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Conserved domains on  [gi|1834395698|ref|NP_001307604|]
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BCL2/adenovirus E1B 19 kDa protein-interacting protein 2 isoform 2 [Homo sapiens]

Protein Classification

SEC14 family lipid-binding protein( domain architecture ID 81984)

SEC14 family lipid-binding protein contains a lipid-binding domain that is found in secretory proteins and in lipid regulated proteins

CATH:  3.40.525.10
Gene Ontology:  GO:0008289
PubMed:  17428729
SCOP:  4003560

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
BNIP2 pfam12496
Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in ...
49-163 4.96e-53

Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in eukaryotes, and is typically between 119 and 133 amino acids in length. There is a conserved HGGY sequence motif. This family is Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2. It interacts with pro- and anti- apoptotic molecules in the cell.


:

Pssm-ID: 463609  Cd Length: 135  Bit Score: 170.26  E-value: 4.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834395698  49 VRKKLMAPDISLTLDPSDGSVLS-------DDLDESG--EIDLDGLDTPSE--------NSNEFEWEDDLPKPKTTEVIR 111
Cdd:pfam12496   1 KRKRLVAPELSLSLDQSEDSFLSaflspspDDFSDTDdlDINVDDLETPSDsdslefpeNGNELEWEDDLPRLGRGSGPS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1834395698 112 KG--SITEYTAAEEKED-GRRWRMFRIGEQDHRVDMKAIEPYKKVISHGGYYGDG 163
Cdd:pfam12496  81 EAaeSLPQYTAEDEVDDsGRRWRTFRIGEQEHRIDMKVIEPYKRVLSHGGYYGDG 135
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
147-295 3.49e-23

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: 93.52  E-value: 3.49e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834395698  147 IEPYKKVIShgGYYGDGLNAIVVFAVCFMPessQPNYRYLMDNLFKYVIGTLELLV---AENYMIVYLNGATTRRKMPS- 222
Cdd:smart00516   2 LELLKAYIP--GGRGYDKDGRPVLIERAGR---FDLKSVTLEELLRYLVYVLEKILqeeKKTGGIEGFTVIFDLKGLSMs 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834395698  223 ---LGWLRKCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLA--ELAELVPMEYvgIPEC 295
Cdd:smart00516  77 npdLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSkeELLEYIDKEQ--LPEE 152
 
Name Accession Description Interval E-value
BNIP2 pfam12496
Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in ...
49-163 4.96e-53

Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in eukaryotes, and is typically between 119 and 133 amino acids in length. There is a conserved HGGY sequence motif. This family is Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2. It interacts with pro- and anti- apoptotic molecules in the cell.


Pssm-ID: 463609  Cd Length: 135  Bit Score: 170.26  E-value: 4.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834395698  49 VRKKLMAPDISLTLDPSDGSVLS-------DDLDESG--EIDLDGLDTPSE--------NSNEFEWEDDLPKPKTTEVIR 111
Cdd:pfam12496   1 KRKRLVAPELSLSLDQSEDSFLSaflspspDDFSDTDdlDINVDDLETPSDsdslefpeNGNELEWEDDLPRLGRGSGPS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1834395698 112 KG--SITEYTAAEEKED-GRRWRMFRIGEQDHRVDMKAIEPYKKVISHGGYYGDG 163
Cdd:pfam12496  81 EAaeSLPQYTAEDEVDDsGRRWRTFRIGEQEHRIDMKVIEPYKRVLSHGGYYGDG 135
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
147-295 3.49e-23

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: 93.52  E-value: 3.49e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834395698  147 IEPYKKVIShgGYYGDGLNAIVVFAVCFMPessQPNYRYLMDNLFKYVIGTLELLV---AENYMIVYLNGATTRRKMPS- 222
Cdd:smart00516   2 LELLKAYIP--GGRGYDKDGRPVLIERAGR---FDLKSVTLEELLRYLVYVLEKILqeeKKTGGIEGFTVIFDLKGLSMs 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834395698  223 ---LGWLRKCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLA--ELAELVPMEYvgIPEC 295
Cdd:smart00516  77 npdLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSkeELLEYIDKEQ--LPEE 152
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
165-305 1.62e-20

