: 2.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319525 326 YYAGGWHHHDKDGRPLYVLRLGQMDTKglvrALGEEALLRYVLSINEEGLRRCEEntkvfgRPISSWTCLVDLEGLNMRH 405
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLGRHDPK----KSSEEELVRFLVLVLERALLLMPE------GQVEGLTVIIDLKGLSLSN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319525 406 LWRPGVKALLRIIEVVEANYPETLGRLLILRAPRVFPVLWTLVSPFIDDNTRRKFLIYAGNDYQgpgGLLDYIDKEIIPD 485
Cdd:pfam00650  71 MDWWSISLLKKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKNSNEE---ELEKYIPPEQLPK 147

                  ....
gi 1676319525 486 FLSG 489
Cdd:pfam00650 148 EYGG 151
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
319-491 2.01e-36

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: 134.35  E-value: 2.01e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319525  319 PPQVLQDYYAGGWHHhDKDGRPLYVLRLGQMDtkglVRALGEEALLRYVLSINEEGLRRceentKVFGRPISSWTCLVDL 398
Cdd:smart00516   1 ELELLKAYIPGGRGY-DKDGRPVLIERAGRFD----LKSVTLEELLRYLVYVLEKILQE-----EKKTGGIEGFTVIFDL 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319525  399 EGLNMRHlwrPGVKALLRIIEVVEANYPETLGRLLILRAPRVFPVLWTLVSPFIDDNTRRKFLIyAGNDYQgpGGLLDYI 478
Cdd:smart00516  71 KGLSMSN---PDLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRF-VGNDSK--EELLEYI 144
                          170
                   ....*....|...
gi 1676319525  479 DKEIIPDFLSGEC 491
Cdd:smart00516 145 DKEQLPEELGGTL 157
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
325-490 8.22e-36

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: 132.46  E-value: 8.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319525 325 DYYAGGWHHHDKDGRPLYVLRLGQMDTKglvrALGEEALLRYVLSINEEGLRRCEEntkvfgrPISSWTCLVDLEGLNMR 404
Cdd:cd00170     8 LGGIGYLGGRDKEGRPVLVFRAGWDPPK----LLDLEELLRYLVYLLEKALRELEE-------QVEGFVVIIDLKGFSLS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319525 405 HLWrpGVKALLRIIEVVEANYPETLGRLLILRAPRVFPVLWTLVSPFIDDNTRRKFLIYAGNdyqgPGGLLDYIDKEIIP 484
Cdd:cd00170    77 NLS--DLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSD----LEELLEYIDPDQLP 150

                  ....*.
gi 1676319525 485 DFLSGE 490
Cdd:cd00170   151 KELGGT 156
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
256-301 1.01e-09

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 54.48  E-value: 1.01e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1676319525  256 ESCLIRLRQWLQETHKGKIPK--DEHILRFLRARDFNIDKAREIMCQS 301
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.
262-296 2.50e-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: 2.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1676319525 262 LRQWLQETHKGKIPK----------DEHILRFLRARDFNIDKARE 296
Cdd:pfam03765   5 LLELLKDEDEETDREkfwltredhdDVCLLRFLRARKWDVEKAIK 49
 
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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