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Conserved domains on  [gi|1907194730|ref|XP_036010470|]
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BCL2/adenovirus E1B 19 kDa protein-interacting protein 2 isoform X3 [Mus musculus]

Protein Classification

SEC14 family lipid-binding protein( domain architecture ID 11271205)

SEC14 family lipid-binding protein contains a lipid-binding domain that is found in secretory proteins and in lipid regulated proteins; similar to Saccharomyces cerevisiae phosphatidylinositol transfer protein SFH5

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

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 ...
 16-164 1.97e-21

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: 86.20  E-value: 1.97e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194730   16 IEPYKKVIShgGYYGDGLNAIVVFAVCFMPesgQPNYRYLMDNLFKYVIGTLELLV---AENYMIIYLNGATTRRKMPS- 91
Cdd:smart00516   2 LELLKAYIP--GGRGYDKDGRPVLIERAGR---FDLKSVTLEELLRYLVYVLEKILqeeKKTGGIEGFTVIFDLKGLSMs 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907194730   92 ---LGWLRRCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLA--ELAELVPMEYvgIPEC 164
Cdd:smart00516  77 npdLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSkeELLEYIDKEQ--LPEE 152
 
Name Accession Description Interval E-value
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 16-164 1.97e-21

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: 86.20  E-value: 1.97e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194730   16 IEPYKKVIShgGYYGDGLNAIVVFAVCFMPesgQPNYRYLMDNLFKYVIGTLELLV---AENYMIIYLNGATTRRKMPS- 91
Cdd:smart00516   2 LELLKAYIP--GGRGYDKDGRPVLIERAGR---FDLKSVTLEELLRYLVYVLEKILqeeKKTGGIEGFTVIFDLKGLSMs 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907194730   92 ---LGWLRRCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLA--ELAELVPMEYvgIPEC 164
Cdd:smart00516  77 npdLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSkeELLEYIDKEQ--LPEE 152
BNIP2 pfam12496
Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in ...
 1-32 1.17e-20

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: 83.20  E-value: 1.17e-20
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907194730   1 MFRIGEQDHRVDMKAIEPYKKVISHGGYYGDG 32
Cdd:pfam12496 104 TFRIGEQEHRIDMKVIEPYKRVLSHGGYYGDG 135
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 16-159 4.57e-18

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: 76.99  E-value: 4.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194730  16 IEPYKKVISHGGYYG--DGLNAIVVFAVCFMPESGQPNyrylMDNLFKYVIGTLELLVAENY-------MIIYLNGATTR 86
Cdd:cd00170     1 LEELLELLGGIGYLGgrDKEGRPVLVFRAGWDPPKLLD----LEELLRYLVYLLEKALRELEeqvegfvVIIDLKGFSLS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907194730  87 rKMPSLGWLRRCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVF-NLAELAELVPMEYV 159
Cdd:cd00170    77 -NLSDLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsDLEELLEYIDPDQL 149
 
Name Accession Description Interval E-value
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 16-164 1.97e-21

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: 86.20  E-value: 1.97e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194730   16 IEPYKKVIShgGYYGDGLNAIVVFAVCFMPesgQPNYRYLMDNLFKYVIGTLELLV---AENYMIIYLNGATTRRKMPS- 91
Cdd:smart00516   2 LELLKAYIP--GGRGYDKDGRPVLIERAGR---FDLKSVTLEELLRYLVYVLEKILqeeKKTGGIEGFTVIFDLKGLSMs 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907194730   92 ---LGWLRRCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLA--ELAELVPMEYvgIPEC 164
Cdd:smart00516  77 npdLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSkeELLEYIDKEQ--LPEE 152
BNIP2 pfam12496
Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in ...
 1-32 1.17e-20

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: 83.20  E-value: 1.17e-20
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907194730   1 MFRIGEQDHRVDMKAIEPYKKVISHGGYYGDG 32
Cdd:pfam12496 104 TFRIGEQEHRIDMKVIEPYKRVLSHGGYYGDG 135
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 34-171 2.46e-18

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: 77.37  E-value: 2.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194730  34 NAIVVFAVCFMPESGQPNYRYlmDNLFKYVIGTL-ELLVAENYMIIYLNGATTRRKMPSLGWLRRCYQQIDRRLRKNLKS 112
Cdd:pfam13716   2 RPVLVFISKLLPSRPASLDDL--DRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907194730 113 LIIVHPSWFIRTLLAVT-RPFISSKFSQKIRYVFNLAELAELVPMEyvGIPECIK---QYEEE 171
Cdd:pfam13716  80 VYVVHPSTFLRTFLKTLgSLLGSKKLRKKVHYVSSLSELWEGIDRE--QLPTELPgvlSYDEE 140
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 16-159 4.57e-18

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: 76.99  E-value: 4.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194730  16 IEPYKKVISHGGYYG--DGLNAIVVFAVCFMPESGQPNyrylMDNLFKYVIGTLELLVAENY-------MIIYLNGATTR 86
Cdd:cd00170     1 LEELLELLGGIGYLGgrDKEGRPVLVFRAGWDPPKLLD----LEELLRYLVYLLEKALRELEeqvegfvVIIDLKGFSLS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907194730  87 rKMPSLGWLRRCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVF-NLAELAELVPMEYV 159
Cdd:cd00170    77 -NLSDLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsDLEELLEYIDPDQL 149
CRAL_TRIO pfam00650
CRAL/TRIO domain;
56-159 1.80e-03

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 37.24  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194730  56 MDNLFKYVIGTLELLVAENY--------MIIYLNGATTRrKMPSLGW--LRRCYQQIDRRLRKNLKSLIIVHPSWFIRTL 125
Cdd:pfam00650  31 EEELVRFLVLVLERALLLMPegqvegltVIIDLKGLSLS-NMDWWSIslLKKIIKILQDNYPERLGKILIVNAPWIFNTI 109

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907194730 126 LAVTRPFISSKFSQKIRYVF--NLAELAELVPMEYV 159
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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