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: 85.84  E-value: 1.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834395698 165 NAIVVFAVCFMPESSQPNYRYlmDNLFKYVIGTL-ELLVAENYMIVYLNGATTRRKMPSLGWLRKCYQQIDRRLRKNLKS 243
Cdd:pfam13716   2 RPVLVFISKLLPSRPASLDDL--DRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834395698 244 LIIVHPSWFIRTLLAVT-RPFISSKFSQKIRYVFNLAELAELVPmeyvgipecIKQVDQELNG 305
Cdd:pfam13716  80 VYVVHPSTFLRTFLKTLgSLLGSKKLRKKVHYVSSLSELWEGID---------REQLPTELPG 133
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
147-295 5.64e-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: 82.00  E-value: 5.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834395698 147 IEPYKKVISHGGYYG----DGlNAIVVFAVCFMPESsqpnyRYLMDNLFKYVIGTLELLVAENY-------MIVYLNGAT 215
Cdd:cd00170     1 LEELLELLGGIGYLGgrdkEG-RPVLVFRAGWDPPK-----LLDLEELLRYLVYLLEKALRELEeqvegfvVIIDLKGFS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834395698 216 TRrKMPSLGWLRKCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVF-NLAELAELVPMEYvgIPE 294
Cdd:cd00170    75 LS-NLSDLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsDLEELLEYIDPDQ--LPK 151

                  .
gi 1834395698 295 C 295
Cdd:cd00170   152 E 152
 
Name Accession Description Interval E-value
BNIP2 pfam12496
Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in ...
49-163 4.96e-53

Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in eukaryotes, and is typically between 119 and 133 amino acids in length. There is a conserved HGGY sequence motif. This family is Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2. It interacts with pro- and anti- apoptotic molecules in the cell.


Pssm-ID: 463609  Cd Length: 135  Bit Score: 170.26  E-value: 4.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834395698  49 VRKKLMAPDISLTLDPSDGSVLS-------DDLDESG--EIDLDGLDTPSE--------NSNEFEWEDDLPKPKTTEVIR 111
Cdd:pfam12496   1 KRKRLVAPELSLSLDQSEDSFLSaflspspDDFSDTDdlDINVDDLETPSDsdslefpeNGNELEWEDDLPRLGRGSGPS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1834395698 112 KG--SITEYTAAEEKED-GRRWRMFRIGEQDHRVDMKAIEPYKKVISHGGYYGDG 163
Cdd:pfam12496  81 EAaeSLPQYTAEDEVDDsGRRWRTFRIGEQEHRIDMKVIEPYKRVLSHGGYYGDG 135
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
147-295 3.49e-23

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: 93.52  E-value: 3.49e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834395698  147 IEPYKKVIShgGYYGDGLNAIVVFAVCFMPessQPNYRYLMDNLFKYVIGTLELLV---AENYMIVYLNGATTRRKMPS- 222
Cdd:smart00516   2 LELLKAYIP--GGRGYDKDGRPVLIERAGR---FDLKSVTLEELLRYLVYVLEKILqeeKKTGGIEGFTVIFDLKGLSMs 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834395698  223 ---LGWLRKCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLA--ELAELVPMEYvgIPEC 295
Cdd:smart00516  77 npdLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSkeELLEYIDKEQ--LPEE 152
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
165-305 1.62e-20

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: 85.84  E-value: 1.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834395698 165 NAIVVFAVCFMPESSQPNYRYlmDNLFKYVIGTL-ELLVAENYMIVYLNGATTRRKMPSLGWLRKCYQQIDRRLRKNLKS 243
Cdd:pfam13716   2 RPVLVFISKLLPSRPASLDDL--DRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834395698 244 LIIVHPSWFIRTLLAVT-RPFISSKFSQKIRYVFNLAELAELVPmeyvgipecIKQVDQELNG 305
Cdd:pfam13716  80 VYVVHPSTFLRTFLKTLgSLLGSKKLRKKVHYVSSLSELWEGID---------REQLPTELPG 133
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
147-295 5.64e-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: 82.00  E-value: 5.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834395698 147 IEPYKKVISHGGYYG----DGlNAIVVFAVCFMPESsqpnyRYLMDNLFKYVIGTLELLVAENY-------MIVYLNGAT 215
Cdd:cd00170     1 LEELLELLGGIGYLGgrdkEG-RPVLVFRAGWDPPK-----LLDLEELLRYLVYLLEKALRELEeqvegfvVIIDLKGFS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834395698 216 TRrKMPSLGWLRKCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVF-NLAELAELVPMEYvgIPE 294
Cdd:cd00170    75 LS-NLSDLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsDLEELLEYIDPDQ--LPK 151

                  .
gi 1834395698 295 C 295
Cdd:cd00170   152 E 152
CRAL_TRIO pfam00650
CRAL/TRIO domain;
187-290 1.03e-03

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 38.78  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834395698 187 MDNLFKYVIGTLELLVAENY--------MIVYLNGATTRrKMPSLGW--LRKCYQQIDRRLRKNLKSLIIVHPSWFIRTL 256
Cdd:pfam00650  31 EEELVRFLVLVLERALLLMPegqvegltVIIDLKGLSLS-NMDWWSIslLKKIIKILQDNYPERLGKILIVNAPWIFNTI 109
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1834395698 257 LAVTRPFISSKFSQKIRYVF--NLAELAELVPMEYV 290
Cdd:pfam00650 110 WKLIKPFLDPKTREKIVFLKnsNEEELEKYIPPEQL 145
 
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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