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Conserved domains on  [gi|1720403289|ref|XP_030108308|]
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bcl-2/adenovirus E1B 19 kDa-interacting protein 2-like protein isoform X1 [Mus musculus]

Protein Classification

BNIP2 family protein( domain architecture ID 10575844)

BNIP2 (Bcl-2/adenovirus E1B 19 kDa-interacting protein 2) family protein containing a Sec14p-like lipid-binding domain, similar to human caytaxin (or BNIP-H) that functions in the development of neural tissues, particularly the postnatal maturation of the cerebellar cortex

Graphical summary

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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 ...
50-178 3.50e-54

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: 173.34  E-value: 3.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403289  50 MRKRLSAPEWQLSLTEGTGE--NGASPTRSASSSSAGSLDLEVDELETPSDSEQLD---SGHEFEWEDDLPR-AEGLGAS 123
Cdd:pfam12496   1 KRKRLVAPELSLSLDQSEDSflSAFLSPSPDDFSDTDDLDINVDDLETPSDSDSLEfpeNGNELEWEDDLPRlGRGSGPS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720403289 124 EAAERLGRGCVCDVAGEDGHRWRVFRTGQREQRVDMTIIEPYKKVLSHGGYHGDG 178
Cdd:pfam12496  81 EAAESLPQYTAEDEVDDSGRRWRTFRIGEQEHRIDMKVIEPYKRVLSHGGYYGDG 135
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
180-317 8.02e-26

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: 100.09  E-value: 8.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403289 180 NAVILFASCYLPRSSIPNYTYimEHLFRYMVGTL-ELLVAENYLLVHLSGGTSRAQVPPLSWIRQCYRTLDRRLRKNLRA 258
Cdd:pfam13716   2 RPVLVFISKLLPSRPASLDDL--DRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720403289 259 LVVVHATWYVKAFLA-LVRPFISSKFTRKIRFLDSLGELAQLISLEQV--HIPEVVrQLDRD 317
Cdd:pfam13716  80 VYVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLptELPGVL-SYDEE 140
 
Name Accession Description Interval E-value
BNIP2 pfam12496
Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in ...
50-178 3.50e-54

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: 173.34  E-value: 3.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403289  50 MRKRLSAPEWQLSLTEGTGE--NGASPTRSASSSSAGSLDLEVDELETPSDSEQLD---SGHEFEWEDDLPR-AEGLGAS 123
Cdd:pfam12496   1 KRKRLVAPELSLSLDQSEDSflSAFLSPSPDDFSDTDDLDINVDDLETPSDSDSLEfpeNGNELEWEDDLPRlGRGSGPS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720403289 124 EAAERLGRGCVCDVAGEDGHRWRVFRTGQREQRVDMTIIEPYKKVLSHGGYHGDG 178
Cdd:pfam12496  81 EAAESLPQYTAEDEVDDSGRRWRTFRIGEQEHRIDMKVIEPYKRVLSHGGYYGDG 135
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
180-317 8.02e-26

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: 100.09  E-value: 8.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403289 180 NAVILFASCYLPRSSIPNYTYimEHLFRYMVGTL-ELLVAENYLLVHLSGGTSRAQVPPLSWIRQCYRTLDRRLRKNLRA 258
Cdd:pfam13716   2 RPVLVFISKLLPSRPASLDDL--DRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720403289 259 LVVVHATWYVKAFLA-LVRPFISSKFTRKIRFLDSLGELAQLISLEQV--HIPEVVrQLDRD 317
Cdd:pfam13716  80 VYVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLptELPGVL-SYDEE 140
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
162-308 1.78e-23

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: 94.32  E-value: 1.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403289 162 IEPYKKVLSHGGYHG----DGlNAVILFASCYLPRSSIPnytyiMEHLFRYMVGTLELLVAENY------LLVHLSGGTS 231
Cdd:cd00170     1 LEELLELLGGIGYLGgrdkEG-RPVLVFRAGWDPPKLLD-----LEELLRYLVYLLEKALRELEeqvegfVVIIDLKGFS 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720403289 232 RAQVPPLSWIRQCYRTLDRRLRKNLRALVVVHATWYVKAFLALVRPFISSKFTRKIRFLDS-LGELAQLISLEQVHIP 308
Cdd:cd00170    75 LSNLSDLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSdLEELLEYIDPDQLPKE 152
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
162-309 2.71e-19

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: 83.12  E-value: 2.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403289  162 IEPYKKVLShGGYHGDGLNAVILFASCYLprssIPNYTYIMEHLFRYMVGTLELLVAENYLLVHLSG--------GTSRA 233
Cdd:smart00516   2 LELLKAYIP-GGRGYDKDGRPVLIERAGR----FDLKSVTLEELLRYLVYVLEKILQEEKKTGGIEGftvifdlkGLSMS 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720403289  234 QvPPLSWIRQCYRTLDRRLRKNLRALVVVHATWYVKAFLALVRPFISSKFTRKIRFL--DSLGELAQLISLEQvhIPE 309
Cdd:smart00516  77 N-PDLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVgnDSKEELLEYIDKEQ--LPE 151
 
Name Accession Description Interval E-value
BNIP2 pfam12496
Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in ...
50-178 3.50e-54

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: 173.34  E-value: 3.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403289  50 MRKRLSAPEWQLSLTEGTGE--NGASPTRSASSSSAGSLDLEVDELETPSDSEQLD---SGHEFEWEDDLPR-AEGLGAS 123
Cdd:pfam12496   1 KRKRLVAPELSLSLDQSEDSflSAFLSPSPDDFSDTDDLDINVDDLETPSDSDSLEfpeNGNELEWEDDLPRlGRGSGPS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720403289 124 EAAERLGRGCVCDVAGEDGHRWRVFRTGQREQRVDMTIIEPYKKVLSHGGYHGDG 178
Cdd:pfam12496  81 EAAESLPQYTAEDEVDDSGRRWRTFRIGEQEHRIDMKVIEPYKRVLSHGGYYGDG 135
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
180-317 8.02e-26

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: 100.09  E-value: 8.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403289 180 NAVILFASCYLPRSSIPNYTYimEHLFRYMVGTL-ELLVAENYLLVHLSGGTSRAQVPPLSWIRQCYRTLDRRLRKNLRA 258
Cdd:pfam13716   2 RPVLVFISKLLPSRPASLDDL--DRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720403289 259 LVVVHATWYVKAFLA-LVRPFISSKFTRKIRFLDSLGELAQLISLEQV--HIPEVVrQLDRD 317
Cdd:pfam13716  80 VYVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLptELPGVL-SYDEE 140
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
162-308 1.78e-23

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: 94.32  E-value: 1.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403289 162 IEPYKKVLSHGGYHG----DGlNAVILFASCYLPRSSIPnytyiMEHLFRYMVGTLELLVAENY------LLVHLSGGTS 231
Cdd:cd00170     1 LEELLELLGGIGYLGgrdkEG-RPVLVFRAGWDPPKLLD-----LEELLRYLVYLLEKALRELEeqvegfVVIIDLKGFS 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720403289 232 RAQVPPLSWIRQCYRTLDRRLRKNLRALVVVHATWYVKAFLALVRPFISSKFTRKIRFLDS-LGELAQLISLEQVHIP 308
Cdd:cd00170    75 LSNLSDLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSdLEELLEYIDPDQLPKE 152
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
162-309 2.71e-19

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: 83.12  E-value: 2.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403289  162 IEPYKKVLShGGYHGDGLNAVILFASCYLprssIPNYTYIMEHLFRYMVGTLELLVAENYLLVHLSG--------GTSRA 233
Cdd:smart00516   2 LELLKAYIP-GGRGYDKDGRPVLIERAGR----FDLKSVTLEELLRYLVYVLEKILQEEKKTGGIEGftvifdlkGLSMS 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720403289  234 QvPPLSWIRQCYRTLDRRLRKNLRALVVVHATWYVKAFLALVRPFISSKFTRKIRFL--DSLGELAQLISLEQvhIPE 309
Cdd:smart00516  77 N-PDLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVgnDSKEELLEYIDKEQ--LPE 151
CRAL_TRIO pfam00650
CRAL/TRIO domain;
202-305 1.01e-07

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 50.72  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403289 202 MEHLFRYMVGTLELLVAENY--------LLVHLSG-GTSRAQVPPLSWIRQCYRTLDRRLRKNLRALVVVHATWYVKAFL 272
Cdd:pfam00650  31 EEELVRFLVLVLERALLLMPegqvegltVIIDLKGlSLSNMDWWSISLLKKIIKILQDNYPERLGKILIVNAPWIFNTIW 110
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1720403289 273 ALVRPFISSKFTRKIRFLDS--LGELAQLISLEQV 305
Cdd:pfam00650 111 KLIKPFLDPKTREKIVFLKNsnEEELEKYIPPEQL 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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